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Conserved domains on  [gi|665410160|ref|NP_001287009|]
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laminin B2, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 61-296 2.06e-113

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


:

Pssm-ID: 214532  Cd Length: 238  Bit Score: 358.21  E-value: 2.06e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160     61 YGRPQKCLPEFINAAYQLQIESTNTCGEQNDNHFCIQT-MNQNHKNCEFCKYND----HNPSFLTDLHDPQSPTWWQSET 135
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVgHTEQGKKCDYCDARNprrsHPAENLTDGNNPNNPTWWQSEP 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    136 MFEGIQhpnYVNLTLHLGKSYDITYVRILFRSPRPeSFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRAIRKGeGEAH 215
Cdd:smart00136   81 LSNGPQ---NVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    216 ALCTSEYSDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDS-QVLKSYFYAISDIA 294
Cdd:smart00136  156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRpEVTRRYYYAISDIA 235


                    ..
gi 665410160    295 VG 296
Cdd:smart00136  236 VG 237
LamB smart00281
Laminin B domain;
572-697 5.26e-41

Laminin B domain;


:

Pssm-ID: 214597  Cd Length: 127  Bit Score: 147.41  E-value: 5.26e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    572 GNEHVYFQAPDRFLGDQRASYNRDLKFKLQLVGQVANTGVS--DVILEGAGSRISLPifAQGNGIPDQGVK-EYTFRLHE 648
Cdd:smart00281    1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapDVILEGNGLRISHP--AEGPPLPDELTTvEVRFREEN 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 665410160    649 HHDYQWQPSQSARgFLSILSNLTAIKIRATYSVQGEAI-LDDVELQTAHR 697
Cdd:smart00281   79 WQYYGGRPVTRED-LMMVLANLTAILIRATYSQQMAGSrLSDVSLEVAVP 127
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1054-1621 1.21e-25

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: 115.92  E-value: 1.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1054 YNLVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEFEAKLKAVQEkvavlaQDARDNSGDGGQTYAEvIDDLHKHLDSVR 1133
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE------AELKELQAELEELEEE-LEELQEELERLE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1134 EHLVSADKFQADANGEIDRARQNYTILDQITEnAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARAL 1213
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1214 ADKLESEAQFDL-KNAKDAKDAVE--------KAHQLAKSAID------LQLKIGTELRSEVGLELSHVKQS-------- 1270
Cdd:TIGR02168  540 EAALGGRLQAVVvENLNAAKKAIAflkqnelgRVTFLPLDSIKgteiqgNDREILKNIEGFLGVAKDLVKFDpklrkals 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1271 --LGT--VVQTSKEALRKANE---------------------VYDTALTLLNDVNRQtqpeIDISQLKKDAVAANERADE 1325
Cdd:TIGR02168  620 ylLGGvlVVDDLDNALELAKKlrpgyrivtldgdlvrpggviTGGSAKTNSSILERR----REIEELEEKIEELEEKIAE 695

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1326 LLKQITELSNSNGELfadfETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANntyEKLAGFQS 1405
Cdd:TIGR02168  696 LEKALAELRKELEEL----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE---AEIEELEE 768

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1406 DVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYaEQASKDAELIRRKANETKVAA 1485
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-ESLERRIAATERRLEDLEEQI 847

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1486 RNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDIntgd 1565
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK---- 923

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160  1566 LDRLENRLATVEGEINrvNLTGRI-EKYR-EQRTIQKN------LIDKYDAELRELKDEVQNIG 1621
Cdd:TIGR02168  924 LAQLELRLEGLEVRID--NLQERLsEEYSlTLEEAEALenkiedDEEEARRRLKRLENKIKELG 985
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
956-1001 1.27e-14

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.27e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160    956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSSEGC 1001
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 743-791 4.89e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 4.89e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  743 PCDCHGHADI---CDSETGRCICQHNTHGDNCDQCAKGFYGNALggTPNDCK 791
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS--QGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 461-511 1.33e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.53  E-value: 1.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410160   461 CGCDSGGSHqnTPACDTETGICFCKENVEGRRCNECKPGFFNLDKNNRFGC 511
Cdd:pfam00053    1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
414-458 9.44e-12

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.17  E-value: 9.44e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160    414 CACDPVGSRSLQCNS-HGKCQCKPGVTGDKCDRCDNNYYQFGPHGC 458
Cdd:smart00180    1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 902-953 1.74e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.44  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665410160   902 CSCYEAGTEQDeqsitRCDQVTGQCQCKPNVIGRDCGECQPGYFNIRSGNGC 953
Cdd:pfam00053    1 CDCNPHGSLSD-----TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 847-897 7.25e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 58.90  E-value: 7.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410160   847 CDCNGNVDPNavGNCNRTTGECLkCIHNTAGEHCDQCLSGHFGDPLALPHG 897
Cdd:pfam00053    1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1004-1046 4.30e-10

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 4.30e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 665410160  1004 CECDESGSKGFQCDQN-GQCPCNDNVEGRRCDRCKENKYDRHRG 1046
Cdd:pfam00053    1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 298-347 1.10e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.66  E-value: 1.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665410160  298 RCKCNGHASK---CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYNDLKWKR 347
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTG-------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 359-414 2.15e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160   359 CNCNGLA---DKCFFdanlfnrtgHGGHCLdCRENRDGPNCERCKENFYMRDDGYCVNC 414
Cdd:pfam00053    1 CDCNPHGslsDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
793-836 2.24e-03

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.24e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 665410160    793 CPCPNDGA----ClqiNEDTVICtECPKGYFGSRCEQCSDGFFGDPTG 836
Cdd:smart00180    1 CDCDPGGSasgtC---DPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPP 44
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 61-296 2.06e-113

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


Pssm-ID: 214532  Cd Length: 238  Bit Score: 358.21  E-value: 2.06e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160     61 YGRPQKCLPEFINAAYQLQIESTNTCGEQNDNHFCIQT-MNQNHKNCEFCKYND----HNPSFLTDLHDPQSPTWWQSET 135
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVgHTEQGKKCDYCDARNprrsHPAENLTDGNNPNNPTWWQSEP 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    136 MFEGIQhpnYVNLTLHLGKSYDITYVRILFRSPRPeSFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRAIRKGeGEAH 215
Cdd:smart00136   81 LSNGPQ---NVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    216 ALCTSEYSDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDS-QVLKSYFYAISDIA 294
Cdd:smart00136  156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRpEVTRRYYYAISDIA 235


                    ..
gi 665410160    295 VG 296
Cdd:smart00136  236 VG 237
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
67-297 7.35e-104

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 331.08  E-value: 7.35e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    67 CLPEFINAAYQLQIESTNTCGEQNDNHFCIQTMNQNHKNCEFC----KYNDHNPSFLTDLHDPQSPTWWQSETMFEgiqH 142
Cdd:pfam00055    1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGKKCFICdsrdPHNSHPPSNLTDSNNGTNETWWQSETGVI---Q 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   143 PNYVNLTLHLGKSYDITYVRILFRSPRPESFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRaiRKGEGEAHALCTSEY 222
Cdd:pfam00055   78 YENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGP--SRGIKDDEVICTSEY 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410160   223 SDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDSQVLKSYFYAISDIAVGA 297
Cdd:pfam00055  156 SDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
LamB smart00281
Laminin B domain;
572-697 5.26e-41

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 147.41  E-value: 5.26e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    572 GNEHVYFQAPDRFLGDQRASYNRDLKFKLQLVGQVANTGVS--DVILEGAGSRISLPifAQGNGIPDQGVK-EYTFRLHE 648
Cdd:smart00281    1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapDVILEGNGLRISHP--AEGPPLPDELTTvEVRFREEN 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 665410160    649 HHDYQWQPSQSARgFLSILSNLTAIKIRATYSVQGEAI-LDDVELQTAHR 697
Cdd:smart00281   79 WQYYGGRPVTRED-LMMVLANLTAILIRATYSQQMAGSrLSDVSLEVAVP 127
Laminin_B pfam00052
Laminin B (Domain IV);
577-708 9.05e-36

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 132.78  E-value: 9.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   577 YFQAPDRFLGDQRASYNRDLKFKLQ---LVGQVANTGVSDVILEGAGSRISLPIFAQGNGIPDQGvKEYTFRLHEHHdyq 653
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRyepLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQE-QTYSVRLHEEN--- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   654 WQPSQ----SARGFLSILSNLTAIKIRATYSV-QGEAILDDVELQTAHRGAAGHPATWIE 708
Cdd:pfam00052   77 WRDSDgapvSREDFMMVLANLTAILIRATYSTgSGQVSLSNVSLDSAVPGGSGPPASWVE 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1054-1621 1.21e-25

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: 115.92  E-value: 1.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1054 YNLVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEFEAKLKAVQEkvavlaQDARDNSGDGGQTYAEvIDDLHKHLDSVR 1133
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE------AELKELQAELEELEEE-LEELQEELERLE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1134 EHLVSADKFQADANGEIDRARQNYTILDQITEnAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARAL 1213
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1214 ADKLESEAQFDL-KNAKDAKDAVE--------KAHQLAKSAID------LQLKIGTELRSEVGLELSHVKQS-------- 1270
Cdd:TIGR02168  540 EAALGGRLQAVVvENLNAAKKAIAflkqnelgRVTFLPLDSIKgteiqgNDREILKNIEGFLGVAKDLVKFDpklrkals 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1271 --LGT--VVQTSKEALRKANE---------------------VYDTALTLLNDVNRQtqpeIDISQLKKDAVAANERADE 1325
Cdd:TIGR02168  620 ylLGGvlVVDDLDNALELAKKlrpgyrivtldgdlvrpggviTGGSAKTNSSILERR----REIEELEEKIEELEEKIAE 695

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1326 LLKQITELSNSNGELfadfETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANntyEKLAGFQS 1405
Cdd:TIGR02168  696 LEKALAELRKELEEL----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE---AEIEELEE 768

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1406 DVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYaEQASKDAELIRRKANETKVAA 1485
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-ESLERRIAATERRLEDLEEQI 847

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1486 RNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDIntgd 1565
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK---- 923

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160  1566 LDRLENRLATVEGEINrvNLTGRI-EKYR-EQRTIQKN------LIDKYDAELRELKDEVQNIG 1621
Cdd:TIGR02168  924 LAQLELRLEGLEVRID--NLQERLsEEYSlTLEEAEALenkiedDEEEARRRLKRLENKIKELG 985
PTZ00121 PTZ00121
MAEBL; Provisional
 1165-1615 2.07e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 89.04  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1165 ENAKKeLQQALDLLNDEGAQALARAKE-KSVEFGQQSEQISDIsREARALADKLESEAqfdLKNAKDAKDAVEKAHQLAK 1243
Cdd:PTZ00121 1173 EDAKK-AEAARKAEEVRKAEELRKAEDaRKAEAARKAEEERKA-EEARKAEDAKKAEA---VKKAEEAKKDAEEAKKAEE 1247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1244 saidlqLKIGTELRSEVGLELSHVKQSLGTVvqtSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAAnERA 1323
Cdd:PTZ00121 1248 ------ERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA-KKA 1317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1324 DELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKlagf 1403
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA---- 1393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1404 qSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEAldganKNANEAKKNAQEAqlKYAEQASKDAELiRRKANETKV 1483
Cdd:PTZ00121 1394 -DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-----KKADEAKKKAEEA--KKADEAKKKAEE-AKKAEEAKK 1464

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1484 AARNLR--EEADQLNHRVKLTEMDIFKLEESSTKDDNLvddakRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDI 1561
Cdd:PTZ00121 1465 KAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665410160 1562 NTGDLDRLENRLATVEgEINRVNLTGRIEKYREQRTiQKNLIDKYDAELRELKD 1615
Cdd:PTZ00121 1540 KKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEE 1591
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1279-1622 4.80e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.22  E-value: 4.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1279 KEALRKANEVyDTALTLLND----VNRQtqpeidISQLKKDAVAAnERADELLKQITELSnsnGELFA----DFETEQEL 1350
Cdd:COG1196   175 EEAERKLEAT-EENLERLEDilgeLERQ------LEPLERQAEKA-ERYRELKEELKELE---AELLLlklrELEAELEE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1351 TEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTY----EKLAGFQSDVQRSSESAEKALQTVPNIEK 1426
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1427 EIQNAESLISQAEEALDGANKNANEAKK--NAQEAQLKYAEQASKDAELIRRKANETKVAARN--LREEADQLNHRVKLT 1502
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEelEEAEAELAEAEEALLEAEAELAEAEEELEELAEelLEALRAAAELAAQLE 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1503 EmdifkLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINR 1582
Cdd:COG1196   404 E-----LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 665410160 1583 VN-LTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGL 1622
Cdd:COG1196   479 LAeLLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
956-1001 1.27e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.27e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160    956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSSEGC 1001
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 956-1004 2.12e-14

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 68.92  E-value: 2.12e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665410160   956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSSEGCKPC 1004
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 743-791 4.89e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 4.89e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  743 PCDCHGHADI---CDSETGRCICQHNTHGDNCDQCAKGFYGNALggTPNDCK 791
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS--QGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 956-1002 9.14e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 64.30  E-value: 9.14e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665410160  956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSS--EGCK 1002
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 461-511 1.33e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.53  E-value: 1.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410160   461 CGCDSGGSHqnTPACDTETGICFCKENVEGRRCNECKPGFFNLDKNNRFGC 511
Cdd:pfam00053    1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 744-790 2.13e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.14  E-value: 2.13e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 665410160   744 CDCHGHA---DICDSETGRCICQHNTHGDNCDQCAKGFYGNAlGGTPNDC 790
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
414-458 9.44e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.17  E-value: 9.44e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160    414 CACDPVGSRSLQCNS-HGKCQCKPGVTGDKCDRCDNNYYQFGPHGC 458
Cdd:smart00180    1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 902-953 1.74e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.44  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665410160   902 CSCYEAGTEQDeqsitRCDQVTGQCQCKPNVIGRDCGECQPGYFNIRSGNGC 953
Cdd:pfam00053    1 CDCNPHGSLSD-----TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 414-459 2.08e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 60.45  E-value: 2.08e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665410160  414 CACDPVGSRSLQCNSH-GKCQCKPGVTGDKCDRCDNNYYQF--GPHGCQ 459
Cdd:cd00055     2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 414-461 2.11e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.06  E-value: 2.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665410160   414 CACDPVGSRSLQCNSH-GKCQCKPGVTGDKCDRCDNNYYQFGPHGCQQC 461
Cdd:pfam00053    1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1091-1618 3.54e-11

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: 68.61  E-value: 3.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1091 AKLKAVQEKVAVLAQDARDNSGdggqTYAEVIDDLHKHLDSVREHLVSADKFQAD-----------ANGEIDRARQNYTI 1159
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNS----MYMRQLSDLESTVSQLRSELREAKRMYEDkieelekqlvlANSELTEARTERDQ 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1160 LDQITENAKKELQQALdllndegAQALARAKEKSVEfGQQSEQISDISREARALADKLESEaqFDLKNAKdakdaVEKAH 1239
Cdd:pfam15921  368 FSQESGNLDDQLQKLL-------ADLHKREKELSLE-KEQNKRLWDRDTGNSITIDHLRRE--LDDRNME-----VQRLE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1240 QLAKS-AIDLQLKIGTELRSEVGLELSHVK-QSLGTVVQTSKEALRKA-NEVYDTALTLLNdvNRQTQPEIDIS-QLKKD 1315
Cdd:pfam15921  433 ALLKAmKSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKEMLRKVvEELTAKKMTLES--SERTVSDLTASlQEKER 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1316 AVAAN--------ERADELLKQITELSNSnGELFADFETEqelTEAL-LKRAEQQQL-----EDIELLERAKAAHDKATK 1381
Cdd:pfam15921  511 AIEATnaeitklrSRVDLKLQELQHLKNE-GDHLRNVQTE---CEALkLQMAEKDKVieilrQQIENMTQLVGQHGRTAG 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1382 AVEQGDNTL-KEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEiqnAESLISQAEEALDGANKNANEAKKNAQEAQ 1460
Cdd:pfam15921  587 AMQVEKAQLeKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE---KVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1461 LKYAE--QASKDAELIRRkanetkvaarNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQ 1538
Cdd:pfam15921  664 TSRNElnSLSEDYEVLKR----------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1539 KQIEKANADLTAIKDELENLKDINTG----------DLDRLENRLATVEGEINRvnLTGRIEKYREQ-RTIQKNL----- 1602
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEAMTNankekhflkeEKNKLSQELSTVATEKNK--MAGELEVLRSQeRRLKEKVanmev 811

                          570
                   ....*....|....*..
gi 665410160  1603 -IDKYDAELRELKDEVQ 1618
Cdd:pfam15921  812 aLDKASLQFAECQDIIQ 828
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 847-897 7.25e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 58.90  E-value: 7.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410160   847 CDCNGNVDPNavGNCNRTTGECLkCIHNTAGEHCDQCLSGHFGDPLALPHG 897
Cdd:pfam00053    1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 901-954 7.72e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 58.52  E-value: 7.72e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665410160  901 RCSCYEAGTEQDEqsitrCDQVTGQCQCKPNVIGRDCGECQPGYFNIRS-GNGCE 954
Cdd:cd00055     1 PCDCNGHGSLSGQ-----CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
902-953 1.36e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 57.71  E-value: 1.36e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 665410160    902 CSCYEAGTEQDEqsitrCDQVTGQCQCKPNVIGRDCGECQPGYFNiRSGNGC 953
Cdd:smart00180    1 CDCDPGGSASGT-----CDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
growth_prot_Scy NF041483
polarized growth protein Scy;
1165-1545 2.13e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 66.00  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1165 ENAKKELQQALDLLNDEGAQALARAKEK-----SVEFGQQ--------------------------SEQISDISREARAL 1213
Cdd:NF041483  326 EALKAEAEQALADARAEAEKLVAEAAEKartvaAEDTAAQlakaartaeevltkasedakattraaAEEAERIRREAEAE 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1214 ADKLESEA--QFD-LKNAkdAKD--------AVE----------KAHQLAKSAIDLQLKIGTELRSEvglelshvkqslg 1272
Cdd:NF041483  406 ADRLRGEAadQAEqLKGA--AKDdtkeyrakTVElqeearrlrgEAEQLRAEAVAEGERIRGEARRE------------- 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1273 tVVQTSKEALRKANEvydtaltLLndvnrqTQPEIDISQLKKDAVA--------ANERADELLKQITE-LSNSNGELFAD 1343
Cdd:NF041483  471 -AVQQIEEAARTAEE-------LL------TKAKADADELRSTATAeservrteAIERATTLRRQAEEtLERTRAEAERL 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1344 FETEQELTEALLKRAEQQQLEDIELLERAKAA------------HDKATKAVEQGDNTLKEANNTYEKL---AGFQSDVQ 1408
Cdd:NF041483  537 RAEAEEQAEEVRAAAERAARELREETERAIAArqaeaaeeltrlHTEAEERLTAAEEALADARAEAERIrreAAEETERL 616

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1409 RsSESAE--KALQTVPNIEKE----------------------------IQNAESLISQAEEALDGANKNANE-AKKNAQ 1457
Cdd:NF041483  617 R-TEAAEriRTLQAQAEQEAErlrteaaadasaaraegenvavrlrseaAAEAERLKSEAQESADRVRAEAAAaAERVGT 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1458 EAQLKYAEqASKDAELIRRKANETKVAArnlREEADQLNHRVKltemdifklEESstkdDNLVDDAKRKVGQAKAdtqEA 1537
Cdd:NF041483  696 EAAEALAA-AQEEAARRRREAEETLGSA---RAEADQERERAR---------EQS----EELLASARKRVEEAQA---EA 755


                  ....*...
gi 665410160 1538 QKQIEKAN 1545
Cdd:NF041483  756 QRLVEEAD 763
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 461-512 2.38e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.36  E-value: 2.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  461 CGCDSGGSHQNTpaCDTETGICFCKENVEGRRCNECKPGFFNLDKnNRFGCT 512
Cdd:cd00055     2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
461-511 3.10e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.94  E-value: 3.10e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 665410160    461 CGCDSGGSHQNTpaCDTETGICFCKENVEGRRCNECKPGFFNldkNNRFGC 511
Cdd:smart00180    1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1004-1046 4.30e-10

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 4.30e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 665410160  1004 CECDESGSKGFQCDQN-GQCPCNDNVEGRRCDRCKENKYDRHRG 1046
Cdd:pfam00053    1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
744-785 4.36e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.55  E-value: 4.36e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 665410160    744 CDCH--GHAD-ICDSETGRCICQHNTHGDNCDQCAKGFYGNALGG 785
Cdd:smart00180    1 CDCDpgGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
growth_prot_Scy NF041483
polarized growth protein Scy;
1139-1593 5.92e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 64.46  E-value: 5.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1139 ADKFQADANGEIDRARqnytildqitenakKELQQALDLLNDEGAQALARAKEKSV---------------EFGQQSEQI 1203
Cdd:NF041483  668 AERLKSEAQESADRVR--------------AEAAAAAERVGTEAAEALAAAQEEAArrrreaeetlgsaraEADQERERA 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1204 SDISREARALADKLESEAQfdlknaKDAKDAVEKAHQLAksaidlqlkigTELRSEVGLELSHVKQSL-GTVVQTSKE-- 1280
Cdd:NF041483  734 REQSEELLASARKRVEEAQ------AEAQRLVEEADRRA-----------TELVSAAEQTAQQVRDSVaGLQEQAEEEia 796

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1281 ALRKANEvydtalTLLNDVNRQTQPEIDisQLKKDAVAANERADELLKQITElsnsngelfadfeTEQELTEALLKRAEQ 1360
Cdd:NF041483  797 GLRSAAE------HAAERTRTEAQEEAD--RVRSDAYAERERASEDANRLRR-------------EAQEETEAAKALAER 855

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1361 QQLEDIELLERAKA-AHDKATKAVEQGDNTLKEA-NNTYEKLAGFQSDVQR-SSESAEKA--LQTVPNIEKEIQNAESlI 1435
Cdd:NF041483  856 TVSEAIAEAERLRSdASEYAQRVRTEASDTLASAeQDAARTRADAREDANRiRSDAAAQAdrLIGEATSEAERLTAEA-R 934

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1436 SQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANET----KVAARNLREEADqlnhRVKL-TEMDIFKLE 1510
Cdd:NF041483  935 AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETvgsaQQHAERIRTEAE----RVKAeAAAEAERLR 1010

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1511 -ESSTKDDNLVDDAKRKVGQAKAD------------TQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRL---A 1574
Cdd:NF041483 1011 tEAREEADRTLDEARKDANKRRSEaaeqadtliteaAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIvaeA 1090

                         490
                  ....*....|....*....
gi 665410160 1575 TVEGeinrvnlTGRIEKYR 1593
Cdd:NF041483 1091 TVEG-------NSLVEKAR 1102
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1003-1050 6.38e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.21  E-value: 6.38e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665410160 1003 PCECDESGSKGFQCDQ-NGQCPCNDNVEGRRCDRCKENKYDRHRGCIDC 1050
Cdd:cd00055     1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1091-1548 4.45e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 61.77  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1091 AKLKAVQEKVAVLAQDARdnsgdggqTYAEVIDDLHKHL-DSVREHLVSADKFQADANGEIDRAR-QNYTILDQITENAK 1168
Cdd:NF041483  354 ARTVAAEDTAAQLAKAAR--------TAEEVLTKASEDAkATTRAAAEEAERIRREAEAEADRLRgEAADQAEQLKGAAK 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1169 KELQQAldllndegaqalaRAKekSVEFgqQSEqisdiSREARALADKLESEA--QFDLKNAKDAKDAVEKAHQLAKSAI 1246
Cdd:NF041483  426 DDTKEY-------------RAK--TVEL--QEE-----ARRLRGEAEQLRAEAvaEGERIRGEARREAVQQIEEAARTAE 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1247 DLQLKIGT---ELRSEVGLELSHV------------KQSLGTVVQTSKEALRKANEVYDTALTLlndvnrQTQPEIDISQ 1311
Cdd:NF041483  484 ELLTKAKAdadELRSTATAESERVrteaierattlrRQAEETLERTRAEAERLRAEAEEQAEEV------RAAAERAARE 557

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1312 LKKD---AVAAN--ERADELLKQITE-----------LSNSNGELF-----ADFETEQELTEALLK-RAEQQQLE-DIEL 1368
Cdd:NF041483  558 LREEterAIAARqaEAAEELTRLHTEaeerltaaeeaLADARAEAErirreAAEETERLRTEAAERiRTLQAQAEqEAER 637

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1369 LeRAKAAHDkATKAVEQGDNTL----KEANNTYEKLagfQSDVQrssESAEKalqtvpnIEKEIQNA-ESLISQAEEALD 1443
Cdd:NF041483  638 L-RTEAAAD-ASAARAEGENVAvrlrSEAAAEAERL---KSEAQ---ESADR-------VRAEAAAAaERVGTEAAEALA 702

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1444 GANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVkltemdifkLEESSTKDDNLVDDA 1523
Cdd:NF041483  703 AAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRL---------VEEADRRATELVSAA 773

                         490       500
                  ....*....|....*....|....*
gi 665410160 1524 KRKVGQAKADTQEAQKQIEKANADL 1548
Cdd:NF041483  774 EQTAQQVRDSVAGLQEQAEEEIAGL 798
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1004-1047 5.13e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 5.13e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160   1004 CECDESGSKGFQCDQ-NGQCPCNDNVEGRRCDRCKENKYDRH-RGC 1047
Cdd:smart00180    1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGpPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 846-893 6.56e-09

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.13  E-value: 6.56e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 665410160  846 SCDCNGNVDPNavGNCNRTTGECLkCIHNTAGEHCDQCLSGHFGDPLA 893
Cdd:cd00055     1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
growth_prot_Scy NF041483
polarized growth protein Scy;
1134-1572 8.67e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 60.61  E-value: 8.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1134 EHLVSADKFQADANGEIDR----ARQNYTILDQITENAKKELQQALDLLNDEGAQALArakeksvefGQQS--EQISDIS 1207
Cdd:NF041483  739 ELLASARKRVEEAQAEAQRlveeADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIA---------GLRSaaEHAAERT 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1208 R-EARALADKLESEAQFDLKNA--------KDAKDAVEKAHQLAKSAIDLQLKIGTELRSEvglelshvkqslgtvvqTS 1278
Cdd:NF041483  810 RtEAQEEADRVRSDAYAERERAsedanrlrREAQEETEAAKALAERTVSEAIAEAERLRSD-----------------AS 872

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1279 KEALRKANEVYDTALTLLNDVNR-QTQPEIDISQLKKDAVAaneRADELlkqITElsnsngelfADFETEQELTEAllkR 1357
Cdd:NF041483  873 EYAQRVRTEASDTLASAEQDAARtRADAREDANRIRSDAAA---QADRL---IGE---------ATSEAERLTAEA---R 934

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1358 AEQQQLEDiellERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSD-VQRSSESAEKALQTVPNIEKEIQ-NAESLI 1435
Cdd:NF041483  935 AEAERLRD----EARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAEtVGSAQQHAERIRTEAERVKAEAAaEAERLR 1010

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1436 SQAEEAldgANKNANEAKKNAQEAQLKYAEQASkdaelirRKANETKVAARNLREEADQLNHRVKLtemdifkleESSTK 1515
Cdd:NF041483 1011 TEAREE---ADRTLDEARKDANKRRSEAAEQAD-------TLITEAAAEADQLTAKAQEEALRTTT---------EAEAQ 1071

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1516 DDNLVDDAKRKVGQAKAD-TQEAQKQIEKANADL-----------TAIKDELENLKDINTGDLDRLENR 1572
Cdd:NF041483 1072 ADTMVGAARKEAERIVAEaTVEGNSLVEKARTDAdellvgarrdaTAIRERAEELRDRITGEIEELHER 1140
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 298-347 1.10e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.66  E-value: 1.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665410160  298 RCKCNGHASK---CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYNDLKWKR 347
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTG-------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
growth_prot_Scy NF041483
polarized growth protein Scy;
1181-1618 7.48e-07

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 54.45  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1181 EGAQALA-RAKEKSVEFGQQSEQISdisREARALADKLESEAQFDLKNAKDAKDAVEKAHqlAKSAIDLQLKIGTEL--- 1256
Cdd:NF041483   54 EARRSLAsRPAYDGADIGYQAEQLL---RNAQIQADQLRADAERELRDARAQTQRILQEH--AEHQARLQAELHTEAvqr 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1257 RSEVGLEL--------SHVKQSLGTVVQ----TSKEALRKANEVY---DTAL-------TLLNDVNRQ----------TQ 1304
Cdd:NF041483  129 RQQLDQELaerrqtveSHVNENVAWAEQlrarTESQARRLLDESRaeaEQALaaaraeaERLAEEARQrlgseaesarAE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1305 PEIDISQLKKDA----VAANERADELLKQITELSNSNGElfadfETEQELTEA--LLKRAEQQQLEDIELLERAKAAHDK 1378
Cdd:NF041483  209 AEAILRRARKDAerllNAASTQAQEATDHAEQLRSSTAA-----ESDQARRQAaeLSRAAEQRMQEAEEALREARAEAEK 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1379 A-TKAVEQGDNTLKEANNTYEklagfqsdvQRSSESAEKALQTVPNIEKEiqnAESLISQAEEALDGANKNANEAKKNAQ 1457
Cdd:NF041483  284 VvAEAKEAAAKQLASAESANE---------QRTRTAKEEIARLVGEATKE---AEALKAEAEQALADARAEAEKLVAEAA 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1458 E-----------AQL----KYAEQ----ASKDAELIRRKANEtkvAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDN 1518
Cdd:NF041483  352 EkartvaaedtaAQLakaaRTAEEvltkASEDAKATTRAAAE---EAERIRREAEAEADRLRGEAADQAEQLKGAAKDDT 428

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1519 ---------LVDDAKRKVGQA---KADT------------QEAQKQIEKANAdlTAikdelENLKDINTGDLDRLENRlA 1574
Cdd:NF041483  429 keyraktveLQEEARRLRGEAeqlRAEAvaegerirgearREAVQQIEEAAR--TA-----EELLTKAKADADELRST-A 500

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 665410160 1575 TVEGEinRVNlTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQ 1618
Cdd:NF041483  501 TAESE--RVR-TEAIERATTLRRQAEETLERTRAEAERLRAEAE 541
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 299-343 1.11e-06

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 46.96  E-value: 1.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 665410160   299 CKCNGHASK---CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYNDL 343
Cdd:pfam00053    1 CDCNPHGSLsdtCDPETG-------QCLCKPGVTGRHCDRCKPGYYGL 41
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1272-1492 1.34e-06

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: 51.99  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1272 GTVVQTSKEALRKANEVYDTALTLLNDVN-RQTQPEID---------ISQLKKDAVAANERADELLKQITELSNSNGELF 1341
Cdd:cd22656    76 GDIYNYAQNAGGTIDSYYAEILELIDDLAdATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1342 ADFET-EQELTEALLKRAEQQQLEDIE-LLERAKAAHDKATKAVEqgdNTLKEANNTYEKLAGFQSDVQRSSESAEKALQ 1419
Cdd:cd22656   156 TALETlEKALKDLLTDEGGAIARKEIKdLQKELEKLNEEYAAKLK---AKIDELKALIADDEAKLAAALRLIADLTAADT 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1420 TVPNIEKEIQNAESLISQAEEA-------LDGANKNANEAKKNAqeaqlKYAEQASKDAELIRRKANETKVAARNLREEA 1492
Cdd:cd22656   233 DLDNLLALIGPAIPALEKLQGAwqaiatdLDSLKDLLEDDISKI-----PAAILAKLELEKAIEKWNELAEKADKFRQNA 307
growth_prot_Scy NF041483
polarized growth protein Scy;
1181-1557 1.43e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 53.29  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1181 EGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEaqfdlknakdAKDAVEKAHQLAKSAIDLQLKIGTE----L 1256
Cdd:NF041483  248 ESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAE----------AKEAAAKQLASAESANEQRTRTAKEeiarL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1257 RSEVGLELSHVKQSLGTVVQTSK-EALRKANEVYDTAltllndvnRQTQPEIDISQLKKDAVAANE---RADELLKQITE 1332
Cdd:NF041483  318 VGEATKEAEALKAEAEQALADARaEAEKLVAEAAEKA--------RTVAAEDTAAQLAKAARTAEEvltKASEDAKATTR 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1333 LSNSNGELF---ADFETEQELTEAL-----LKRAEQQQLED-----IELLERAKAAHDKA----TKAVEQGD-------- 1387
Cdd:NF041483  390 AAAEEAERIrreAEAEADRLRGEAAdqaeqLKGAAKDDTKEyraktVELQEEARRLRGEAeqlrAEAVAEGErirgearr 469

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1388 ---NTLKEANNTYEKL---AGFQSDVQRSSESAEKALQTVPNIEKeiqnAESLISQAEEALDGANKNANEAKKNAQEAQL 1461
Cdd:NF041483  470 eavQQIEEAARTAEELltkAKADADELRSTATAESERVRTEAIER----ATTLRRQAEETLERTRAEAERLRAEAEEQAE 545

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1462 KYAEQASKDAELIRRKAnETKVAARnlREEADQLNHRVKL-----------------TEMDIFKLEESSTKDDNLVDDAK 1524
Cdd:NF041483  546 EVRAAAERAARELREET-ERAIAAR--QAEAAEELTRLHTeaeerltaaeealadarAEAERIRREAAEETERLRTEAAE 622

                         410       420       430
                  ....*....|....*....|....*....|....
gi 665410160 1525 R-KVGQAKADtQEAQKQIEKANADLTAIKDELEN 1557
Cdd:NF041483  623 RiRTLQAQAE-QEAERLRTEAAADASAARAEGEN 655
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
847-891 1.52e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 46.54  E-value: 1.52e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410160    847 CDCN--GNVDPNavgnCNRTTGECLkCIHNTAGEHCDQCLSGHFGDP 891
Cdd:smart00180    1 CDCDpgGSASGT----CDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 359-414 2.15e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160   359 CNCNGLA---DKCFFdanlfnrtgHGGHCLdCRENRDGPNCERCKENFYMRDDGYCVNC 414
Cdd:pfam00053    1 CDCNPHGslsDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1191-1470 8.38e-05

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 47.52  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1191 EKSVEFGQQSEQISDISREARALADKLESEAqfDLKNAKDakdavEKAHQLAKSAidlqlkiGTELRSEvglelSHVKQS 1270
Cdd:NF012221 1539 ESSQQADAVSKHAKQDDAAQNALADKERAEA--DRQRLEQ-----EKQQQLAAIS-------GSQSQLE-----STDQNA 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1271 LGTVVQTSKEALR-KANEVYDTALTLLNDVNrqtqpeidisQLKKDAVAANERADELLKQitelsnsngelFAD--FETE 1347
Cdd:NF012221 1600 LETNGQAQRDAILeESRAVTKELTTLAQGLD----------ALDSQATYAGESGDQWRNP-----------FAGglLDRV 1658

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1348 QE-LTEAllKRAEQQQLEDIEllERAKAAHDKATKAVEQGDNTLKeanNTYEKLAGFQSDVQRSSESAEKALQTVPNIEK 1426
Cdd:NF012221 1659 QEqLDDA--KKISGKQLADAK--QRHVDNQQKVKDAVAKSEAGVA---QGEQNQANAEQDIDDAKADAEKRKDDALAKQN 1731

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1427 EIQNAES----LISQAEEALD----GANKNANEAKKNAQEAQLKYAEQASKD 1470
Cdd:NF012221 1732 EAQQAESdanaAANDAQSRGEqdasAAENKANQAQADAKGAKQDESDKPNRQ 1783
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1056-1456 1.29e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 47.14  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1056 LVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEF----------EAKLKAVQEKVAVLAQDARDN----SGDGGQTYAEV 1121
Cdd:NF012221 1450 LYQDLSNLTAGEVIALSFDFARRAGLSTNNGIEVlwngevvfasSGDASAWQQKTLKLTAKAGSNrlefKGTGHNDGLGY 1529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1122 IDD-------LHKHLDSVREHlVSADKFQADANGEIDRARQNYTILDQitenakkELQQALDLLNdeGAQALARAKEKSV 1194
Cdd:NF012221 1530 ILDnvvatseSSQQADAVSKH-AKQDDAAQNALADKERAEADRQRLEQ-------EKQQQLAAIS--GSQSQLESTDQNA 1599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1195 EFGQQSEQISDISREARALADKLESEAQ-FDLKNAkDAKDAVEKAHQLAKsaidlqlkigtelRSEVGLeLSHVKQSLGT 1273
Cdd:NF012221 1600 LETNGQAQRDAILEESRAVTKELTTLAQgLDALDS-QATYAGESGDQWRN-------------PFAGGL-LDRVQEQLDD 1664

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1274 VVQTSKEALRKANEVYdtaltllndVNRQTQpeidisqlKKDAVAANE----RADELLKQITELSNSngelfADFETEQE 1349
Cdd:NF012221 1665 AKKISGKQLADAKQRH---------VDNQQK--------VKDAVAKSEagvaQGEQNQANAEQDIDD-----AKADAEKR 1722

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1350 LTEALLKRAEQQQledielleRAKAAHDKATKAVEQGDNTLKEANNTYEK-------------------------LAGFQ 1404
Cdd:NF012221 1723 KDDALAKQNEAQQ--------AESDANAAANDAQSRGEQDASAAENKANQaqadakgakqdesdkpnrqgaagsgLSGKA 1794

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1405 SDVQRSSESAEkALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNA 1456
Cdd:NF012221 1795 YSVEGVAEPGS-HINPDSPAAADGRFSEGLTEQEQEALEGATNAVNRLQINA 1845
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
299-342 2.70e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.99  E-value: 2.70e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410160    299 CKCN--GHASK-CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYND 342
Cdd:smart00180    1 CDCDpgGSASGtCDPDTG-------QCECKPNVTGRRCDRCAPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
793-836 2.24e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.24e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 665410160    793 CPCPNDGA----ClqiNEDTVICtECPKGYFGSRCEQCSDGFFGDPTG 836
Cdd:smart00180    1 CDCDPGGSasgtC---DPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPP 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
359-411 2.24e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.24e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160    359 CNCNG---LADKCFFDanlfnrtghGGHCLdCRENRDGPNCERCKENFYMRDDGYC 411
Cdd:smart00180    1 CDCDPggsASGTCDPD---------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPGC 46
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1423-1521 3.46e-03

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 41.12  E-value: 3.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   1423 NIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLT 1502
Cdd:smart00283    1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAAN-ADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEA 79

                            90
                    ....*....|....*....
gi 665410160   1503 EMDIFKLEESSTKDDNLVD 1521
Cdd:smart00283   80 VSAVEELEESSDEIGEIVS 98
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 721-848 3.69e-03

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 39.98  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  721 CESCAPGYRHSPARGGPfMPCIPC-DCHGHAdicdSETGRCICQHNTHgdnCDqCAKGFYGNALGGTPNDCKRCPcPNDG 799
Cdd:cd13416    35 CEPCLDGVTFSDVVSHT-EPCQPCtRCPGLM----SMRAPCTATHDTV---CE-CAYGYYLDEDSGTCEPCTVCP-PGQG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  800 A---ClQINEDTVictecpkgyfgsrCEQCSDGFFGDPTGLLGEVQTCKSCD 848
Cdd:cd13416   105 VvqsC-GPNQDTV-------------CEACPEGTYSDEDSSTDPCLPCTVCE 142
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 1427-1499 5.26e-03

Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.


Pssm-ID: 468572 [Multi-domain]  Cd Length: 90  Bit Score: 37.66  E-value: 5.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1427 EIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKDAElirrkanetkvAARnlrEEADQLNHRV 1499
Cdd:NF040598   23 DLENLQSQVQELDAKVDQASSDAAAAQSRADEAAAK-AEQAEAAAN-----------AAQ---QEADEANERA 80
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 358-408 5.66e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.56  E-value: 5.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665410160  358 ACNCNGLADK---CFFdanlfnrtgHGGHCLdCRENRDGPNCERCKENFYMRDD 408
Cdd:cd00055     1 PCDCNGHGSLsgqCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGLPS 44
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 61-296 2.06e-113

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


Pssm-ID: 214532  Cd Length: 238  Bit Score: 358.21  E-value: 2.06e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160     61 YGRPQKCLPEFINAAYQLQIESTNTCGEQNDNHFCIQT-MNQNHKNCEFCKYND----HNPSFLTDLHDPQSPTWWQSET 135
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVgHTEQGKKCDYCDARNprrsHPAENLTDGNNPNNPTWWQSEP 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    136 MFEGIQhpnYVNLTLHLGKSYDITYVRILFRSPRPeSFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRAIRKGeGEAH 215
Cdd:smart00136   81 LSNGPQ---NVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKG-NEDE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    216 ALCTSEYSDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDS-QVLKSYFYAISDIA 294
Cdd:smart00136  156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRpEVTRRYYYAISDIA 235


                    ..
gi 665410160    295 VG 296
Cdd:smart00136  236 VG 237
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
67-297 7.35e-104

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 331.08  E-value: 7.35e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    67 CLPEFINAAYQLQIESTNTCGEQNDNHFCIQTMNQNHKNCEFC----KYNDHNPSFLTDLHDPQSPTWWQSETMFEgiqH 142
Cdd:pfam00055    1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGKKCFICdsrdPHNSHPPSNLTDSNNGTNETWWQSETGVI---Q 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   143 PNYVNLTLHLGKSYDITYVRILFRSPRPESFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRaiRKGEGEAHALCTSEY 222
Cdd:pfam00055   78 YENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGP--SRGIKDDEVICTSEY 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410160   223 SDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDSQVLKSYFYAISDIAVGA 297
Cdd:pfam00055  156 SDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
LamB smart00281
Laminin B domain;
572-697 5.26e-41

Laminin B domain;


Pssm-ID: 214597  Cd Length: 127  Bit Score: 147.41  E-value: 5.26e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160    572 GNEHVYFQAPDRFLGDQRASYNRDLKFKLQLVGQVANTGVS--DVILEGAGSRISLPifAQGNGIPDQGVK-EYTFRLHE 648
Cdd:smart00281    1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSapDVILEGNGLRISHP--AEGPPLPDELTTvEVRFREEN 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 665410160    649 HHDYQWQPSQSARgFLSILSNLTAIKIRATYSVQGEAI-LDDVELQTAHR 697
Cdd:smart00281   79 WQYYGGRPVTRED-LMMVLANLTAILIRATYSQQMAGSrLSDVSLEVAVP 127
Laminin_B pfam00052
Laminin B (Domain IV);
577-708 9.05e-36

Laminin B (Domain IV);


Pssm-ID: 459652  Cd Length: 136  Bit Score: 132.78  E-value: 9.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   577 YFQAPDRFLGDQRASYNRDLKFKLQ---LVGQVANTGVSDVILEGAGSRISLPIFAQGNGIPDQGvKEYTFRLHEHHdyq 653
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRyepLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQE-QTYSVRLHEEN--- 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   654 WQPSQ----SARGFLSILSNLTAIKIRATYSV-QGEAILDDVELQTAHRGAAGHPATWIE 708
Cdd:pfam00052   77 WRDSDgapvSREDFMMVLANLTAILIRATYSTgSGQVSLSNVSLDSAVPGGSGPPASWVE 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1054-1621 1.21e-25

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: 115.92  E-value: 1.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1054 YNLVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEFEAKLKAVQEkvavlaQDARDNSGDGGQTYAEvIDDLHKHLDSVR 1133
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE------AELKELQAELEELEEE-LEELQEELERLE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1134 EHLVSADKFQADANGEIDRARQNYTILDQITEnAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARAL 1213
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1214 ADKLESEAQFDL-KNAKDAKDAVE--------KAHQLAKSAID------LQLKIGTELRSEVGLELSHVKQS-------- 1270
Cdd:TIGR02168  540 EAALGGRLQAVVvENLNAAKKAIAflkqnelgRVTFLPLDSIKgteiqgNDREILKNIEGFLGVAKDLVKFDpklrkals 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1271 --LGT--VVQTSKEALRKANE---------------------VYDTALTLLNDVNRQtqpeIDISQLKKDAVAANERADE 1325
Cdd:TIGR02168  620 ylLGGvlVVDDLDNALELAKKlrpgyrivtldgdlvrpggviTGGSAKTNSSILERR----REIEELEEKIEELEEKIAE 695

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1326 LLKQITELSNSNGELfadfETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANntyEKLAGFQS 1405
Cdd:TIGR02168  696 LEKALAELRKELEEL----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE---AEIEELEE 768

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1406 DVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYaEQASKDAELIRRKANETKVAA 1485
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-ESLERRIAATERRLEDLEEQI 847

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1486 RNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDIntgd 1565
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK---- 923

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160  1566 LDRLENRLATVEGEINrvNLTGRI-EKYR-EQRTIQKN------LIDKYDAELRELKDEVQNIG 1621
Cdd:TIGR02168  924 LAQLELRLEGLEVRID--NLQERLsEEYSlTLEEAEALenkiedDEEEARRRLKRLENKIKELG 985
PTZ00121 PTZ00121
MAEBL; Provisional
 1165-1615 2.07e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 89.04  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1165 ENAKKeLQQALDLLNDEGAQALARAKE-KSVEFGQQSEQISDIsREARALADKLESEAqfdLKNAKDAKDAVEKAHQLAK 1243
Cdd:PTZ00121 1173 EDAKK-AEAARKAEEVRKAEELRKAEDaRKAEAARKAEEERKA-EEARKAEDAKKAEA---VKKAEEAKKDAEEAKKAEE 1247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1244 saidlqLKIGTELRSEVGLELSHVKQSLGTVvqtSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAAnERA 1323
Cdd:PTZ00121 1248 ------ERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA-KKA 1317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1324 DELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKlagf 1403
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA---- 1393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1404 qSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEAldganKNANEAKKNAQEAqlKYAEQASKDAELiRRKANETKV 1483
Cdd:PTZ00121 1394 -DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-----KKADEAKKKAEEA--KKADEAKKKAEE-AKKAEEAKK 1464

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1484 AARNLR--EEADQLNHRVKLTEMDIFKLEESSTKDDNLvddakRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDI 1561
Cdd:PTZ00121 1465 KAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665410160 1562 NTGDLDRLENRLATVEgEINRVNLTGRIEKYREQRTiQKNLIDKYDAELRELKD 1615
Cdd:PTZ00121 1540 KKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEE 1591
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1130-1629 1.55e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 85.89  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1130 DSVREHLV----SADKFQ-ADAN-GEIDRArqnytiLDQITENAKKELQQALDLLNdegaqalaRAKEKSVEFGQQSEQI 1203
Cdd:PRK03918  144 DESREKVVrqilGLDDYEnAYKNlGEVIKE------IKRRIERLEKFIKRTENIEE--------LIKEKEKELEEVLREI 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1204 SDISREARALADKLEsEAQFDLKNAKDAKDAVEKAH----QLAKSAIDLQLKIGtELRS---EVGLELSHVKQSLGTV-- 1274
Cdd:PRK03918  210 NEISSELPELREELE-KLEKEVKELEELKEEIEELEkeleSLEGSKRKLEEKIR-ELEErieELKKEIEELEEKVKELke 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1275 VQTSKEALRKANEVYDTALTLLNDVN-RQTQPEIDISQLK---KDAVAANERADELLKQITELSNSNGELFadfETEQEL 1350
Cdd:PRK03918  288 LKEKAEEYIKLSEFYEEYLDELREIEkRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELE---ERHELY 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1351 TEALLKRAEQQQL-------------EDIELLERAK--------------AAHDKATKAVEQGDNTLKEAN--------- 1394
Cdd:PRK03918  365 EEAKAKKEELERLkkrltgltpekleKELEELEKAKeeieeeiskitariGELKKEIKELKKAIEELKKAKgkcpvcgre 444

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1395 ----------NTY-EKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEAldganKNANEAKKNAQEAQLKY 1463
Cdd:PRK03918  445 lteehrkellEEYtAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-----EQLKELEEKLKKYNLEE 519

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1464 AEQASKDAELIRRKANETKVAARNLREEADQ---LNHRVKLTEMDIFKLEE--------------SSTKDDN-------- 1518
Cdd:PRK03918  520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEelaellkeleelgfESVEELEerlkelep 599

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1519 -------LVD------DAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDI-NTGDLDRLENRLATVEGEINRvn 1584
Cdd:PRK03918  600 fyneyleLKDaekeleREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAG-- 677

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 665410160 1585 LTGRIEKYREQR-TIQKNLiDKYDAELRELKDEVQNIGLISKALPD 1629
Cdd:PRK03918  678 LRAELEELEKRReEIKKTL-EKLKEELEEREKAKKELEKLEKALER 722
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1065-1627 2.39e-16

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 85.09  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1065 RAKLFNLSQTLDEIARTPVTNDDEFEAKLKAVQEKVAVL------AQDARDNSGDGG---QTYAEVIDDLHKHLDSVREH 1135
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeeRDDLLAEAGLDDadaEAVEARREELEDRDEELRDR 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1136 LVSADKFQADANGEIDRARQNytiLDQITENAKKELQQALDLlnDEGAQALARAKEKsvefgqQSEQISDISREARALad 1215
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLRED---ADDLEERAEELREEAAEL--ESELEEAREAVED------RREEIEELEEEIEEL-- 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1216 klesEAQFDlkNAKDAKDAVEKAHQLAKSAIDlqlkigtELRSEVGlelshvkqSLGTVVQTSKEALRKANEVYDTALTl 1295
Cdd:PRK02224  397 ----RERFG--DAPVDLGNAEDFLEELREERD-------ELREREA--------ELEATLRTARERVEEAEALLEAGKC- 454

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1296 lndvnrqtqPEidISQLKKDAVAAnERADELLKQITELsnsngelfadfetEQELTEAllkRAEQQQLEdiELLERAKAA 1375
Cdd:PRK02224  455 ---------PE--CGQPVEGSPHV-ETIEEDRERVEEL-------------EAELEDL---EEEVEEVE--ERLERAEDL 504

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1376 hdkatKAVEQGDNTLKEANNTYEKLAGfqsdvQRSSESAEKALQtvpnIEKEIQNAESLISQAEEALDGANKNANEAKKN 1455
Cdd:PRK02224  505 -----VEAEDRIERLEERREDLEELIA-----ERRETIEEKRER----AEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1456 AQEAQLKYAEQASKDAELIRRKANETKVAAR-NLREEADQLNHRVK-LTEMDIF---KLEESSTKDDNL---VDDAkrKV 1527
Cdd:PRK02224  571 REEVAELNSKLAELKERIESLERIRTLLAAIaDAEDEIERLREKREaLAELNDErreRLAEKRERKRELeaeFDEA--RI 648

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1528 GQAKADTQEAQKQIEKAN---ADLTAIKDELENLKDINTGDLDRLEN---RLATVEgeiNRVnltGRIEK-YREQRTIQK 1600
Cdd:PRK02224  649 EEAREDKERAEEYLEQVEeklDELREERDDLQAEIGAVENELEELEElreRREALE---NRV---EALEAlYDEAEELES 722

                         570       580
                  ....*....|....*....|....*..
gi 665410160 1601 NLIDkYDAELRElkdevQNIGLISKAL 1627
Cdd:PRK02224  723 MYGD-LRAELRQ-----RNVETLERML 743
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1279-1622 4.80e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.22  E-value: 4.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1279 KEALRKANEVyDTALTLLND----VNRQtqpeidISQLKKDAVAAnERADELLKQITELSnsnGELFA----DFETEQEL 1350
Cdd:COG1196   175 EEAERKLEAT-EENLERLEDilgeLERQ------LEPLERQAEKA-ERYRELKEELKELE---AELLLlklrELEAELEE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1351 TEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTY----EKLAGFQSDVQRSSESAEKALQTVPNIEK 1426
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEELEE 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1427 EIQNAESLISQAEEALDGANKNANEAKK--NAQEAQLKYAEQASKDAELIRRKANETKVAARN--LREEADQLNHRVKLT 1502
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEelEEAEAELAEAEEALLEAEAELAEAEEELEELAEelLEALRAAAELAAQLE 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1503 EmdifkLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINR 1582
Cdd:COG1196   404 E-----LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 665410160 1583 VN-LTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGL 1622
Cdd:COG1196   479 LAeLLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1088-1559 8.21e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 83.57  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1088 EFEAKLKAVQEKVAVLAQDardnsgdggqtyaeviddlHKHLDSVREHLVSADKFQADANG-EIDRARQNYTILdqitEN 1166
Cdd:PRK03918  342 ELKKKLKELEKRLEELEER-------------------HELYEEAKAKKEELERLKKRLTGlTPEKLEKELEEL----EK 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1167 AKKELQQALDLLNDEGAQALARAKE--KSVEFGQQSEQI-----SDISREARAladKLESEAQFDLKN-AKDAKDAVEKA 1238
Cdd:PRK03918  399 AKEEIEEEISKITARIGELKKEIKElkKAIEELKKAKGKcpvcgRELTEEHRK---ELLEEYTAELKRiEKELKEIEEKE 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1239 HQLAKSAIDLQLKIGTELR----SEVGLELSHVKQSLGTVvqtSKEALRKANEVYDTALTLLNDVnrqtqpEIDISQLKK 1314
Cdd:PRK03918  476 RKLRKELRELEKVLKKESEliklKELAEQLKELEEKLKKY---NLEELEKKAEEYEKLKEKLIKL------KGEIKSLKK 546

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1315 DAvaanERADELLKQITELSNSNGELfadfetEQELTEaLLKRAEQQQLEDIELLERakaahdkatKAVEqgdntLKEAN 1394
Cdd:PRK03918  547 EL----EKLEELKKKLAELEKKLDEL------EEELAE-LLKELEELGFESVEELEE---------RLKE-----LEPFY 601

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1395 NTYEKLAGFQSDVQRssesaekalqtvpnIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEqasKDAELI 1474
Cdd:PRK03918  602 NEYLELKDAEKELER--------------EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE---EEYEEL 664

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1475 RRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKddnlVDDAKRKVgqakadtqeaqKQIEKANADLTAIKDE 1554
Cdd:PRK03918  665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKEL-----------EKLEKALERVEELREK 729


                  ....*
gi 665410160 1555 LENLK 1559
Cdd:PRK03918  730 VKKYK 734
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1116-1616 2.17e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 82.29  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1116 QTYAEVIDDLHKHLDSVREHLVSADkfQADANGEIDRARQNYTILD---QITENAKKELQQALDLLNDEGAQALARAKEK 1192
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAE--LEELEAELEELEAELEELEaelAELEAELEELRLELEELELELEEAQAEEYEL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1193 SVEFGQQSEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQlkigtELRSEVGLELSHVKQSLG 1272
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-----EELEEAEAELAEAEEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1273 TVVQTSKEALRKANEVYDTALTLLNDVNRQTQpeiDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTE 1352
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAA---QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1353 ALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEAN----------NTYEKLAGFQSDVQRSSESAEKAL--QT 1420
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeaaarlllllEAEADYEGFLEGVKAALLLAGLRGlaGA 525

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1421 VPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKDAELIRRKANETKVAARNLR---EEADQLNH 1497
Cdd:COG1196   526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALArgaIGAAVDLV 604

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1498 RVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVE 1577
Cdd:COG1196   605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 665410160 1578 GEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDE 1616
Cdd:COG1196   685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1087-1613 2.41e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.91  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1087 DEFEAKLKAVQEKVAVLAQDARDNSgdggQTYAEVIDDLHKHLDSVREHLVSADKFQADANgEIDRARQNYTILDQITEN 1166
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAE----AELAEAEEELEELAEELLEALRAAAELAAQLE-ELEEAEEALLERLERLEE 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1167 AKKELQQALDLLNDEGAQALARAKEksvefgQQSEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAI 1246
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEE------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1247 DLQLKIGTELRSEVGLELSHVKQS-----LGTVVQTSKEALRKANEVYDTALtLLNDVNRQTQPEID-ISQLKKDA---- 1316
Cdd:COG1196   496 LLEAEADYEGFLEGVKAALLLAGLrglagAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAaIEYLKAAKagra 574

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1317 --VAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEAn 1394
Cdd:COG1196   575 tfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG- 653

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1395 ntyeklagfqsdvQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELI 1474
Cdd:COG1196   654 -------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1475 RRKANETKVAARNLREEADQLnhrvkltemdifkLEESSTKDDNLVDDAkrkvgQAKADTQEAQKQIEKanadltaIKDE 1554
Cdd:COG1196   721 LEEEALEEQLEAEREELLEEL-------------LEEEELLEEEALEEL-----PEPPDLEELERELER-------LERE 775

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1555 LENLKDINTG---DLDRLENRLATVEGEINrvNLTGRIEKYREqrtiqknLIDKYDAELREL 1613
Cdd:COG1196   776 IEALGPVNLLaieEYEELEERYDFLSEQRE--DLEEARETLEE-------AIEEIDRETRER 828
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1215-1620 3.98e-15

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: 80.83  E-value: 3.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1215 DKLESEaqfdLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGlELSHVKQSLGTVV-QTSKEALRKANEVYDTAL 1293
Cdd:TIGR04523  120 NKLEVE----LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELnLLEKEKLNIQKNIDKIKN 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1294 TLLNDvnrqtqpEIDISQLKKdavaANERADELLKQITELSNSNGELFADFETEQ-ELTE--ALLKRAEQQQLEDIELLE 1370
Cdd:TIGR04523  195 KLLKL-------ELLLSNLKK----KIQKNKSLESQISELKKQNNQLKDNIEKKQqEINEktTEISNTQTQLNQLKDEQN 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1371 RAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDV-QRSSESAEKALQT-VPNIEKEIQNAESLISQAEEALDGANKN 1448
Cdd:TIGR04523  264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnNQKEQDWNKELKSeLKNQEKKLEEIQNQISQNNKIISQLNEQ 343

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1449 ANEAKKnaqEAQLKYAEQASKDAELirrkaNETKVAARNLREEADQlnhrvKLTEmdIFKLEESSTkddnlvdDAKRKVG 1528
Cdd:TIGR04523  344 ISQLKK---ELTNSESENSEKQREL-----EEKQNEIEKLKKENQS-----YKQE--IKNLESQIN-------DLESKIQ 401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1529 QAKADTQEAQKQIEKANADLTAIKDELENLKDINT---GDLDRLENRLATVEGEINrvNLtgriEKYREQrtiQKNLIDK 1605
Cdd:TIGR04523  402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnSEIKDLTNQDSVKELIIK--NL----DNTRES---LETQLKV 472

                          410
                   ....*....|....*
gi 665410160  1606 YDAELRELKDEVQNI 1620
Cdd:TIGR04523  473 LSRSINKIKQNLEQK 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1201-1584 4.21e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.14  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1201 EQISDISREaraLADKLESeaqfdLKnaKDAKDAvEKAHQLAKSAIDLQLkigtELRsevGLELSHVKQSLgTVVQTSKE 1280
Cdd:COG1196   189 ERLEDILGE---LERQLEP-----LE--RQAEKA-ERYRELKEELKELEA----ELL---LLKLRELEAEL-EELEAELE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1281 ALRKANEVYDTALTLLndvnrqtqpEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQ 1360
Cdd:COG1196   250 ELEAELEELEAELAEL---------EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1361 QQLEDIEL----------LERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQtvpNIEKEIQN 1430
Cdd:COG1196   321 LEEELAELeeeleeleeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---EALRAAAE 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1431 AESLISQAEEALDGANKNANEAKKNAQEAQlkyAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEmdifkLE 1510
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLEEELEELE---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-----LL 469

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1511 ESSTKDDNLVDDAKRKVGQAKA---DTQEAQKQIEKANADLTAIKDELENLKDINTGDLDR---------LENRLATVEG 1578
Cdd:COG1196   470 EEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaayeaaLEAALAAALQ 549


                  ....*.
gi 665410160 1579 EINRVN 1584
Cdd:COG1196   550 NIVVED 555
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1149-1551 4.41e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 4.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1149 EIDRARQNYTILDQITENAKKELQQA---LDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEaQFDL 1225
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL-SKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1226 KNAKDAKDAVEKahQLAKSaiDLQLKIGTELRSEVGLELSHVKQSLgtvvQTSKEALRKANEVY-DTALTLLNDVNRQTQ 1304
Cdd:TIGR02168  757 TELEAEIEELEE--RLEEA--EEELAEAEAEIEELEAQIEQLKEEL----KALREALDELRAELtLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1305 PEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQlediELLERAKAAHDKATKAVE 1384
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE----EALALLRSELEELSEELR 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1385 QGDNTLKEANNTYEKLAGFQSDVQRssesaekalqtvpniekEIQNAESLISQAEEALdganknANEAKKNAQEAQLKYA 1464
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLEL-----------------RLEGLEVRIDNLQERL------SEEYSLTLEEAEALEN 961

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1465 EQASKDAELIRRkanetkvaARNLREEADQLNhRVKLTEMDIFKlEESSTKDDnlvddakrkVGQAKADTQEAQKQIEKA 1544
Cdd:TIGR02168  962 KIEDDEEEARRR--------LKRLENKIKELG-PVNLAAIEEYE-ELKERYDF---------LTAQKEDLTEAKETLEEA 1022


                   ....*..
gi 665410160  1545 NADLTAI 1551
Cdd:TIGR02168 1023 IEEIDRE 1029
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1279-1618 9.85e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.10  E-value: 9.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1279 KEALRKANEVyDTALTLLNDV----NRQTQPeidisqLKKDAVAAnERADELLKQITELSnsnGELFAD----FETEQEL 1350
Cdd:TIGR02168  175 KETERKLERT-RENLDRLEDIlnelERQLKS------LERQAEKA-ERYKELKAELRELE---LALLVLrleeLREELEE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1351 TEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQtvpNIEKEIQN 1430
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA---NLERQLEE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1431 AESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELirrkanetkvaarnlreeadqlnhrvkltEMDIFKLE 1510
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL-----------------------------EAELEELE 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1511 ESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRL-ENRLATVEGEINRVN----- 1584
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEeelee 451

                          330       340       350
                   ....*....|....*....|....*....|....
gi 665410160  1585 LTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQ 1618
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELA 485
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
956-1001 1.27e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 69.26  E-value: 1.27e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160    956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSSEGC 1001
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 956-1004 2.12e-14

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 68.92  E-value: 2.12e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665410160   956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSSEGCKPC 1004
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1161-1627 3.26e-14

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 78.16  E-value: 3.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1161 DQITENAKKELQQALDLLNDEGAQA------LARAKEKSVEFGQQSEQISDISREARALADKLESE---AQFDLKNAKDA 1231
Cdd:PRK02224  194 AQIEEKEEKDLHERLNGLESELAELdeeierYEEQREQARETRDEADEVLEEHEERREELETLEAEiedLRETIAETERE 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1232 KDAVEKAHQLAKSAIDLQLKIGTELRSEVGLElshvkqslgtvvQTSKEALRKANEVYDTALTLLNDVNRQTQPeiDISQ 1311
Cdd:PRK02224  274 REELAEEVRDLRERLEELEEERDDLLAEAGLD------------DADAEAVEARREELEDRDEELRDRLEECRV--AAQA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1312 LKKDAVAANERADELLKQITELSNSNGELFADFE-TEQELTEALLKRAE-QQQLEDIE---------------LLERAKA 1374
Cdd:PRK02224  340 HNEEAESLREDADDLEERAEELREEAAELESELEeAREAVEDRREEIEElEEEIEELRerfgdapvdlgnaedFLEELRE 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1375 AHDKATKAVEQGDNTLKEANNTYEKLAGFQS---------DVQRSS--ESAEKALQTVPNIEKEIQNAESLISQAEEALD 1443
Cdd:PRK02224  420 ERDELREREAELEATLRTARERVEEAEALLEagkcpecgqPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEVEERLE 499

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1444 gankNANEAKKNAQEAQlKYAEQASKDAELI---RRKANETKVAARNLREEADQLNhrvklTEMDifkleesstkddnlv 1520
Cdd:PRK02224  500 ----RAEDLVEAEDRIE-RLEERREDLEELIaerRETIEEKRERAEELRERAAELE-----AEAE--------------- 554

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1521 ddAKRKVGQAKAD-TQEAQKQIEKANADLTAIKDELENLKDINTgDLDRLENRLATVE---------GEIN--------- 1581
Cdd:PRK02224  555 --EKREAAAEAEEeAEEAREEVAELNSKLAELKERIESLERIRT-LLAAIADAEDEIErlrekrealAELNderrerlae 631

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1582 ----RVNLTG-----RIEKYREQRTIQKNLIDKYDAELREL---KDEVQN-IGLISKAL 1627
Cdd:PRK02224  632 krerKRELEAefdeaRIEEAREDKERAEEYLEQVEEKLDELreeRDDLQAeIGAVENEL 690
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1080-1618 7.65e-14

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 76.73  E-value: 7.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1080 RTPVTNDDEFEAKLKAVQEKVAVLAQdardnsgdggqtYAEVIDDLHKhldsVREHLVSADKFQADANGEIDRARQNYTI 1159
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEE------------YAELQEELEE----LEEELEELEAELEELREELEKLEKLLQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1160 LDQITEnaKKELQQALDLLNDEgaqaLARAKEKSVEFGQQSEQISDISREARALADKLESE-AQFDLKNAKDAKDAVEKA 1238
Cdd:COG4717   128 LPLYQE--LEALEAELAELPER----LEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEEL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1239 HQLAKsaidlqlkigtelrsevglELSHVKQSLGTVvQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLkkDAVA 1318
Cdd:COG4717   202 EELQQ-------------------RLAELEEELEEA-QEELEELEEELEQLENELEAAALEERLKEARLLLLIA--AALL 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1319 A----NERADELLKQITELSNSNGELFADFETEQELTEALLkraeQQQLEDIELLERAKAAHDKATKAveqgdntlkean 1394
Cdd:COG4717   260 AllglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL----GKEAEELQALPALEELEEEELEE------------ 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1395 ntYEKLAGFQSDVQRSsesaekalqtvpniekEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLK--YAEQASKDAE 1472
Cdd:COG4717   324 --LLAALGLPPDLSPE----------------ELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEE 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1473 LIRRKANETKvAARNLREEADQLNHRvkLTEMDIFKLEESSTKDDnlvDDAKRKVGQAKADTQEAQKQIEKANADLTAIK 1552
Cdd:COG4717   386 ELRAALEQAE-EYQELKEELEELEEQ--LEELLGELEELLEALDE---EELEEELEELEEELEELEEELEELREELAELE 459

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160 1553 DELENLKdiNTGDLDRLENRLATVEGEINRVnltgrIEKYREQRTIQKNLidkyDAELRELKDEVQ 1618
Cdd:COG4717   460 AELEQLE--EDGELAELLQELEELKAELREL-----AEEWAALKLALELL----EEAREEYREERL 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1186-1624 1.01e-13

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 76.65  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1186 LARAKEKSVEFGQQSEQISDISREARALADKLESEaqfdlknakdaKDAVEKAHQLAKsaidlqlkigtELRSEVGLELS 1265
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-----------REKAERYQALLK-----------EKREYEGYELL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1266 HVKQSLgtvvQTSKEALRKAnevydtaltlLNDVNRQ-TQPEIDISQLKKDAVAANERADELLKQITELSnsngelfadf 1344
Cdd:TIGR02169  230 KEKEAL----ERQKEAIERQ----------LASLEEElEKLTEEISELEKRLEEIEQLLEELNKKIKDLG---------- 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1345 ETEQ-ELTEALLK-RAEQQQLEDI--ELLERAKAAHDKATKAVEQGDNTLKEAnntyEKLAGFQSDVQRSSESAEKALQt 1420
Cdd:TIGR02169  286 EEEQlRVKEKIGElEAEIASLERSiaEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRDKLTEEYA- 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1421 vpNIEKEIqnaESLISQAEEaLDGANKNANEAKKNAQEAqlkyaeqaskdAELIRRKANETKVAARNLREEADQLNHRVK 1500
Cdd:TIGR02169  361 --ELKEEL---EDLRAELEE-VDKEFAETRDELKDYREK-----------LEKLKREINELKRELDRLQEELQRLSEELA 423

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1501 LTEMDIFKLEESSTKDDNLVDDAKRKVgqaKADTQEaqkqIEKANADLTAIKDELENLKDintgDLDRLENRLATVEGEI 1580
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEI---KKQEWK----LEQLAADLSKYEQELYDLKE----EYDRVEKELSKLQREL 492

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 665410160  1581 NRVnltgriEKyrEQRTIQKNLIDKYDAELrELKDEVQNI-GLIS 1624
Cdd:TIGR02169  493 AEA------EA--QARASEERVRGGRAVEE-VLKASIQGVhGTVA 528
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 743-791 4.89e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 65.07  E-value: 4.89e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  743 PCDCHGHADI---CDSETGRCICQHNTHGDNCDQCAKGFYGNALggTPNDCK 791
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS--QGGGCQ 50
PTZ00121 PTZ00121
MAEBL; Provisional
 1161-1635 5.29e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.79  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1161 DQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARAlADKLESEAQfdlkNAKDAKDAVEKAHQ 1240
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK-ADEAKKKAE----EAKKAEEAKKKAEE 1468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1241 lAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKdaVAAN 1320
Cdd:PTZ00121 1469 -AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEK 1545

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1321 ERADEL-----LKQITELSNSNGELFADFETEQELTEA-LLKRAEQQQLEDI-ELLERAKAAHDKATKAVEQGDNTLKEA 1393
Cdd:PTZ00121 1546 KKADELkkaeeLKKAEEKKKAEEAKKAEEDKNMALRKAeEAKKAEEARIEEVmKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1394 NNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGAN--KNANEAKKNAQEAQLKYAEQASKdA 1471
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKK-A 1704

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1472 ELIRRKANETKVAARNLREEadqlnhrvklTEMDIFKLEESSTKDdnlvDDAKRKVGQAKADTQEAQK-QIEKANADLTA 1550
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKA----------EEENKIKAEEAKKEA----EEDKKKAEEAKKDEEEKKKiAHLKKEEEKKA 1770

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1551 IKDELENLKDINTGDLDRLENRLATVEGEINRV--NLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGLISKALP 1628
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850


                  ....*..
gi 665410160 1629 DSCFSRN 1635
Cdd:PTZ00121 1851 KHKFNKN 1857
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 956-1002 9.14e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 64.30  E-value: 9.14e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665410160  956 CLCDPVGSYNSTCDRYSGQCHCRPGVMGQRCDQCENYFYGFSS--EGCK 1002
Cdd:cd00055     2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1347-1622 1.16e-12

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 72.38  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1347 EQELTEALLKRAEQQQLEDIELLERA-------KAAHDKAT-KAVEQGDNTLKEANntyEKLAGFQSDVQRSSESAEKAL 1418
Cdd:COG3064    10 AEAAAQERLEQAEAEKRAAAEAEQKAkeeaeeeRLAELEAKrQAEEEAREAKAEAE---QRAAELAAEAAKKLAEAEKAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1419 QTVpniEKEIQ-NAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKdaelirRKANETKVAArnlREEADQLNH 1497
Cdd:COG3064    87 AEA---EKKAAaEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRK-AEEEAK------RKAEEERKAA---EAEAAAKAE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1498 RVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVE 1577
Cdd:COG3064   154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 665410160 1578 GEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGL 1622
Cdd:COG3064   234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGL 278
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1290-1559 1.21e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 73.41  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1290 DTALTLLNdvnrQTQ---PEIDISQLKKDAV----AANERADELLKQITELSNsngelfadfeteqelTEALLKRAEQQq 1362
Cdd:COG4913   191 EKALRLLH----KTQsfkPIGDLDDFVREYMleepDTFEAADALVEHFDDLER---------------AHEALEDAREQ- 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1363 ledIELLERAKAAHDKATKAVEQGD--NTLKEANNTYEKlagfqsdvQRSSESAEKALQtvpNIEKEIQNAESLISQAEE 1440
Cdd:COG4913   251 ---IELLEPIRELAERYAAARERLAelEYLRAALRLWFA--------QRRLELLEAELE---ELRAELARLEAELERLEA 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1441 ALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDifkLEESSTKDDNLV 1520
Cdd:COG4913   317 RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAAALL 393

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 665410160 1521 DDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLK 1559
Cdd:COG4913   394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 461-511 1.33e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.53  E-value: 1.33e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410160   461 CGCDSGGSHqnTPACDTETGICFCKENVEGRRCNECKPGFFNLDKNNRFGC 511
Cdd:pfam00053    1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 744-790 2.13e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 63.14  E-value: 2.13e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 665410160   744 CDCHGHA---DICDSETGRCICQHNTHGDNCDQCAKGFYGNAlGGTPNDC 790
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1054-1620 2.90e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 71.87  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1054 YNLVQDAADLHRAklfNLSQTLDEIARTpvtnddefEAKLKAVQEKVAVLAQDARDNSGDGGQTYAEVIDDLHKHLDSVR 1133
Cdd:COG4913   290 LELLEAELEELRA---ELARLEAELERL--------EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1134 EHLVSADKFQADAN-------GEIDRARQNYTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDI 1206
Cdd:COG4913   359 RRRARLEALLAALGlplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1207 SREA----RALADKL---ESEAQF-----DLKnAKDAK--DAVEKA--------------HQLAKSAIDlQLKIGTELRS 1258
Cdd:COG4913   439 PARLlalrDALAEALgldEAELPFvgeliEVR-PEEERwrGAIERVlggfaltllvppehYAAALRWVN-RLHLRGRLVY 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1259 E-VGLELSH-------------------------VKQSLG---TVVQ-TSKEALRKanevYDTALTllndVNRQT-QP-- 1305
Cdd:COG4913   517 ErVRTGLPDperprldpdslagkldfkphpfrawLEAELGrrfDYVCvDSPEELRR----HPRAIT----RAGQVkGNgt 588

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1306 --EID------------------ISQLKKDAVAANERADELLKQITELSnsngelfADFETEQELTEALLKRAEQQQLE- 1364
Cdd:COG4913   589 rhEKDdrrrirsryvlgfdnrakLAALEAELAELEEELAEAEERLEALE-------AELDALQERREALQRLAEYSWDEi 661

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1365 DIELLERAKAAHDKATKAVEQGDNTLKEAnntYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDG 1444
Cdd:COG4913   662 DVASAEREIAELEAELERLDASSDDLAAL---EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1445 ANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNhrvklTEMDIFKLE---ESSTKDDNlVD 1521
Cdd:COG4913   739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE-----RAMRAFNREwpaETADLDAD-LE 812

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1522 DAkrkvgqakADTQEAQKQIEkaNADLTAIKDELENLKDINTGD-----LDRLENRLATVEGEINRVNLT-GRIEkYREQ 1595
Cdd:COG4913   813 SL--------PEYLALLDRLE--EDGLPEYEERFKELLNENSIEfvadlLSKLRRAIREIKERIDPLNDSlKRIP-FGPG 881

                         650       660
                  ....*....|....*....|....*
gi 665410160 1596 RTIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:COG4913   882 RYLRLEARPRPDPEVREFRQELRAV 906
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1407-1629 5.30e-12

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 69.55  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1407 VQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQlKYAEQASKDAELIRRKANETKVAAR 1486
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEELE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1487 NLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDintgdl 1566
Cdd:COG4372   105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE------ 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1567 DRLENRLATVEGEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGLISKALPD 1629
Cdd:COG4372   179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1287-1611 8.18e-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: 69.99  E-value: 8.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1287 EVYDTALTLLNDVNRQTQPEIDISQLKkdavAANERADELLKQITELS----NSNGELFADFEteqELTEALLKRAEQQQ 1362
Cdd:COG5185   223 EKAKEIINIEEALKGFQDPESELEDLA----QTSDKLEKLVEQNTDLRleklGENAESSKRLN---ENANNLIKQFENTK 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1363 lEDIEllERAKAAHDKatKAVEQGDNTLK--EANNTYE-KLAGFQSDVQRSSESAEKALQTVPNIEKEIQN------AES 1433
Cdd:COG5185   296 -EKIA--EYTKSIDIK--KATESLEEQLAaaEAEQELEeSKRETETGIQNLTAEIEQGQESLTENLEAIKEeienivGEV 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1434 LISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRR--KANETKVAarNLREEADQLNHRVKLTEMDIFKLEE 1511
Cdd:COG5185   371 ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtlKAADRQIE--ELQRQIEQATSSNEEVSKLLNELIS 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1512 SSTKDDNLVDDAKRKVGQAKAD--TQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRV----NL 1585
Cdd:COG5185   449 ELNKVMREADEESQSRLEEAYDeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVaeslKD 528

                         330       340
                  ....*....|....*....|....*....
gi 665410160 1586 TGRIEKY---REQRTIQKNLIDKYDAELR 1611
Cdd:COG5185   529 FMRARGYahiLALENLIPASELIQASNAK 557
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
414-458 9.44e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.17  E-value: 9.44e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160    414 CACDPVGSRSLQCNS-HGKCQCKPGVTGDKCDRCDNNYYQFGPHGC 458
Cdd:smart00180    1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1124-1500 1.19e-11

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: 69.98  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1124 DLHKHLDSVREHLVSADkFQADANgeidRARQNytiLDQITEnAKKELQQALDLLNDEGAQALARAKeksvEFGQQSEQI 1203
Cdd:COG3096   256 DLFKHLITEATNYVAAD-YMRHAN----ERREL---SERALE-LRRELFGARRQLAEEQYRLVEMAR----ELEELSARE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1204 SDISREARALADKLESeaqfdLKNAKDAKDAVEKaHQLAKSAIDLQLKIGTELRSEVGLELshvkqslgtvvQTSKEALR 1283
Cdd:COG3096   323 SDLEQDYQAASDHLNL-----VQTALRQQEKIER-YQEDLEELTERLEEQEEVVEEAAEQL-----------AEAEARLE 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1284 KANEVYDTALTLLNDVnrqtQPEIDISQLK----KDAVAANERADELLkQITELSNSN-GELFADFET-EQELTEALLKr 1357
Cdd:COG3096   386 AAEEEVDSLKSQLADY----QQALDVQQTRaiqyQQAVQALEKARALC-GLPDLTPENaEDYLAAFRAkEQQATEEVLE- 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1358 AEQQqledIELLERAKAAHDKATKAVeqgdntlkeanntyEKLAGfqsDVQRSS--ESAEKAL----------QTVPNIE 1425
Cdd:COG3096   460 LEQK----LSVADAARRQFEKAYELV--------------CKIAG---EVERSQawQTARELLrryrsqqalaQRLQQLR 518

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1426 KEIQNAESLISQ---AEEALDGANKNANEAKKNAQEAQLKYAEQaskDAELIR--RKANETKVAARNLREEADQLNHRVK 1500
Cdd:COG3096   519 AQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEELLAEL---EAQLEEleEQAAEAVEQRSELRQQLEQLRARIK 595
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 902-953 1.74e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.44  E-value: 1.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 665410160   902 CSCYEAGTEQDeqsitRCDQVTGQCQCKPNVIGRDCGECQPGYFNIRSGNGC 953
Cdd:pfam00053    1 CDCNPHGSLSD-----TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1253-1620 2.02e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 67.62  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1253 GTELRSEVG---LELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQ-TQPEIDISQLKKDAVAANERADELLK 1328
Cdd:COG4372     1 GDRLGEKVGkarLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREElEQAREELEQLEEELEQARSELEQLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1329 QITELsnsngelfadfetEQELTEALLKRAEQQqlediELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQ 1408
Cdd:COG4372    81 ELEEL-------------NEQLQAAQAELAQAQ-----EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1409 RSSESAEKALQtvpNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQL-KYAEQASKDAELIRRKANETKVAARN 1487
Cdd:COG4372   143 SEIAEREEELK---ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAnRNAEKEEELAEAEKLIESLPRELAEE 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1488 LREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADtQEAQKQIEKANADLTAIKDELENLKDINTGDLD 1567
Cdd:COG4372   220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL-AILVEKDTEEEELEIAALELEALEEAALELKLL 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1568 RLENRLATVEGEINRVNLTGRIEKyreqrTIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:COG4372   299 ALLLNLAALSLIGALEDALLAALL-----ELAKKLELALAILLAELADLLQLL 346
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 414-459 2.08e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 60.45  E-value: 2.08e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665410160  414 CACDPVGSRSLQCNSH-GKCQCKPGVTGDKCDRCDNNYYQF--GPHGCQ 459
Cdd:cd00055     2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 414-461 2.11e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.06  E-value: 2.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 665410160   414 CACDPVGSRSLQCNSH-GKCQCKPGVTGDKCDRCDNNYYQFGPHGCQQC 461
Cdd:pfam00053    1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1056-1620 2.93e-11

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: 68.56  E-value: 2.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1056 LVQDAADLHR--AKLFNLSQTLDEIA--RTPVTND-----DEFEAKLKAVQEkVAVLAQDARDNSGDGGQT---YAEVID 1123
Cdd:TIGR02169  324 LAKLEAEIDKllAEIEELEREIEEERkrRDKLTEEyaelkEELEDLRAELEE-VDKEFAETRDELKDYREKlekLKREIN 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1124 DLHKHLDSVREHLVSADKFQADANGEIDRARQNYTILDQITENAKKELQQAldllndegAQALARAKEKsveFGQQSEQI 1203
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--------EWKLEQLAAD---LSKYEQEL 471

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1204 SDISREARALADKLeSEAQFDLKNAKDAKDAVEKAHQLAKSAIDLqlkIGTELRSEVGL--ELSHVKQSLGTVVQTSKEA 1281
Cdd:TIGR02169  472 YDLKEEYDRVEKEL-SKLQRELAEAEAQARASEERVRGGRAVEEV---LKASIQGVHGTvaQLGSVGERYATAIEVAAGN 547

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1282 lRKANEVYDT------ALTLLNDV----------NRQTQPEIDISQLKKDAV---AAN---------------------- 1320
Cdd:TIGR02169  548 -RLNNVVVEDdavakeAIELLKRRkagratflplNKMRDERRDLSILSEDGVigfAVDlvefdpkyepafkyvfgdtlvv 626

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1321 ---ERADELLKQItELSNSNGELF---------------------ADFETEQELTEAL--LKRAE---QQQLEDIE-LLE 1370
Cdd:TIGR02169  627 ediEAARRLMGKY-RMVTLEGELFeksgamtggsraprggilfsrSEPAELQRLRERLegLKRELsslQSELRRIEnRLD 705

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1371 RAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTV----PNIEKEIQNAESLISQAEEAL---- 1442
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselKELEARIEELEEDLHKLEEALndle 785

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1443 ------------DGANK------------NANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAAR----NLREEADQ 1494
Cdd:TIGR02169  786 arlshsripeiqAELSKleeevsriearlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEkeieNLNGKKEE 865

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1495 LNHRVKLTEMDIFKLEES----STKDDNLVDD---AKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDI------ 1561
Cdd:TIGR02169  866 LEEELEELEAALRDLESRlgdlKKERDELEAQlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgedee 945

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410160  1562 ---NTGDLDRLENRLATVEGEINR---VNLtGRIEKYREQRTIQKNLIDKYD---AELRELKDEVQNI 1620
Cdd:TIGR02169  946 ipeEELSLEDVQAELQRVEEEIRAlepVNM-LAIQEYEEVLKRLDELKEKRAkleEERKAILERIEEY 1012
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1091-1618 3.54e-11

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: 68.61  E-value: 3.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1091 AKLKAVQEKVAVLAQDARDNSGdggqTYAEVIDDLHKHLDSVREHLVSADKFQAD-----------ANGEIDRARQNYTI 1159
Cdd:pfam15921  292 SQANSIQSQLEIIQEQARNQNS----MYMRQLSDLESTVSQLRSELREAKRMYEDkieelekqlvlANSELTEARTERDQ 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1160 LDQITENAKKELQQALdllndegAQALARAKEKSVEfGQQSEQISDISREARALADKLESEaqFDLKNAKdakdaVEKAH 1239
Cdd:pfam15921  368 FSQESGNLDDQLQKLL-------ADLHKREKELSLE-KEQNKRLWDRDTGNSITIDHLRRE--LDDRNME-----VQRLE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1240 QLAKS-AIDLQLKIGTELRSEVGLELSHVK-QSLGTVVQTSKEALRKA-NEVYDTALTLLNdvNRQTQPEIDIS-QLKKD 1315
Cdd:pfam15921  433 ALLKAmKSECQGQMERQMAAIQGKNESLEKvSSLTAQLESTKEMLRKVvEELTAKKMTLES--SERTVSDLTASlQEKER 510

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1316 AVAAN--------ERADELLKQITELSNSnGELFADFETEqelTEAL-LKRAEQQQL-----EDIELLERAKAAHDKATK 1381
Cdd:pfam15921  511 AIEATnaeitklrSRVDLKLQELQHLKNE-GDHLRNVQTE---CEALkLQMAEKDKVieilrQQIENMTQLVGQHGRTAG 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1382 AVEQGDNTL-KEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEiqnAESLISQAEEALDGANKNANEAKKNAQEAQ 1460
Cdd:pfam15921  587 AMQVEKAQLeKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE---KVKLVNAGSERLRAVKDIKQERDQLLNEVK 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1461 LKYAE--QASKDAELIRRkanetkvaarNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQ 1538
Cdd:pfam15921  664 TSRNElnSLSEDYEVLKR----------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1539 KQIEKANADLTAIKDELENLKDINTG----------DLDRLENRLATVEGEINRvnLTGRIEKYREQ-RTIQKNL----- 1602
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEAMTNankekhflkeEKNKLSQELSTVATEKNK--MAGELEVLRSQeRRLKEKVanmev 811

                          570
                   ....*....|....*..
gi 665410160  1603 -IDKYDAELRELKDEVQ 1618
Cdd:pfam15921  812 aLDKASLQFAECQDIIQ 828
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1116-1622 3.88e-11

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: 68.22  E-value: 3.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1116 QTYAEVIDDLHKHLDSVREhLVSADKF------------------QADANGEIdRARQNytildQITENAKKELQQALDL 1177
Cdd:pfam15921   81 EEYSHQVKDLQRRLNESNE-LHEKQKFylrqsvidlqtklqemqmERDAMADI-RRRES-----QSQEDLRNQLQNTVHE 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1178 LndEGAQALaraKEKSVE-FGQQSEQISDISREARALADKLESeAQFDLKNAKDAK----DAVEKAH-QLAKSAIDLQLK 1251
Cdd:pfam15921  154 L--EAAKCL---KEDMLEdSNTQIEQLRKMMLSHEGVLQEIRS-ILVDFEEASGKKiyehDSMSTMHfRSLGSAISKILR 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1252 igtelrsEVGLELSHVKqslGTV--VQTSKEALrKANEVYDTALTLLNDVNRQTQ----PEIDISQLKKDAVAANERADE 1325
Cdd:pfam15921  228 -------ELDTEISYLK---GRIfpVEDQLEAL-KSESQNKIELLLQQHQDRIEQliseHEVEITGLTEKASSARSQANS 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1326 LLKQ---ITELSNSNGELF----ADFET-----EQELTEAllKRAEQQQLEDIEllERAKAAHDKATKAVEQGDNTLKEA 1393
Cdd:pfam15921  297 IQSQleiIQEQARNQNSMYmrqlSDLEStvsqlRSELREA--KRMYEDKIEELE--KQLVLANSELTEARTERDQFSQES 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1394 NNTYEKLAGFQSDVQRSsesaEKALqtvpNIEKEiQN--------AESL-ISQAEEALDGANKNANEAkknaqEAQLKyA 1464
Cdd:pfam15921  373 GNLDDQLQKLLADLHKR----EKEL----SLEKE-QNkrlwdrdtGNSItIDHLRRELDDRNMEVQRL-----EALLK-A 437

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1465 EQASKDAELIRRKAnetKVAARNLR-EEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEK 1543
Cdd:pfam15921  438 MKSECQGQMERQMA---AIQGKNESlEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1544 ANADLTAIKD-------ELENLKdiNTGDldRLENrlATVEGEINRVNLTGR---IEKYREQ------------RT---I 1598
Cdd:pfam15921  515 TNAEITKLRSrvdlklqELQHLK--NEGD--HLRN--VQTECEALKLQMAEKdkvIEILRQQienmtqlvgqhgRTagaM 588

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....
gi 665410160  1599 Q--------------------KNLIDKYDAELRELKDEVQNIGL 1622
Cdd:pfam15921  589 QvekaqlekeindrrlelqefKILKDKKDAKIRELEARVSDLEL 632
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 847-897 7.25e-11

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 58.90  E-value: 7.25e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 665410160   847 CDCNGNVDPNavGNCNRTTGECLkCIHNTAGEHCDQCLSGHFGDPLALPHG 897
Cdd:pfam00053    1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1122-1620 7.53e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 67.25  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1122 IDDLhkhldsVREHLVsaDKFQADAngEIDRARQNYTILDQITENAKKELQQaLDLLND--EGAQALARAKEK------- 1192
Cdd:COG4913   209 LDDF------VREYML--EEPDTFE--AADALVEHFDDLERAHEALEDAREQ-IELLEPirELAERYAAARERlaeleyl 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1193 ----SVEFGQQS-----EQISDISREARALADKLEsEAQFDLKNAKDAKDAVEKAHQLA----KSAIDLQLKIGTELRSE 1259
Cdd:COG4913   278 raalRLWFAQRRlelleAELEELRAELARLEAELE-RLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEE 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1260 VGLELSHVKQ---SLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDisQLKKDAVAANERADELLKQITELSNS 1336
Cdd:COG4913   357 RERRRARLEAllaALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA--EAEAALRDLRRELRELEAEIASLERR 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1337 NG-------ELFADFETEQELTEA-------LLK-RAEQQQLED-IELLERAKA-------AH-DKATKAVEQGDNTLKE 1392
Cdd:COG4913   435 KSniparllALRDALAEALGLDEAelpfvgeLIEvRPEEERWRGaIERVLGGFAltllvppEHyAAALRWVNRLHLRGRL 514

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1393 annTYEKLAGFQSDVQRSSES----AEKaLQTVPN-----IEKEIQNAESLIS-QAEEALDGANKnA------------- 1449
Cdd:COG4913   515 ---VYERVRTGLPDPERPRLDpdslAGK-LDFKPHpfrawLEAELGRRFDYVCvDSPEELRRHPR-Aitragqvkgngtr 589

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1450 ------------------NEAKKNAQEAQLKYAEQASKDAELIRRKANEtkvAARNLREEADQLNHRVKLTEMDI----- 1506
Cdd:COG4913   590 hekddrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEA---ELDALQERREALQRLAEYSWDEIdvasa 666

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1507 -FKLEE------SSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDintgDLDRLENRLATVEgE 1579
Cdd:COG4913   667 eREIAEleaeleRLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAE-D 741

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665410160 1580 INRVNLTGRIEKYREQ-------RTIQKNL---IDKYDAELRELKDEVQNI 1620
Cdd:COG4913   742 LARLELRALLEERFAAalgdaveRELRENLeerIDALRARLNRAEEELERA 792
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 901-954 7.72e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 58.52  E-value: 7.72e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665410160  901 RCSCYEAGTEQDEqsitrCDQVTGQCQCKPNVIGRDCGECQPGYFNIRS-GNGCE 954
Cdd:cd00055     1 PCDCNGHGSLSGQ-----CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1088-1620 8.14e-11

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: 67.17  E-value: 8.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1088 EFEAKLKAVQEKVAVLAQDARDNSGDGGQTYAEV--IDDLHKHLDSVR-----EHLVSADKFQADANgEIDRarqnytIL 1160
Cdd:pfam12128  291 LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELeaLEDQHGAFLDADietaaADQEQLPSWQSELE-NLEE------RL 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1161 DQITENAKKeLQQALD----LLNDEGAQALARAKEKSvefGQQSEQISDISREARALADKLESEAQFDLKNAKdaKDAVE 1236
Cdd:pfam12128  364 KALTGKHQD-VTAKYNrrrsKIKEQNNRDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGK--LEFNE 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1237 KAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLnDVNRQTQPEidisQLKKDA 1316
Cdd:pfam12128  438 EEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA-RKRRDQASE----ALRQAS 512

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1317 VAANERADELLKQITELSNSNGELFADFETEQELTEALLKRaeqqqLEDIELLERAKAaHDKATKAVEQGDNTLKEANNT 1396
Cdd:pfam12128  513 RRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK-----VISPELLHRTDL-DPEVWDGSVGGELNLYGVKLD 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1397 YEKLagfqsDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKnaqeaQLKYAEQASKDAEL-IR 1475
Cdd:pfam12128  587 LKRI-----DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKNARLdLR 656

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1476 RKANE-----------TKVAARNLREEADQLNHRVKLTEMDI--FKLEESSTKDDN-LVDDAKRKVGQAKADTQEAQKQI 1541
Cdd:pfam12128  657 RLFDEkqsekdkknkaLAERKDSANERLNSLEAQLKQLDKKHqaWLEEQKEQKREArTEKQAYWQVVEGALDAQLALLKA 736

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1542 EKAnADLTAIKDELENLKDINTGDLDRL---ENRLATVEGEINrvNLTGRIEK--------------YREQRTIQKnliD 1604
Cdd:pfam12128  737 AIA-ARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIR--TLERKIERiavrrqevlryfdwYQETWLQRR---P 810

                          570
                   ....*....|....*.
gi 665410160  1605 KYDAELRELKDEVQNI 1620
Cdd:pfam12128  811 RLATQLSNIERAISEL 826
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
902-953 1.36e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 57.71  E-value: 1.36e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 665410160    902 CSCYEAGTEQDEqsitrCDQVTGQCQCKPNVIGRDCGECQPGYFNiRSGNGC 953
Cdd:smart00180    1 CDCDPGGSASGT-----CDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1073-1588 1.49e-10

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: 66.28  E-value: 1.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1073 QTLDEIARTPVtNDDEFEAKLKAVQ--EK------VAVLAQDARDNSgDGGQTYAEVIDDLHKHLDSVREHLVSADKfqa 1144
Cdd:pfam05483  225 QHLEEEYKKEI-NDKEKQVSLLLIQitEKenkmkdLTFLLEESRDKA-NQLEEKTKLQDENLKELIEKKDHLTKELE--- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1145 DANGEIDRARQNYTILDQITENAKKELQQaldLLNDEGAQALARAKEKSVefgqQSEQISDISREARALADKLESEAQfD 1224
Cdd:pfam05483  300 DIKMSLQRSMSTQKALEEDLQIATKTICQ---LTEEKEAQMEELNKAKAA----HSFVVTEFEATTCSLEELLRTEQQ-R 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1225 LKNAKDakdavekahQLAKSAIDLQLKIG-----TELRSEVGLELSHVKQSLG---TVVQTSKEALRKANEVYDTA--LT 1294
Cdd:pfam05483  372 LEKNED---------QLKIITMELQKKSSeleemTKFKNNKEVELEELKKILAedeKLLDEKKQFEKIAEELKGKEqeLI 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1295 LLNDVNRQTQPEIDIS----------QLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALL--------- 1355
Cdd:pfam05483  443 FLLQAREKEIHDLEIQltaiktseehYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLelkkhqedi 522

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1356 ---KRAEQQQLEDIELLERAKAAHDKATKAV-----EQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKE 1427
Cdd:pfam05483  523 incKKQEERMLKQIENLEEKEMNLRDELESVreefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1428 IQNAESLIS---QAEEAL----DGANK--NANEAKKNAQEAQLKYAEQasKDAELI---RRKANETKVAARNLREEADQ- 1494
Cdd:pfam05483  603 IENKNKNIEelhQENKALkkkgSAENKqlNAYEIKVNKLELELASAKQ--KFEEIIdnyQKEIEDKKISEEKLLEEVEKa 680

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1495 ---LNHRVKL-TEMD----------IFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKd 1560
Cdd:pfam05483  681 kaiADEAVKLqKEIDkrcqhkiaemVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLK- 759

                          570       580
                   ....*....|....*....|....*...
gi 665410160  1561 iNTGDLDRLENRLATVEGEINRVNLTGR 1588
Cdd:pfam05483  760 -KQLEIEKEEKEKLKMEAKENTAILKDK 786
PTZ00121 PTZ00121
MAEBL; Provisional
 1175-1543 1.50e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1175 LDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDlqlkigt 1254
Cdd:PTZ00121 1050 EDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKK------- 1122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1255 elRSEVGLELSHVKQSlgtvvqtskEALRKANEVYDTALTLLNDVNRQTQP--EIDISQLKKDAVAANE-RADELLKQIT 1331
Cdd:PTZ00121 1123 --KAEDARKAEEARKA---------EDARKAEEARKAEDAKRVEIARKAEDarKAEEARKAEDAKKAEAaRKAEEVRKAE 1191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1332 ELSNSN----GELFADFETEQELTEAllKRAEQ-QQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSD 1406
Cdd:PTZ00121 1192 ELRKAEdarkAEAARKAEEERKAEEA--RKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1407 VQRSSESAEKAlqtvpnieKEIQNAESlISQAEEALDGAN-KNANEAKKNAQEAqlKYAEQASKDAELIRRKANETK--- 1482
Cdd:PTZ00121 1270 AAIKAEEARKA--------DELKKAEE-KKKADEAKKAEEkKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKkka 1338

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410160 1483 --------VAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDA--KRKVGQAKADTQEAQKQIEK 1543
Cdd:PTZ00121 1339 eeakkaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeeKKKADEAKKKAEEDKKKADE 1409
growth_prot_Scy NF041483
polarized growth protein Scy;
1165-1545 2.13e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 66.00  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1165 ENAKKELQQALDLLNDEGAQALARAKEK-----SVEFGQQ--------------------------SEQISDISREARAL 1213
Cdd:NF041483  326 EALKAEAEQALADARAEAEKLVAEAAEKartvaAEDTAAQlakaartaeevltkasedakattraaAEEAERIRREAEAE 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1214 ADKLESEA--QFD-LKNAkdAKD--------AVE----------KAHQLAKSAIDLQLKIGTELRSEvglelshvkqslg 1272
Cdd:NF041483  406 ADRLRGEAadQAEqLKGA--AKDdtkeyrakTVElqeearrlrgEAEQLRAEAVAEGERIRGEARRE------------- 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1273 tVVQTSKEALRKANEvydtaltLLndvnrqTQPEIDISQLKKDAVA--------ANERADELLKQITE-LSNSNGELFAD 1343
Cdd:NF041483  471 -AVQQIEEAARTAEE-------LL------TKAKADADELRSTATAeservrteAIERATTLRRQAEEtLERTRAEAERL 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1344 FETEQELTEALLKRAEQQQLEDIELLERAKAA------------HDKATKAVEQGDNTLKEANNTYEKL---AGFQSDVQ 1408
Cdd:NF041483  537 RAEAEEQAEEVRAAAERAARELREETERAIAArqaeaaeeltrlHTEAEERLTAAEEALADARAEAERIrreAAEETERL 616

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1409 RsSESAE--KALQTVPNIEKE----------------------------IQNAESLISQAEEALDGANKNANE-AKKNAQ 1457
Cdd:NF041483  617 R-TEAAEriRTLQAQAEQEAErlrteaaadasaaraegenvavrlrseaAAEAERLKSEAQESADRVRAEAAAaAERVGT 695

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1458 EAQLKYAEqASKDAELIRRKANETKVAArnlREEADQLNHRVKltemdifklEESstkdDNLVDDAKRKVGQAKAdtqEA 1537
Cdd:NF041483  696 EAAEALAA-AQEEAARRRREAEETLGSA---RAEADQERERAR---------EQS----EELLASARKRVEEAQA---EA 755


                  ....*...
gi 665410160 1538 QKQIEKAN 1545
Cdd:NF041483  756 QRLVEEAD 763
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 461-512 2.38e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.36  E-value: 2.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  461 CGCDSGGSHQNTpaCDTETGICFCKENVEGRRCNECKPGFFNLDKnNRFGCT 512
Cdd:cd00055     2 CDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
461-511 3.10e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.94  E-value: 3.10e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 665410160    461 CGCDSGGSHQNTpaCDTETGICFCKENVEGRRCNECKPGFFNldkNNRFGC 511
Cdd:smart00180    1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1004-1046 4.30e-10

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 4.30e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 665410160  1004 CECDESGSKGFQCDQN-GQCPCNDNVEGRRCDRCKENKYDRHRG 1046
Cdd:pfam00053    1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
744-785 4.36e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.55  E-value: 4.36e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 665410160    744 CDCH--GHAD-ICDSETGRCICQHNTHGDNCDQCAKGFYGNALGG 785
Cdd:smart00180    1 CDCDpgGSASgTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
growth_prot_Scy NF041483
polarized growth protein Scy;
1139-1593 5.92e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 64.46  E-value: 5.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1139 ADKFQADANGEIDRARqnytildqitenakKELQQALDLLNDEGAQALARAKEKSV---------------EFGQQSEQI 1203
Cdd:NF041483  668 AERLKSEAQESADRVR--------------AEAAAAAERVGTEAAEALAAAQEEAArrrreaeetlgsaraEADQERERA 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1204 SDISREARALADKLESEAQfdlknaKDAKDAVEKAHQLAksaidlqlkigTELRSEVGLELSHVKQSL-GTVVQTSKE-- 1280
Cdd:NF041483  734 REQSEELLASARKRVEEAQ------AEAQRLVEEADRRA-----------TELVSAAEQTAQQVRDSVaGLQEQAEEEia 796

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1281 ALRKANEvydtalTLLNDVNRQTQPEIDisQLKKDAVAANERADELLKQITElsnsngelfadfeTEQELTEALLKRAEQ 1360
Cdd:NF041483  797 GLRSAAE------HAAERTRTEAQEEAD--RVRSDAYAERERASEDANRLRR-------------EAQEETEAAKALAER 855

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1361 QQLEDIELLERAKA-AHDKATKAVEQGDNTLKEA-NNTYEKLAGFQSDVQR-SSESAEKA--LQTVPNIEKEIQNAESlI 1435
Cdd:NF041483  856 TVSEAIAEAERLRSdASEYAQRVRTEASDTLASAeQDAARTRADAREDANRiRSDAAAQAdrLIGEATSEAERLTAEA-R 934

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1436 SQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANET----KVAARNLREEADqlnhRVKL-TEMDIFKLE 1510
Cdd:NF041483  935 AEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETvgsaQQHAERIRTEAE----RVKAeAAAEAERLR 1010

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1511 -ESSTKDDNLVDDAKRKVGQAKAD------------TQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRL---A 1574
Cdd:NF041483 1011 tEAREEADRTLDEARKDANKRRSEaaeqadtliteaAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIvaeA 1090

                         490
                  ....*....|....*....
gi 665410160 1575 TVEGeinrvnlTGRIEKYR 1593
Cdd:NF041483 1091 TVEG-------NSLVEKAR 1102
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1003-1050 6.38e-10

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 56.21  E-value: 6.38e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665410160 1003 PCECDESGSKGFQCDQ-NGQCPCNDNVEGRRCDRCKENKYDRHRGCIDC 1050
Cdd:cd00055     1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1424-1615 7.28e-10

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: 61.09  E-value: 7.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAEL-IRRKANETKV-AARNLREeADQLNHrvkl 1501
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVeARIKKYEEQLgNVRNNKE-YEALQK---- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1502 tEMDIfkleesstkddnlvddAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEIN 1581
Cdd:COG1579    97 -EIES----------------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 665410160 1582 RvnLTGRIEKYREqrTIQKNLIDKYDaELRELKD 1615
Cdd:COG1579   160 E--LEAEREELAA--KIPPELLALYE-RIRKRKN 188
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 1054-1638 7.29e-10

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: 64.30  E-value: 7.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1054 YNLVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEFEAKLKA------VQEKvAVLAQDARDNSGDGGQTYAEVIDDLHK 1127
Cdd:TIGR01612 1054 YNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHynfddfGKEE-NIKYADEINKIKDDIKNLDQKIDHHIK 1132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1128 HLDSVR---EHLVSADKFQA-------------DANGEIDRARQN-YTILDQ---ITENAKKELQQALDLLNDEgaQALA 1187
Cdd:TIGR01612 1133 ALEEIKkksENYIDEIKAQIndledvadkaisnDDPEEIEKKIENiVTKIDKkknIYDEIKKLLNEIAEIEKDK--TSLE 1210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1188 RAKEKSVEFGQQS-----EQISDISREARALADKLESEAQfDLknakdakDAVEKAHQLAKSAIDLQLKIGTELRSevgL 1262
Cdd:TIGR01612 1211 EVKGINLSYGKNLgklflEKIDEEKKKSEHMIKAMEAYIE-DL-------DEIKEKSPEIENEMGIEMDIKAEMET---F 1279

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1263 ELSHVKQSLGTVvqTSKEALRKANEVYDTALTLLNDVNRQTqpeiDISQLKK-------DAVAANERADELLKQIT---- 1331
Cdd:TIGR01612 1280 NISHDDDKDHHI--ISKKHDENISDIREKSLKIIEDFSEES----DINDIKKelqknllDAQKHNSDINLYLNEIAniyn 1353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1332 ---------------ELSNSNGELFADFETEQELTEALLKR-AEQQQLED----IELLERAKAAHDKATKAVEQGDNTLK 1391
Cdd:TIGR01612 1354 ilklnkikkiidevkEYTKEIEENNKNIKDELDKSEKLIKKiKDDINLEEckskIESTLDDKDIDECIKKIKELKNHILS 1433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1392 EA--NNTYEKLAG-FQSDVQ---RSSESAEKALQTVPNIEKEiqNAES----LISQAEEALDGANKNANEAKKNAQEAQL 1461
Cdd:TIGR01612 1434 EEsnIDTYFKNADeNNENVLllfKNIEMADNKSQHILKIKKD--NATNdhdfNINELKEHIDKSKGCKDEADKNAKAIEK 1511

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1462 -----------------KYAE--------QASKDAELIrrkANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKD 1516
Cdd:TIGR01612 1512 nkelfeqykkdvtellnKYSAlaiknkfaKTKKDSEII---IKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKN 1588

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1517 DnlvddakrKVGQAKADTQEAQKQIEKANADLTAIK-------DELENL-KDINTGDLDRLENRLAtvEGEINRVNLTGR 1588
Cdd:TIGR01612 1589 D--------KSNKAAIDIQLSLENFENKFLKISDIKkkindclKETESIeKKISSFSIDSQDTELK--ENGDNLNSLQEF 1658

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160  1589 IEKYREQRT---IQKNLIDKYDAELRELKDEVQN------IGLISKALPDSCFSRNRLE 1638
Cdd:TIGR01612 1659 LESLKDQKKnieDKKKELDELDSEIEKIEIDVDQhkknyeIGIIEKIKEIAIANKEEIE 1717
mukB PRK04863
chromosome partition protein MukB;
1124-1582 7.55e-10

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 64.21  E-value: 7.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1124 DLHKHLDSVREHLVSADkFQADANgEIDRARQNYTILDQITENAKKEL---QQALDLLNDEgAQALARAkEKSVEfgQQS 1200
Cdd:PRK04863  257 DLFKHLITESTNYVAAD-YMRHAN-ERRVHLEEALELRRELYTSRRQLaaeQYRLVEMARE-LAELNEA-ESDLE--QDY 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1201 EQISD---ISREARALADKLEsEAQFDLKnakdakdavEKAHQLAKSAidlqlkigtELRSEVGLElshvkqslgtvVQT 1277
Cdd:PRK04863  331 QAASDhlnLVQTALRQQEKIE-RYQADLE---------ELEERLEEQN---------EVVEEADEQ-----------QEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1278 SKEALRKANEVYDTALTLLNDVnrqtQPEIDISQLK----KDAVAANERADELLkQITELSNSN-GELFADFET-EQELT 1351
Cdd:PRK04863  381 NEARAEAAEEEVDELKSQLADY----QQALDVQQTRaiqyQQAVQALERAKQLC-GLPDLTADNaEDWLEEFQAkEQEAT 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1352 EALLKrAEQQqledIELLERAKAAHDKATKAVEQ--GDNTLKEANNTyeklagFQSDVQRSSEsaEKAL-QTVPNIEKEI 1428
Cdd:PRK04863  456 EELLS-LEQK----LSVAQAAHSQFEQAYQLVRKiaGEVSRSEAWDV------ARELLRRLRE--QRHLaEQLQQLRMRL 522

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1429 QNAE-SLISQ--AEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELirrkanetKVAARNLREEADQLNHRVKLTEMD 1505
Cdd:PRK04863  523 SELEqRLRQQqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL--------SESVSEARERRMALRQQLEQLQAR 594

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160 1506 IFKLEESSTKDDNLvDDAKRKVGQAKADTQEAQKQIEkanadlTAIKDELENLKDInTGDLDRLENRLATVEGEINR 1582
Cdd:PRK04863  595 IQRLAARAPAWLAA-QDALARLREQSGEEFEDSQDVT------EYMQQLLEREREL-TVERDELAARKQALDEEIER 663
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1036-1404 7.93e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 7.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1036 CKENKYDRHRGCIDC--PDCYNLVQDAADLhRAKLFNLSQTLDEIARTPVTNDDEF---EAKLKAVQEKVAVLAQDARDN 1110
Cdd:TIGR02168  674 ERRREIEELEEKIEEleEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1111 SGDGGQtYAEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNytiLDQITEnAKKELQQALDLLNDEGAQA----- 1185
Cdd:TIGR02168  753 SKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---LKALRE-ALDELRAELTLLNEEAANLrerle 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1186 --LARAKEKSVEFGQQSEQISDISREARALADKLES------EAQFDLKNAKDAKDAVEKAHQLAKSA-IDLQLKIGtEL 1256
Cdd:TIGR02168  828 slERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleelieELESELEALLNERASLEEALALLRSElEELSEELR-EL 906

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1257 RSEVGlELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAAN--ERADELLKQITELS 1334
Cdd:TIGR02168  907 ESKRS-ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEarRRLKRLENKIKELG 985

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410160  1335 NSNGELFADFETEQELTEALLKraeqqQLEDI----ELLERAKAAHDKATKaveqgdNTLKEannTYEKL-AGFQ 1404
Cdd:TIGR02168  986 PVNLAAIEEYEELKERYDFLTA-----QKEDLteakETLEEAIEEIDREAR------ERFKD---TFDQVnENFQ 1046
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1054-1636 1.37e-09

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 63.00  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1054 YNLVQDAADLHRAKLFNLSQTLDEIAR---------TPVTNDDEFEAKLKAVQEKVAVLAQDA--------RDNSGDGGQ 1116
Cdd:PRK01156  227 YNNAMDDYNNLKSALNELSSLEDMKNRyeseiktaeSDLSMELEKNNYYKELEERHMKIINDPvyknrnyiNDYFKYKND 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1117 --TYAEVIDDLHKHLDSVREHLVSADKFQADangeidraRQNYTILDQITENAKKELqqaLDLLNDEgaqalarakEKSV 1194
Cdd:PRK01156  307 ieNKKQILSNIDAEINKYHAIIKKLSVLQKD--------YNDYIKKKSRYDDLNNQI---LELEGYE---------MDYN 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1195 EFGQQSEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDlqlkigtelrsEVGLELSHVKQSLGTV 1274
Cdd:PRK01156  367 SYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ-----------DISSKVSSLNQRIRAL 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1275 VQTSKEALRKAN--------EVYDTAL------TLLNDVNRQ-TQPEIDISQLKKDAVAANERADELLKQITELsnsNGE 1339
Cdd:PRK01156  436 RENLDELSRNMEmlngqsvcPVCGTTLgeeksnHIINHYNEKkSRLEEKIREIEIEVKDIDEKIVDLKKRKEYL---ESE 512

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1340 LFADFETEQELTEALlkraeQQQLEDIEL-LERAKAAHDKATKAVEQgDNTLKeanntyeklagfQSDVQRSSESAEKAL 1418
Cdd:PRK01156  513 EINKSINEYNKIESA-----RADLEDIKIkINELKDKHDKYEEIKNR-YKSLK------------LEDLDSKRTSWLNAL 574

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1419 QTVPNIEkeiqnAESLISQAEEAldgaNKNANEAKKNAQEAQLKYAEQASKDAELIRRKANEtkvaARNLREEADQLNHR 1498
Cdd:PRK01156  575 AVISLID-----IETNRSRSNEI----KKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE----ANNLNNKYNEIQEN 641

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1499 VKLTEM---DIFKLEESSTKDDNLVDDAKR---KVGQAKADTQEAQKQIEKANADLTaikdELENLKDINTGDLDRLENR 1572
Cdd:PRK01156  642 KILIEKlrgKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAKANRA----RLESTIEILRTRINELSDR 717

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160 1573 LAtvegEINRvnltgRIEKyreQRTIQKNLIDKydAELREL--KDEVQNIglISKALPDSCFSRNR 1636
Cdd:PRK01156  718 IN----DINE-----TLES---MKKIKKAIGDL--KRLREAfdKSGVPAM--IRKSASQAMTSLTR 767
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
1116-1558 1.43e-09

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 62.62  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1116 QTYAEVIDDLHKHLDSVREHLvsadkfqADANGEIDRARQnytiLDQITENAKKELQQALDLLNDEGAQAlARAKEKSVE 1195
Cdd:COG5278    79 EPYEEARAEIDELLAELRSLT-------ADNPEQQARLDE----LEALIDQWLAELEQVIALRRAGGLEA-ALALVRSGE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1196 FGQQSEQISDISREARALADKLES----EAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQSL 1271
Cdd:COG5278   147 GKALMDEIRARLLLLALALAALLLaaaaLLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAAL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1272 GTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELT 1351
Cdd:COG5278   227 AALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELEL 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1352 EALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNA 1431
Cdd:COG5278   307 LLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1432 ESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEE 1511
Cdd:COG5278   387 AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAE 466

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 665410160 1512 SSTKDDNLVDDAKRKVGQAkadTQEAQKQIEKANADLTAIKDELENL 1558
Cdd:COG5278   467 ELAAVAALAALAAAAAALA---EAEAAAALAAAAALSLALALAALLL 510
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1415-1584 1.50e-09

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 62.74  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1415 EKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQlKYAEQASKDAEL--IRRK------ANETKVAAR 1486
Cdd:pfam05701   45 EKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQ-TEEAQAKQDSELakLRVEemeqgiADEASVAAK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1487 NLREEADQlNHRVKLTEMDIFKLE-ESSTKD-DNLV---DDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENL--- 1558
Cdd:pfam05701  124 AQLEVAKA-RHAAAVAELKSVKEElESLRKEyASLVserDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAhaa 202

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 665410160  1559 ------KDIN---TGDLDRL--ENRLATVEGEINRVN 1584
Cdd:pfam05701  203 hleaeeHRIGaalAREQDKLnwEKELKQAEEELQRLN 239
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1345-1605 1.53e-09

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.79  E-value: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1345 ETEQELTEALLKR-AEQQQLEDIEllERAKAAhdKATKAVEQGDntlKEANntyeklagfqsdvQRSSESAEKalqtvpn 1423
Cdd:TIGR02794   72 KLEQQAEEAEKQRaAEQARQKELE--QRAAAE--KAAKQAEQAA---KQAE-------------EKQKQAEEA------- 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1424 ieKEIQNAESLisQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKA-NETKVAArnlreEADQlnhrvklt 1502
Cdd:TIGR02794  125 --KAKQAAEAK--AKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeAEAKAKA-----EAEA-------- 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1503 emdifKLEESSTKDDNLVDDAKRKVgQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLEN--RLATVEGEI 1580
Cdd:TIGR02794  188 -----KAKAEEAKAKAEAAKAKAAA-EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGgaRGAAAGSEV 261

                          250       260
                   ....*....|....*....|....*
gi 665410160  1581 NRvnLTGRIekyreQRTIQKNLIDK 1605
Cdd:TIGR02794  262 DK--YAAII-----QQAIQQNLYDD 279
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1375-1582 1.67e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 61.77  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1375 AHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKK 1454
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1455 NAQE--AQLKYAEQ--ASKD-AELIRRKANETKVAARNlREEADQLNhrvkltemdifkleesstkddnlvdDAKRKVGQ 1529
Cdd:COG3883    94 ALYRsgGSVSYLDVllGSESfSDFLDRLSALSKIADAD-ADLLEELK-------------------------ADKAELEA 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1530 AKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINR 1582
Cdd:COG3883   148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1174-1446 2.30e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 61.38  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1174 ALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLEsEAQFDLKNAKDAKDAVEKAHQLAKSAID-LQLKI 1252
Cdd:COG3883     3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAeAEAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1253 gTELRSEVGLELSHVKQSLGTVvqTSKEALRKANEVYD--TALTLLNDVNRQTQPEID-ISQLKKDAVAANERADELLKQ 1329
Cdd:COG3883    82 -EERREELGERARALYRSGGSV--SYLDVLLGSESFSDflDRLSALSKIADADADLLEeLKADKAELEAKKAELEAKLAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1330 ITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQR 1409
Cdd:COG3883   159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 665410160 1410 SSESAEKALQTVPNIEKEIQNAESLISQAEEALDGAN 1446
Cdd:COG3883   239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAG 275
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1160-1620 2.63e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 61.96  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1160 LDQITENAKKELQQALDLLNDEGAQAlaraKEKSVEFGQQSEQISDISREARALADKLEseaqfDLKNAKDA---KDAVE 1236
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQL----SEKQKELEQNNKKIKELEKQLNQLKSEIS-----DLNNQKEQdwnKELKS 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1237 KAHQLAKSAIDLQLKIgtelrSEVGLELSHVKQSLgTVVQTSKEALRKANEVYDTALTllndvnrqtQPEIDISQLKKDA 1316
Cdd:TIGR04523  315 ELKNQEKKLEEIQNQI-----SQNNKIISQLNEQI-SQLKKELTNSESENSEKQRELE---------EKQNEIEKLKKEN 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1317 vaaneraDELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERakaaHDKATKAVEQGDNTLKEANNT 1396
Cdd:TIGR04523  380 -------QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE----IERLKETIIKNNSEIKDLTNQ 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1397 -------YEKLAGFQSDVQRS----SESAEKALQTVPNIEKEIQNAESLI-------SQAEEALDGANKNANEAKKNAQE 1458
Cdd:TIGR04523  449 dsvkeliIKNLDNTRESLETQlkvlSRSINKIKQNLEQKQKELKSKEKELkklneekKELEEKVKDLTKKISSLKEKIEK 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1459 AQLKYAEQASK----DAELIRRKANETKvaaRNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDdakrkvgQAKADT 1534
Cdd:TIGR04523  529 LESEKKEKESKisdlEDELNKDDFELKK---ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-------QKEKEK 598

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1535 QEAQKQIEKANADLTAIKDELENLK----DINTgDLDRLENRLATVEGEINRVNLTgrIEKYREqrtiQKNLIDKYDAEL 1610
Cdd:TIGR04523  599 KDLIKEIEEKEKKISSLEKELEKAKkeneKLSS-IIKNIKSKKNKLKQEVKQIKET--IKEIRN----KWPEIIKKIKES 671

                          490
                   ....*....|
gi 665410160  1611 RELKDEVQNI 1620
Cdd:TIGR04523  672 KTKIDDIIEL 681
growth_prot_Scy NF041483
polarized growth protein Scy;
1091-1548 4.45e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 61.77  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1091 AKLKAVQEKVAVLAQDARdnsgdggqTYAEVIDDLHKHL-DSVREHLVSADKFQADANGEIDRAR-QNYTILDQITENAK 1168
Cdd:NF041483  354 ARTVAAEDTAAQLAKAAR--------TAEEVLTKASEDAkATTRAAAEEAERIRREAEAEADRLRgEAADQAEQLKGAAK 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1169 KELQQAldllndegaqalaRAKekSVEFgqQSEqisdiSREARALADKLESEA--QFDLKNAKDAKDAVEKAHQLAKSAI 1246
Cdd:NF041483  426 DDTKEY-------------RAK--TVEL--QEE-----ARRLRGEAEQLRAEAvaEGERIRGEARREAVQQIEEAARTAE 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1247 DLQLKIGT---ELRSEVGLELSHV------------KQSLGTVVQTSKEALRKANEVYDTALTLlndvnrQTQPEIDISQ 1311
Cdd:NF041483  484 ELLTKAKAdadELRSTATAESERVrteaierattlrRQAEETLERTRAEAERLRAEAEEQAEEV------RAAAERAARE 557

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1312 LKKD---AVAAN--ERADELLKQITE-----------LSNSNGELF-----ADFETEQELTEALLK-RAEQQQLE-DIEL 1368
Cdd:NF041483  558 LREEterAIAARqaEAAEELTRLHTEaeerltaaeeaLADARAEAErirreAAEETERLRTEAAERiRTLQAQAEqEAER 637

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1369 LeRAKAAHDkATKAVEQGDNTL----KEANNTYEKLagfQSDVQrssESAEKalqtvpnIEKEIQNA-ESLISQAEEALD 1443
Cdd:NF041483  638 L-RTEAAAD-ASAARAEGENVAvrlrSEAAAEAERL---KSEAQ---ESADR-------VRAEAAAAaERVGTEAAEALA 702

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1444 GANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVkltemdifkLEESSTKDDNLVDDA 1523
Cdd:NF041483  703 AAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRL---------VEEADRRATELVSAA 773

                         490       500
                  ....*....|....*....|....*
gi 665410160 1524 KRKVGQAKADTQEAQKQIEKANADL 1548
Cdd:NF041483  774 EQTAQQVRDSVAGLQEQAEEEIAGL 798
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1154-1562 5.07e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 61.19  E-value: 5.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1154 RQNYTILDQIT--ENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDIsreaRALADKLESEAQfDLKNAKDA 1231
Cdd:TIGR04523  377 KENQSYKQEIKnlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL----KETIIKNNSEIK-DLTNQDSV 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1232 KDAVEKAHQLAKSAIDLQLKigtelrsEVGLELSHVKQSLGtvvQTSKEALRKANEvydtaLTLLNDVNRQTQPEIdiSQ 1311
Cdd:TIGR04523  452 KELIIKNLDNTRESLETQLK-------VLSRSINKIKQNLE---QKQKELKSKEKE-----LKKLNEEKKELEEKV--KD 514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1312 LKKDAVAANERADELLKQITELSNSNGELFADFET-EQELTEALLKRAEQQQLEDIELLERakaahdkatkaveqgDNTL 1390
Cdd:TIGR04523  515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEIDEKNKEIEELKQ---------------TQKS 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1391 KEANNT--YEKLAGFQSDVQrssesaekalqtvpNIEKEIQNAESLISQAEEALDGA---NKNANEAKKNAQEAQLKYAE 1465
Cdd:TIGR04523  580 LKKKQEekQELIDQKEKEKK--------------DLIKEIEEKEKKISSLEKELEKAkkeNEKLSSIIKNIKSKKNKLKQ 645

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1466 QAskdaELIRRKANETKVAARNLREEADQLNHRV-KLTE-MDIFKLEESSTKDDNLvddaKRKVGQAKADT-QEAQKQIE 1542
Cdd:TIGR04523  646 EV----KQIKETIKEIRNKWPEIIKKIKESKTKIdDIIElMKDWLKELSLHYKKYI----TRMIRIKDLPKlEEKYKEIE 717

                          410       420
                   ....*....|....*....|.
gi 665410160  1543 KANADLTAIKDELENL-KDIN 1562
Cdd:TIGR04523  718 KELKKLDEFSKELENIiKNFN 738
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1004-1047 5.13e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 5.13e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 665410160   1004 CECDESGSKGFQCDQ-NGQCPCNDNVEGRRCDRCKENKYDRH-RGC 1047
Cdd:smart00180    1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGpPGC 46
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1309-1495 5.86e-09

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 59.15  E-value: 5.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1309 ISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQEL------------TEALLKRAEQQQLEDI----ELLERA 1372
Cdd:COG1340    73 VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLrkeierlewrqqTEVLSPEEEKELVEKIkeleKELEKA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1373 KAAHDKATKaveqgdntLKEANNTYEKLagfqsdvqrsSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEA 1452
Cdd:COG1340   153 KKALEKNEK--------LKELRAELKEL----------RKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 665410160 1453 KKNAQEAQLKyaeqaskdAELIRRKANETKVAARNLREEADQL 1495
Cdd:COG1340   215 HKEIVEAQEK--------ADELHEEIIELQKELRELRKELKKL 249
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 846-893 6.56e-09

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.13  E-value: 6.56e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 665410160  846 SCDCNGNVDPNavGNCNRTTGECLkCIHNTAGEHCDQCLSGHFGDPLA 893
Cdd:cd00055     1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1345-1619 8.16e-09

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: 60.76  E-value: 8.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1345 ETEQELTEALLKRAEQQQLEdiELLERAKAAHDkatKAVEQGDNTLKEANNTYEKLAGFQsdvqrssESAEKALQTVPNI 1424
Cdd:pfam02463  181 ETENLAELIIDLEELKLQEL--KLKEQAKKALE---YYQLKEKLELEEEYLLYLDYLKLN-------EERIDLLQELLRD 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1425 EKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEM 1504
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1505 DIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVN 1584
Cdd:pfam02463  329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 665410160  1585 LtgRIEKYREQRTIQKNLIDKYDAELRELKDEVQN 1619
Cdd:pfam02463  409 L--LLELARQLEDLLKEEKKEELEILEEEEESIEL 441
growth_prot_Scy NF041483
polarized growth protein Scy;
1134-1572 8.67e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 60.61  E-value: 8.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1134 EHLVSADKFQADANGEIDR----ARQNYTILDQITENAKKELQQALDLLNDEGAQALArakeksvefGQQS--EQISDIS 1207
Cdd:NF041483  739 ELLASARKRVEEAQAEAQRlveeADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIA---------GLRSaaEHAAERT 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1208 R-EARALADKLESEAQFDLKNA--------KDAKDAVEKAHQLAKSAIDLQLKIGTELRSEvglelshvkqslgtvvqTS 1278
Cdd:NF041483  810 RtEAQEEADRVRSDAYAERERAsedanrlrREAQEETEAAKALAERTVSEAIAEAERLRSD-----------------AS 872

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1279 KEALRKANEVYDTALTLLNDVNR-QTQPEIDISQLKKDAVAaneRADELlkqITElsnsngelfADFETEQELTEAllkR 1357
Cdd:NF041483  873 EYAQRVRTEASDTLASAEQDAARtRADAREDANRIRSDAAA---QADRL---IGE---------ATSEAERLTAEA---R 934

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1358 AEQQQLEDiellERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSD-VQRSSESAEKALQTVPNIEKEIQ-NAESLI 1435
Cdd:NF041483  935 AEAERLRD----EARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAEtVGSAQQHAERIRTEAERVKAEAAaEAERLR 1010

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1436 SQAEEAldgANKNANEAKKNAQEAQLKYAEQASkdaelirRKANETKVAARNLREEADQLNHRVKLtemdifkleESSTK 1515
Cdd:NF041483 1011 TEAREE---ADRTLDEARKDANKRRSEAAEQAD-------TLITEAAAEADQLTAKAQEEALRTTT---------EAEAQ 1071

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1516 DDNLVDDAKRKVGQAKAD-TQEAQKQIEKANADL-----------TAIKDELENLKDINTGDLDRLENR 1572
Cdd:NF041483 1072 ADTMVGAARKEAERIVAEaTVEGNSLVEKARTDAdellvgarrdaTAIRERAEELRDRITGEIEELHER 1140
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1280-1530 1.08e-08

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


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 57.81  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1280 EALRKANE-VYDTALTLLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSnsngelfADFETEQELTEALLKRA 1358
Cdd:pfam06008   12 PAPYKINYnLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTL-------AKAQQVNAESERTLGHA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1359 EqqqlediELLERAKAAHDKATKAVEQGDNTLKEANNTYEklagfqSDVQRSSESAEKALQTVP--NIEKEIQNAESLIS 1436
Cdd:pfam06008   85 K-------ELAEAIKNLIDNIKEINEKVATLGENDFALPS------SDLSRMLAEAQRMLGEIRsrDFGTQLQNAEAELK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1437 QAEEALDGANK------NANEAKKNA-------QEAQLKYAEQASKDAELIRRKANETKVA-ARNLREeadqLNHRVKLT 1502
Cdd:pfam06008  152 AAQDLLSRIQTwfqspqEENKALANAlrdslaeYEAKLSDLRELLREAAAKTRDANRLNLAnQANLRE----FQRKKEEV 227

                          250       260
                   ....*....|....*....|....*...
gi 665410160  1503 EMDIFKLEESSTKDDNLVDDAKRKVGQA 1530
Cdd:pfam06008  228 SEQKNQLEETLKTARDSLDAANLLLQEI 255
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1159-1621 1.57e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.40  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1159 ILDQITENAKKEL---QQALDLLNdegAQALARAKEKSVEFGQQSEQISDISREARALADKLEsEAQFDLKNAKDAKDAV 1235
Cdd:COG4717    46 MLLERLEKEADELfkpQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1236 EKAHQLAKSAIDLQlkigtELRSEvgleLSHVKQSLgtvvqtskEALRKANEVYDTALTllndvnrqtqpeiDISQLKKD 1315
Cdd:COG4717   122 EKLLQLLPLYQELE-----ALEAE----LAELPERL--------EELEERLEELRELEE-------------ELEELEAE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1316 AVAANERADELLKQITelsnsngelfadFETEQELTEALLKRAE-QQQLEDIE-LLERAKAAHDKATKAVEQGDNTLkEA 1393
Cdd:COG4717   172 LAELQEELEELLEQLS------------LATEEELQDLAEELEElQQRLAELEeELEEAQEELEELEEELEQLENEL-EA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1394 NNTYEKL---------AGFQSDVQRSSESAEKALQTVPNI------------EKEIQNAESLISQAEEALDGANKNANEA 1452
Cdd:COG4717   239 AALEERLkearlllliAAALLALLGLGGSLLSLILTIAGVlflvlgllallfLLLAREKASLGKEAEELQALPALEELEE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1453 KK-NAQEAQLKYAEQASKD--AELIRR--KANETKVAARNLREEADQLNHRVKLTEMdifkLEESSTKDDnlvdDAKRKV 1527
Cdd:COG4717   319 EElEELLAALGLPPDLSPEelLELLDRieELQELLREAEELEEELQLEELEQEIAAL----LAEAGVEDE----EELRAA 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1528 GQAKADTQEAQKQIEKANADLTAIKDELENLKDinTGDLDRLENRLATVEGEINRvnLTGRIEKYREqrtiqknlidkyd 1607
Cdd:COG4717   391 LEQAEEYQELKEELEELEEQLEELLGELEELLE--ALDEEELEEELEELEEELEE--LEEELEELRE------------- 453

                         490
                  ....*....|....
gi 665410160 1608 aELRELKDEVQNIG 1621
Cdd:COG4717   454 -ELAELEAELEQLE 466
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1280-1597 1.60e-08

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 59.97  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1280 EALRKANEVYDTALTLLNDVNRQTQpeidisQLKKDAVAANERADELLKQITELSnsngeLFADfETEQELTEALlkRAE 1359
Cdd:COG3096   836 AELAALRQRRSELERELAQHRAQEQ------QLRQQLDQLKEQLQLLNKLLPQAN-----LLAD-ETLADRLEEL--REE 901

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1360 QQQLEDIElleRAKAAHDKATKAVEQGDNTLKEANNTYEKLagfQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAE 1439
Cdd:COG3096   902 LDAAQEAQ---AFIQQHGKALAQLEPLVAVLQSDPEQFEQL---QADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDA 975

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1440 EALDGANKNANEAKKnaqeAQLKYAEQAskdaeliRRKANEtkvAARNLREEADQLNHRvkLTEMDifkleeSSTkddnl 1519
Cdd:COG3096   976 VGLLGENSDLNEKLR----ARLEQAEEA-------RREARE---QLRQAQAQYSQYNQV--LASLK------SSR----- 1028

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1520 vddakrkvgQAKADT-QEAQKQIEK------ANADLTAI--KDELENLKDINTGDLDRLENRLATVEGEINrvNLTGRI- 1589
Cdd:COG3096  1029 ---------DAKQQTlQELEQELEElgvqadAEAEERARirRDELHEELSQNRSRRSQLEKQLTRCEAEMD--SLQKRLr 1097

                         330
                  ....*....|.
gi 665410160 1590 ---EKYREQRT 1597
Cdd:COG3096  1098 kaeRDYKQERE 1108
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1115-1617 1.64e-08

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: 59.68  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1115 GQTYAEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNYTILDQI-TENAKKELQQALDLLNDEG---AQALARAK 1190
Cdd:TIGR00606  463 LQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKAdLDRKLRKLDQEMEQLNHHTttrTQMEMLTK 542

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1191 EKSVEFGQQSEQISDISREARALADKLESEAQFD------LKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGLEL 1264
Cdd:TIGR00606  543 DKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEdwlhskSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1265 SHVK--------QSLGTVVQTSKEALRKANE----------VYDTALTLLNDVNRQTQPEIDisqlkkdavaaneRADEL 1326
Cdd:TIGR00606  623 SYEDklfdvcgsQDEESDLERLKEEIEKSSKqramlagataVYSQFITQLTDENQSCCPVCQ-------------RVFQT 689

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1327 LKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEAN-------NTYEK 1399
Cdd:TIGR00606  690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNrdiqrlkNDIEE 769

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1400 LAGFQSDVQRSSESAEKALQTVPNIEK---EIQNAESLISQAEEALDGAN--KNANEAKKNAQEAQLKYAEQASKdAELI 1474
Cdd:TIGR00606  770 QETLLGTIMPEEESAKVCLTDVTIMERfqmELKDVERKIAQQAAKLQGSDldRTVQQVNQEKQEKQHELDTVVSK-IELN 848

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1475 RRKANETKVAARNLREEADQL-NHRVKLTE--MDIFKLEESSTKDDNLVDDAKRKVGQAK-----------ADTQEAQKQ 1540
Cdd:TIGR00606  849 RKLIQDQQEQIQHLKSKTNELkSEKLQIGTnlQRRQQFEEQLVELSTEVQSLIREIKDAKeqdspletfleKDQQEKEEL 928

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1541 I-------EKANADLTAIKDELEN----LKDINTGDLDRLENRLATVEGEINRVNLT-----GRIEKYREQRTIQKNLID 1604
Cdd:TIGR00606  929 IssketsnKKAQDKVNDIKEKVKNihgyMKDIENKIQDGKDDYLKQKETELNTVNAQleeceKHQEKINEDMRLMRQDID 1008

                          570
                   ....*....|...
gi 665410160  1605 KYDAELRELKDEV 1617
Cdd:TIGR00606 1009 TQKIQERWLQDNL 1021
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1372-1624 1.76e-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: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1372 AKAAHDKATKAVEQgdntLKEANNTYEKLAGFQSDVQRSSESAEKALQtvpNIEKEIQNAESLISQAEEALDGANKNANE 1451
Cdd:COG4942    15 AAAQADAAAEAEAE----LEQLQQEIAELEKELAALKKEEKALLKQLA---ALERRIAALARRIRALEQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1452 AKKNAQEAQLKYAEQASKDAELIR---RKANETKVAARNLREEADQLNHRVKLtemdifkLEESSTKDDNLVDDAKRK-- 1526
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQY-------LKYLAPARREQAEELRADla 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1527 -VGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINrvnltgriEKYREQRTIQkNLIDK 1605
Cdd:COG4942   161 eLAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA--------ELQQEAEELE-ALIAR 231

                         250
                  ....*....|....*....
gi 665410160 1606 YDAELRELKDEVQNIGLIS 1624
Cdd:COG4942   232 LEAEAAAAAERTPAAGFAA 250
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 1264-1627 2.47e-08

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 58.69  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1264 LSHVKQSLGTVVQTSKEALRKANEVYDtALTLLNDVNRQTQPEID-----ISQLKKDaVAAN-----ERADELLKQITEL 1333
Cdd:PRK04778  100 FRKAKHEINEIESLLDLIEEDIEQILE-ELQELLESEEKNREEVEqlkdlYRELRKS-LLANrfsfgPALDELEKQLENL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1334 SnsngELFADFEteqELTEA--------LLKRAE------QQQLEDI-ELLERAKaahdkaTKAVEQgdntLKEANNTYE 1398
Cdd:PRK04778  178 E----EEFSQFV---ELTESgdyveareILDQLEeelaalEQIMEEIpELLKELQ------TELPDQ----LQELKAGYR 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1399 KL--AGFqsdvqrssesaekALQTVpNIEKEIQNAESLISQAEEALDGAN-KNANEAKKNAQEA--QL-----------K 1462
Cdd:PRK04778  241 ELveEGY-------------HLDHL-DIEKEIQDLKEQIDENLALLEELDlDEAEEKNEEIQERidQLydilerevkarK 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1463 YAEQASKDaelIRRKANETKVAARNLREEADQLNHRVKLTEMDIFK----LEESSTKDDNLVDDAKRKVGQAKA--DTQE 1536
Cdd:PRK04778  307 YVEKNSDT---LPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESvrqlEKQLESLEKQYDEITERIAEQEIAysELQE 383

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1537 AQKQIEKAnadLTAIKDE----LENLKDINTGD------LDRLENRLATVEGEINRVNLTGRIEKYREQRTIQKNLIDKY 1606
Cdd:PRK04778  384 ELEEILKQ---LEEIEKEqeklSEMLQGLRKDElearekLERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEAL 460

                         410       420
                  ....*....|....*....|..
gi 665410160 1607 DAELrelkDEVQ-NIGLISKAL 1627
Cdd:PRK04778  461 AEEL----EEKPiNMEAVNRLL 478
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1323-1583 4.96e-08

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 57.74  E-value: 4.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1323 ADELLKQITELSNSNGELfADFETEQELTEALLKRA----EQQQLEDIELLERA--KAAHDKA---TKAVEQGDNTLKEA 1393
Cdd:COG3064     1 AQEALEEKAAEAAAQERL-EQAEAEKRAAAEAEQKAkeeaEEERLAELEAKRQAeeEAREAKAeaeQRAAELAAEAAKKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1394 NNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAES-LISQAE-EALDGANKNANEAKKNAQEAQLKYAEQASKDA 1471
Cdd:COG3064    80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKeKAEEAKrKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1472 ELIRRKAnETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAI 1551
Cdd:COG3064   160 AAAAAAA-AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVE 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 665410160 1552 KDELENLKDINTGDLDRLENRLATVEGEINRV 1583
Cdd:COG3064   239 ATEEAALGGAEEAADLAAVGVLGAALAAAAAG 270
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 1267-1619 5.22e-08

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: 57.56  E-value: 5.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1267 VKQSLGTVVQTSKEALRKANEVYDtALTLLNDVNRQTQPEIDISQLK----KDAVAAN-----ERADELLKQITELSnsn 1337
Cdd:pfam06160   84 AKKALDEIEELLDDIEEDIKQILE-ELDELLESEEKNREEVEELKDKyrelRKTLLANrfsygPAIDELEKQLAEIE--- 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1338 gELFADFEteqELTEA--------LLKRAE------QQQLEDI-ELLERAKaahdkaTKAVEQgdntLKEANNTYEKL-- 1400
Cdd:pfam06160  160 -EEFSQFE---ELTESgdyleareVLEKLEeetdalEELMEDIpPLYEELK------TELPDQ----LEELKEGYREMee 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1401 AGFQSDVQrsseSAEKALQTvpnIEKEIQNAESLISQ-----AEEALDGANKNAN------EAKKNAQeaqlKYAEQasK 1469
Cdd:pfam06160  226 EGYALEHL----NVDKEIQQ---LEEQLEENLALLENleldeAEEALEEIEERIDqlydllEKEVDAK----KYVEK--N 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1470 DAElIRRKANETKVAARNLREEADQLNHRVKLTEMDIfkleesstkddnlvddakrkvgqakADTQEAQKQIEKANADLT 1549
Cdd:pfam06160  293 LPE-IEDYLEHAEEQNKELKEELERVQQSYTLNENEL-------------------------ERVRGLEKQLEELEKRYD 346

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160  1550 AIKDELEN-------LKDintgDLDRLENRLATVEGEINRVNltGRIEKYREQRTIQKNLIDKYDAELRELKDEVQN 1619
Cdd:pfam06160  347 EIVERLEEkevayseLQE----ELEEILEQLEEIEEEQEEFK--ESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1308-1563 5.55e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 56.46  E-value: 5.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1308 DISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGD 1387
Cdd:COG1340    23 EIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1388 NtLKEANNTYEKLagfqsdvQRSSESAEKALQTVP-NIEKEIQNAESlISQAEEALDGAnKNANEAKKNAQEAqLKYAEQ 1466
Cdd:COG1340   103 E-LNKAGGSIDKL-------RKEIERLEWRQQTEVlSPEEEKELVEK-IKELEKELEKA-KKALEKNEKLKEL-RAELKE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1467 ASKDAELIRRKANEtkvaarnLREEADQlnHRVKLTEMdiFKLEESSTKDdnlVDDAKRKVGQAKADTQEAQKQIEKANA 1546
Cdd:COG1340   172 LRKEAEEIHKKIKE-------LAEEAQE--LHEEMIEL--YKEADELRKE---ADELHKEIVEAQEKADELHEEIIELQK 237

                         250
                  ....*....|....*..
gi 665410160 1547 DLTAIKDELENLKDINT 1563
Cdd:COG1340   238 ELRELRKELKKLRKKQR 254
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1329-1550 6.59e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 56.76  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1329 QITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQ 1408
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1409 RS------------SESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRR 1476
Cdd:COG3883    97 RSggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160 1477 KANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTA 1550
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1143-1604 6.76e-08

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 56.97  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1143 QADANGEIDRARQNYTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISdiSREARALAD----KLE 1218
Cdd:COG3064    11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELA--AEAAKKLAEaekaAAE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1219 SEAQFDLKNAKDAKDAvEKAHQLAKSAIDLQLKIGTELR--SEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLL 1296
Cdd:COG3064    89 AEKKAAAEKAKAAKEA-EAAAAAEKAAAAAEKEKAEEAKrkAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1297 NDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAH 1376
Cdd:COG3064   168 AAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1377 DKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNA 1456
Cdd:COG3064   248 AEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGAL 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1457 QEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQE 1536
Cdd:COG3064   328 VVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDL 407

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410160 1537 AQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVNLTGRIEKYREQRTIQKNLID 1604
Cdd:COG3064   408 GAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGA 475
PTZ00121 PTZ00121
MAEBL; Provisional
 1255-1560 7.08e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 7.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1255 ELRSEVGlELSHVKQSLGTVVQTSKEALRkANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVaanERADELlKQITELS 1334
Cdd:PTZ00121 1061 EAKAHVG-QDEGLKPSYKDFDFDAKEDNR-ADEATEEAFGKAEEAKKTETGKAEEARKAEEAK---KKAEDA-RKAEEAR 1134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1335 NSngelfadfETEQELTEAllKRAEQ-------QQLEDIELLERAKAAHD-----KATKAVE-QGDNTLKEANNTYEKLA 1401
Cdd:PTZ00121 1135 KA--------EDARKAEEA--RKAEDakrveiaRKAEDARKAEEARKAEDakkaeAARKAEEvRKAEELRKAEDARKAEA 1204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1402 GFQSDVQRSSESAEKAlQTVPNIEkEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKY---------AEQASKDAE 1472
Cdd:PTZ00121 1205 ARKAEEERKAEEARKA-EDAKKAE-AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfarrqaaikAEEARKADE 1282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1473 LirRKANETKVAarnlrEEADQLNHRVKLTEMDifKLEESSTKDDNL---VDDAKRKVGQAKADTQEAQKQIEKANADLT 1549
Cdd:PTZ00121 1283 L--KKAEEKKKA-----DEAKKAEEKKKADEAK--KKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353

                         330
                  ....*....|.
gi 665410160 1550 AIKDELENLKD 1560
Cdd:PTZ00121 1354 AAADEAEAAEE 1364
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1312-1620 7.97e-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: 57.34  E-value: 7.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1312 LKKDAVAANERADELLKQITELSNsngelfaDFETEQE----LTEALLKRAEQ-QQLED-IELLErakaahdkatKAVEQ 1385
Cdd:TIGR04523   24 YKNIANKQDTEEKQLEKKLKTIKN-------ELKNKEKelknLDKNLNKDEEKiNNSNNkIKILE----------QQIKD 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1386 GDNTLKEANNTYEKLagfQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDganKNANEAKKnaQEAQLKYAE 1465
Cdd:TIGR04523   87 LNDKLKKNKDKINKL---NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNID---KFLTEIKK--KEKELEKLN 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1466 qaSKDAELIRRKA------NETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNL---VDDAKRKVGQAKADTQE 1536
Cdd:TIGR04523  159 --NKYNDLKKQKEelenelNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLesqISELKKQNNQLKDNIEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1537 AQKQIEKANADLTAIKDELENLKDINTGDLDRL-----------------ENRLATVEGEINRVN----------LTGRI 1589
Cdd:TIGR04523  237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekqkeleqnnkkikelEKQLNQLKSEISDLNnqkeqdwnkeLKSEL 316

                          330       340       350
                   ....*....|....*....|....*....|.
gi 665410160  1590 EKYREQRTIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:TIGR04523  317 KNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1143-1592 8.10e-08

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 56.97  E-value: 8.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1143 QADANGEIDRARQNYTILdQITENAKK---ELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISR---EARALADK 1216
Cdd:COG3064    34 KAKEEAEEERLAELEAKR-QAEEEAREakaEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAkeaEAAAAAEK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1217 LESEAQfdlknAKDAKDAVEKAHQLAKSAIDLQlKIGTELRSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLL 1296
Cdd:COG3064   113 AAAAAE-----KEKAEEAKRKAEEEAKRKAEEE-RKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1297 NDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQ-QQLEDIELLERAKAA 1375
Cdd:COG3064   187 AAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEaADLAAVGVLGAALAA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1376 HDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAEsLISQAEEALDGANKNANEAKKN 1455
Cdd:COG3064   267 AAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA-AGALVVRGGGAASLEAALSLLA 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1456 AQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQ 1535
Cdd:COG3064   346 AGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLA 425

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160 1536 EAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVNLTGRIEKY 1592
Cdd:COG3064   426 LAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADLLL 482
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1486-1620 1.05e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.55  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1486 RNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKD--ELENLkdinT 1563
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEAL----Q 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160 1564 GDLDRLENRLATVEGEINRVNltGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:COG1579    96 KEIESLKRRISDLEDEILELM--ERIEELEEELAELEAELAELEAELEEKKAELDEE 150
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 298-347 1.10e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.66  E-value: 1.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665410160  298 RCKCNGHASK---CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYNDLKWKR 347
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTG-------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1133-1594 1.22e-07

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 56.58  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1133 REHLVSADKFQADANGEIDRARQNYTILDQITENAKKELQQA---LDLlndegaqALARAKEksVEFGQQSEQiSDISRE 1209
Cdd:pfam05701   55 KKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAkqdSEL-------AKLRVEE--MEQGIADEA-SVAAKA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1210 ARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRS---EVG-------LELSHVKQSLGTVVQTSK 1279
Cdd:pfam05701  125 QLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSaskEIEktveeltIELIATKESLESAHAAHL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1280 EALRKAnevYDTALTLLNDVNRQ----TQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFE---TEQELTE 1352
Cdd:pfam05701  205 EAEEHR---IGAALAREQDKLNWekelKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMEsklKEEADGE 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1353 ALLKRAEQQQLEDIEL----LERAKAAHDKATKAVeqgdNTLKEAnntyekLAGFQSDVQRSSES-------AEKALQTV 1421
Cdd:pfam05701  282 GNEKKTSTSIQAALASakkeLEEVKANIEKAKDEV----NCLRVA------AASLRSELEKEKAElaslrqrEGMASIAV 351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1422 PNIEKEIQNAESLIS--QAEEA------------LDGANKNANEAKKNAQEAQLKYAEqASKDAELIRRKAN--ETKVAA 1485
Cdd:pfam05701  352 SSLEAELNRTKSEIAlvQAKEKearekmvelpkqLQQAAQEAEEAKSLAQAAREELRK-AKEEAEQAKAAAStvESRLEA 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1486 rNLRE-EADQLNHRVKLTEMDifKLEES-STKDDNLVDDAKRKVGQAKADTQEAQKQI----EKANADLTAIKDELENLK 1559
Cdd:pfam05701  431 -VLKEiEAAKASEKLALAAIK--ALQESeSSAESTNQEDSPRGVTLSLEEYYELSKRAheaeELANKRVAEAVSQIEEAK 507

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 665410160  1560 DINTGDLDRLE--NRlatvEGEINRVNL---TGRIEKYRE 1594
Cdd:pfam05701  508 ESELRSLEKLEevNR----EMEERKEALkiaLEKAEKAKE 543
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1160-1618 1.42e-07

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.59  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1160 LDQITENAKKELQQ---ALDLLNDEGAQAlARAKEKSVEFGQQSEQISDISREARALADKLESEAQ---------FDLKN 1227
Cdd:TIGR00606  191 LRQVRQTQGQKVQEhqmELKYLKQYKEKA-CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiehnlskiMKLDN 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1228 AKDAKDAVEKAHQLAKSAIDLQLK---IGTElrsEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQ 1304
Cdd:TIGR00606  270 EIKALKSRKKQMEKDNSELELKMEkvfQGTD---EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1305 PEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQlediellERAKAAHDKATKAVE 1384
Cdd:TIGR00606  347 VEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQE-------DEAKTAAQLCADLQS 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1385 QGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAES---LISQAEEALDGANKNANEAKKNAQEAQL 1461
Cdd:TIGR00606  420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSKAEKNSLTETL 499

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1462 KYAEQASKD--AELIRRKanetkvaaRNLREEADQLN-HRVKLTEMDIFKlEESSTKDDNLVDDAKR------------- 1525
Cdd:TIGR00606  500 KKEVKSLQNekADLDRKL--------RKLDQEMEQLNhHTTTRTQMEMLT-KDKMDKDEQIRKIKSRhsdeltsllgyfp 570

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1526 --------------KVGQAKADTQEAQKQIEKANADLTAIKDELENLkdinTGDLDRLENRLATVEG----EINRVNLTG 1587
Cdd:TIGR00606  571 nkkqledwlhskskEINQTRDRLAKLNKELASLEQNKNHINNELESK----EEQLSSYEDKLFDVCGsqdeESDLERLKE 646

                          490       500       510
                   ....*....|....*....|....*....|.
gi 665410160  1588 RIEKYREQRTIQKNLIDKYDAELRELKDEVQ 1618
Cdd:TIGR00606  647 EIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1424-1614 1.92e-07

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 53.68  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAESLISQAEEALDG--ANKNANEAKKNAQEAQLK----YAEQASKDAE-------LIRRKANETKVAArnLRE 1490
Cdd:COG1842    28 LDQAIRDMEEDLVEARQALAQviANQKRLERQLEELEAEAEkweeKARLALEKGRedlareaLERKAELEAQAEA--LEA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1491 EADQLNHRV-KLTEMdifkLEESSTKddnlVDDAKRKVGQAKA--DTQEAQKQIEKAnadltaikdelenLKDINTGD-- 1565
Cdd:COG1842   106 QLAQLEEQVeKLKEA----LRQLESK----LEELKAKKDTLKAraKAAKAQEKVNEA-------------LSGIDSDDat 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 665410160 1566 --LDRLENRLATVEGEIN-------RVNLTGRIEKYREQRTIqknlidkyDAELRELK 1614
Cdd:COG1842   165 saLERMEEKIEEMEARAEaaaelaaGDSLDDELAELEADSEV--------EDELAALK 214
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1055-1443 2.04e-07

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 56.11  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1055 NLVQDAADLHRAKLFNLSQTLDEIARTpvtndDEFEAKLKAVQEKVAVLAQD---ARD--NSGDGGQTYAEVIDDLHKHL 1129
Cdd:COG3096   282 ELSERALELRRELFGARRQLAEEQYRL-----VEMARELEELSARESDLEQDyqaASDhlNLVQTALRQQEKIERYQEDL 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1130 DSVREHLVSADKFQADANGEIDRARQNYTILDQITENAKKEL---QQALDLLN------DEGAQALARAKEKSVEFGQQS 1200
Cdd:COG3096   357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQALDVQQtraiqyQQAVQALEKARALCGLPDLTP 436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1201 EQISDISREARALADKLES---EAQFDLKNAKDAKDAVEKAHQLAKSAIDlqlkigtelrsEVGLELSHvkqslgtvvQT 1277
Cdd:COG3096   437 ENAEDYLAAFRAKEQQATEevlELEQKLSVADAARRQFEKAYELVCKIAG-----------EVERSQAW---------QT 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1278 SKEALRKANEvydtaltLLNDVNRQTQPEIDISQLKKDAvAANERADELLKQITELSNSNGELFADFETEQELTEALLKR 1357
Cdd:COG3096   497 ARELLRRYRS-------QQALAQRLQQLRAQLAELEQRL-RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1358 AE-------------QQQLEDI-----ELLERAKA---AHDKATKAVEQGDNTLKeanntyeklagfqsdvqrSSESAEK 1416
Cdd:COG3096   569 LEeqaaeaveqrselRQQLEQLrarikELAARAPAwlaAQDALERLREQSGEALA------------------DSQEVTA 630

                         410       420
                  ....*....|....*....|....*..
gi 665410160 1417 ALQTVPNIEKEIQNAESLISQAEEALD 1443
Cdd:COG3096   631 AMQQLLEREREATVERDELAARKQALE 657
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1155-1372 2.28e-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: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1155 QNYtiLDQITENAKKELQQALDLLNDEGAQA---LARAKEKSVEFgQQSEQISDISREARALADKLE------SEAQFDL 1225
Cdd:COG3206   159 EAY--LEQNLELRREEARKALEFLEEQLPELrkeLEEAEAALEEF-RQKNGLVDLSEEAKLLLQQLSelesqlAEARAEL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1226 KNAKDAKDAVEKahQLAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTSKEAlrkaNEVYDTALTLLNDVNRQTQP 1305
Cdd:COG3206   236 AEAEARLAALRA--QLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQ 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1306 EID--ISQLKKDAVAANERADELLKQITEL---SNSNGELFA-------DFETEQELTEALLKRAEQQQLE------DIE 1367
Cdd:COG3206   310 EAQriLASLEAELEALQAREASLQAQLAQLearLAELPELEAelrrlerEVEVARELYESLLQRLEEARLAealtvgNVR 389


                  ....*
gi 665410160 1368 LLERA 1372
Cdd:COG3206   390 VIDPA 394
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1152-1428 2.33e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1152 RARQNYTILDQItenakKELQQALDLLNDEgaqalaRAKEKSVEFgqqseqisdisREARALADKLESEAqfdlknaKDA 1231
Cdd:PRK03918  494 ELIKLKELAEQL-----KELEEKLKKYNLE------ELEKKAEEY-----------EKLKEKLIKLKGEI-------KSL 544

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1232 KDAVEKAHQLAKSAIDLQLKIGtELRSEVGlELSHVKQSLG-TVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDIS 1310
Cdd:PRK03918  545 KKELEKLEELKKKLAELEKKLD-ELEEELA-ELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1311 QLKKDAVAANERADELLKQITELSNSNGELFADF--ETEQELTEALLK--------RAEQQQLE--------DIELLERA 1372
Cdd:PRK03918  623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYseEEYEELREEYLElsrelaglRAELEELEkrreeikkTLEKLKEE 702

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160 1373 KAAHDKATKAVEQGDNTLKEANNTYEKLAGFQsdvqrsSESAEKALQTVPNIEKEI 1428
Cdd:PRK03918  703 LEEREKAKKELEKLEKALERVEELREKVKKYK------ALLKERALSKVGEIASEI 752
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 1425-1571 2.81e-07

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 51.10  E-value: 2.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1425 EKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRrkanetkvAARNLREEADQLNHRVKltem 1504
Cdd:pfam07926    7 QSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIK--------ALQALREELNELKAEIA---- 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160  1505 difKLEESstkddnlVDDAKRKVGQAKADTQEAQKQIEKANADLtaiKDELENLKDINTGDLDRLEN 1571
Cdd:pfam07926   75 ---ELKAE-------AESAKAELEESEESWEEQKKELEKELSEL---EKRIEDLNEQNKLLHDQLES 128
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1087-1341 3.35e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1087 DEFEAKLKAVQEKVAVLAQDARDnsgdggqtyaEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNYTILDQITEN 1166
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLSH----------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1167 A----------KKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLeSEAQfdlKNAKDAKDAVE 1236
Cdd:TIGR02169  838 LqeqridlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL-RELE---RKIEELEAQIE 913

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1237 KAHQLAK------SAIDLQLK-IGTELRSEVglELSHVKQSLGTVVQTSKEALRkanevydtALTLLNDVNRQTQPEIDI 1309
Cdd:TIGR02169  914 KKRKRLSelkaklEALEEELSeIEDPKGEDE--EIPEEELSLEDVQAELQRVEE--------EIRALEPVNMLAIQEYEE 983

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 665410160  1310 SQL------KKDAVAANERaDELLKQITELSNSNGELF 1341
Cdd:TIGR02169  984 VLKrldelkEKRAKLEEER-KAILERIEEYEKKKREVF 1020
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1088-1599 3.52e-07

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: 55.13  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1088 EFEAKLKAVQEKVAvLAQDARDNSGDGGQTYAEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNYTILD---QIT 1164
Cdd:pfam05557   52 ELQKRIRLLEKREA-EAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAElelQST 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1165 ENAKKELQQALDLLN-----------------DEGAQALARAKEKSVEFGQQS-------------EQISDISREARala 1214
Cdd:pfam05557  131 NSELEELQERLDLLKakaseaeqlrqnlekqqSSLAEAEQRIKELEFEIQSQEqdseivknskselARIPELEKELE--- 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1215 dKLESEAQFDLKNAKDAKDAVEKAHQLaKSAIDLQLKIGTELRSeVGLELSHVKQSLGT---VVQTSKEALRKANEVYDT 1291
Cdd:pfam05557  208 -RLREHNKHLNENIENKLLLKEEVEDL-KRKLEREEKYREEAAT-LELEKEKLEQELQSwvkLAQDTGLNLRSPEDLSRR 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1292 ALTLLND----VNRQTQPEIDISQLKKDAVAANERADELLKQITELsnsngelfadfETEQELTEALLKRAEQQQLedie 1367
Cdd:pfam05557  285 IEQLQQReivlKEENSSLTSSARQLEKARRELEQELAQYLKKIEDL-----------NKKLKRHKALVRRLQRRVL---- 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1368 LL--ERakaahDKATKAVEQGDNTLKEANNTYEKLagfqsdvqRSSESAEKALQTVPNIEKEIqnaESLISQAEEALDGA 1445
Cdd:pfam05557  350 LLtkER-----DGYRAILESYDKELTMSNYSPQLL--------ERIEEAEDMTQKMQAHNEEM---EAQLSVAEEELGGY 413

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1446 NKNANEAkknAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKL------EESSTKDDNL 1519
Cdd:pfam05557  414 KQQAQTL---ERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRclqgdyDPKKTKVLHL 490

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1520 VDDAKRKVGQAKADTQEA-QKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVNLtgRIEKYRE--QR 1596
Cdd:pfam05557  491 SMNPAAEAYQQRKNQLEKlQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAEL--KNQRLKEvfQA 568


                   ...
gi 665410160  1597 TIQ 1599
Cdd:pfam05557  569 KIQ 571
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1164-1382 3.54e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.38  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1164 TENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLEsEAQFDLKNAKDAKDAVEKA----- 1238
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKEIAELRAEleaqk 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1239 HQLAKSAIDLQlKIGTE------LRSEVGLELSHVKQSLGTVVQtskeALRKANEVYDTALTLLNDVNRQTQPEIDisQL 1312
Cdd:COG4942   104 EELAELLRALY-RLGRQpplallLSPEDFLDAVRRLQYLKYLAP----ARREQAEELRADLAELAALRAELEAERA--EL 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410160 1313 KKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALlkRAEQQQLED-IELLERAKAAHDKATKA 1382
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL--QQEAEELEAlIARLEAEAAAAAERTPA 245
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1085-1620 3.56e-07

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 55.61  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1085 NDDEFEAKLKAVQEKVAvlAQDARDNSGDGGQTYAEVIDDLHKHLDSVREHLVSADKFQADANgEIDRARQNYT------ 1158
Cdd:PTZ00440 1097 KNKLIEIKNKSHEHVVN--ADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLN-EVNEIEIEYErilidh 1173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1159 ILDQITENAKKelqqaldllndegaqalarAKEKSVEFGQQSEQI----SDISREARALADKLESEAQFDlknakDAKDA 1234
Cdd:PTZ00440 1174 IVEQINNEAKK-------------------SKTIMEEIESYKKDIdqvkKNMSKERNDHLTTFEYNAYYD-----KATAS 1229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1235 VEKAHQLAKSAIDL--------QLKIGTELRSEVgleLSHVKQSLgTVVQTSKEALRKANEVYDtaLTLLNDVNRQTQpe 1306
Cdd:PTZ00440 1230 YENIEELTTEAKGLkgeanrstNVDELKEIKLQV---FSYLQQVI-KENNKMENALHEIKNMYE--FLISIDSEKILK-- 1301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1307 iDISQLKKDAVAANERADELLKQITELSNsngELFADFETEQELTEALLKRAEQQQLED-IELLERAkaaHDKATKAVEQ 1385
Cdd:PTZ00440 1302 -EILNSTKKAEEFSNDAKKELEKTDNLIK---QVEAKIEQAKEHKNKIYGSLEDKQIDDeIKKIEQI---KEEISNKRKE 1374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1386 GDNTLKEANNTYEKLAGFQSDVQRSSESAE-----KALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNaQEAQ 1460
Cdd:PTZ00440 1375 INKYLSNIKSNKEKCDLHVRNASRGKDKIDflnkhEAIEPSNSKEVNIIKITDNINKCKQYSNEAMETENKADEN-NDSI 1453

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1461 LKYAEQAS---KDAE--LIRRKANETKVAARNLRE----EADQLNHRVKLTEMDIFKLEESS--TKDDNLVDDAKRKVgq 1529
Cdd:PTZ00440 1454 IKYEKEITnilNNSSilGKKTKLEKKKKEATNIMDdingEHSIIKTKLTKSSEKLNQLNEQPniKREGDVLNNDKSTI-- 1531

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1530 AKADTQEAQKQIEKANADLTAIKDELENLKDiNTGDLDRLENRLATVEGEINRVNLTGRIEKYRE---QRTIQKNLIDKY 1606
Cdd:PTZ00440 1532 AYETIQYNLGRVKHNLLNILNIKDEIETILN-KAQDLMRDISKISKIVENKNLENLNDKEADYVKyldNILKEKQLMEAE 1610

                         570
                  ....*....|....
gi 665410160 1607 DAELRELKDEVQNI 1620
Cdd:PTZ00440 1611 YKKLNEIYSDVDNI 1624
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1331-1613 3.56e-07

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: 55.11  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1331 TELSNSNG--ELFADFETEQEL-------TEALLKRAEQQQLEDIELLERAKAA-------HDKATKAVEQG----DNTL 1390
Cdd:pfam05483   68 SDFENSEGlsRLYSKLYKEAEKikkwkvsIEAELKQKENKLQENRKIIEAQRKAiqelqfeNEKVSLKLEEEiqenKDLI 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1391 KEANNTYEKLAGFQSDVQRSSESAEKA-----------LQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEA 1459
Cdd:pfam05483  148 KENNATRHLCNLLKETCARSAEKTKKYeyereetrqvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHL 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1460 QLKYAEQAS---KDAELIRRKANETKVAARNL-------REEADQLNHRVKLTEMDifkLEESSTKDDNL---VDDAK-- 1524
Cdd:pfam05483  228 EEEYKKEINdkeKQVSLLLIQITEKENKMKDLtflleesRDKANQLEEKTKLQDEN---LKELIEKKDHLtkeLEDIKms 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1525 --RKVGQAKA---DTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEgEINRVNlTGRIEKYREQRTIQ 1599
Cdd:pfam05483  305 lqRSMSTQKAleeDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTE-QQRLEKNEDQLKII 382

                          330
                   ....*....|....
gi 665410160  1600 KNLIDKYDAELREL 1613
Cdd:pfam05483  383 TMELQKKSSELEEM 396
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1146-1527 3.85e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1146 ANGEIDRARQNYTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEAQfDL 1225
Cdd:COG4372    11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE-QL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1226 KNAKDAKDAVEKahqlaksaidlQLKigtelrsevglelshvkqslgtVVQTSKEALRKANEVYDTALTLLNDvnRQTQP 1305
Cdd:COG4372    90 QAAQAELAQAQE-----------ELE----------------------SLQEEAEELQEELEELQKERQDLEQ--QRKQL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1306 EIDISQLKKDAVAANERADELLKQITELSNsngELFADFETEQELTEALLKRAEQQQLED----IELLERAKAAHDKATK 1381
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQE---ELAALEQELQALSEAEAEQALDELLKEanrnAEKEEELAEAEKLIES 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1382 AVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLIS-----QAEEALDGANKNANEAKKNA 1456
Cdd:COG4372   212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilvekDTEEEELEIAALELEALEEA 291

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410160 1457 QEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKV 1527
Cdd:COG4372   292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1162-1638 4.36e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.18  E-value: 4.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1162 QITE----NAKKElqqaldllnDEGAQALARAKEksvEFGQQSEQISDIsREARALAdkleSEAQFDLKNAKDAKDAVEK 1237
Cdd:pfam01576  230 QIAElraqLAKKE---------EELQAALARLEE---ETAQKNNALKKI-RELEAQI----SELQEDLESERAARNKAEK 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1238 AhqlaksaidlqlkigtelRSEVGLELshvkqslgtvvqtskEALRkaNEVYDTaltlLNDVNRQ----TQPEIDISQLK 1313
Cdd:pfam01576  293 Q------------------RRDLGEEL---------------EALK--TELEDT----LDTTAAQqelrSKREQEVTELK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1314 KdAVAANERADEllKQITELSnsngelfadfeteQELTEALLKRAEQqqledIELLERAKAAHDKATKAVEQGDNTLKEA 1393
Cdd:pfam01576  334 K-ALEEETRSHE--AQLQEMR-------------QKHTQALEELTEQ-----LEQAKRNKANLEKAKQALESENAELQAE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1394 NNTyekLAGFQSDVQRSSESAEKALQ------------------TVPNIEKEIQNAESLISQAEEALDGANKNANEAKKN 1455
Cdd:pfam01576  393 LRT---LQQAKQDSEHKRKKLEGQLQelqarlseserqraelaeKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1456 AQEAQ----------LKYA---EQASKDAELIRRKANETKVAARNLREEADQLNhrVKLTEMDIfKLEESSTKDDNLVDD 1522
Cdd:pfam01576  470 LQDTQellqeetrqkLNLStrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ--AQLSDMKK-KLEEDAGTLEALEEG 546

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1523 AKRkvgqakadtqeAQKQIEKANADL---TAIKDELENLKDINTGDLDRLenrlaTVEGEINRVNLTGRIEKYR------ 1593
Cdd:pfam01576  547 KKR-----------LQRELEALTQQLeekAAAYDKLEKTKNRLQQELDDL-----LVDLDHQRQLVSNLEKKQKkfdqml 610

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 665410160  1594 -EQRTIQKNLIDKYD---AELRElkDEVQNIGLiSKALPDSCFSRNRLE 1638
Cdd:pfam01576  611 aEEKAISARYAEERDraeAEARE--KETRALSL-ARALEEALEAKEELE 656
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1308-1583 4.55e-07

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 54.65  E-value: 4.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1308 DISQLKKDAVAANERADELLKqitELSNSNG---ELFADFETEQelTEallkraEQQQLEDIEL---------------- 1368
Cdd:pfam05701   50 EIPEYKKQSEAAEAAKAQVLE---ELESTKRlieELKLNLERAQ--TE------EAQAKQDSELaklrveemeqgiadea 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1369 -------LERAKAAHDKAT---KAVEQGDNTLKEannTYEKLAgfqSDVQRSSESAEKALQTVPNIEKEIQNA------- 1431
Cdd:pfam05701  119 svaakaqLEVAKARHAAAVaelKSVKEELESLRK---EYASLV---SERDIAIKRAEEAVSASKEIEKTVEELtieliat 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1432 -ESLIS------QAEEALDGANKnANEAKKNAQEAQLKYAEQaskdaELirRKANETKVAARNLREEAD-----QLNHRV 1499
Cdd:pfam05701  193 kESLESahaahlEAEEHRIGAAL-AREQDKLNWEKELKQAEE-----EL--QRLNQQLLSAKDLKSKLEtasalLLDLKA 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1500 KLTEMDIFKLEESSTKDDNL---VDDAKRKVGQAKADTQEAQKQIEKANADL-------TAIKDELENLKdintGDLDRL 1569
Cdd:pfam05701  265 ELAAYMESKLKEEADGEGNEkktSTSIQAALASAKKELEEVKANIEKAKDEVnclrvaaASLRSELEKEK----AELASL 340

                          330       340
                   ....*....|....*....|.
gi 665410160  1570 ENR-------LATVEGEINRV 1583
Cdd:pfam05701  341 RQRegmasiaVSSLEAELNRT 361
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1424-1620 6.75e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.99  E-value: 6.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAESLISQAEEALDGANKNANE--AKKNAQEAQLK-YAEQASKDAEL----------IRRKANETKVAARNLRE 1490
Cdd:COG1340    13 LEEKIEELREEIEELKEKRDELNEELKElaEKRDELNAQVKeLREEAQELREKrdelnekvkeLKEERDELNEKLNELRE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1491 EADQLNHRVKLT----------EMDIFKLEE-------SSTKDDNLVDDAKRKvgQAKAdtqEAQKQIEKANADLTAIKD 1553
Cdd:COG1340    93 ELDELRKELAELnkaggsidklRKEIERLEWrqqtevlSPEEEKELVEKIKEL--EKEL---EKAKKALEKNEKLKELRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160 1554 ELENLKDintgdldrlenRLATVEGEINrvNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:COG1340   168 ELKELRK-----------EAEEIHKKIK--ELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA 221
growth_prot_Scy NF041483
polarized growth protein Scy;
1181-1618 7.48e-07

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 54.45  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1181 EGAQALA-RAKEKSVEFGQQSEQISdisREARALADKLESEAQFDLKNAKDAKDAVEKAHqlAKSAIDLQLKIGTEL--- 1256
Cdd:NF041483   54 EARRSLAsRPAYDGADIGYQAEQLL---RNAQIQADQLRADAERELRDARAQTQRILQEH--AEHQARLQAELHTEAvqr 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1257 RSEVGLEL--------SHVKQSLGTVVQ----TSKEALRKANEVY---DTAL-------TLLNDVNRQ----------TQ 1304
Cdd:NF041483  129 RQQLDQELaerrqtveSHVNENVAWAEQlrarTESQARRLLDESRaeaEQALaaaraeaERLAEEARQrlgseaesarAE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1305 PEIDISQLKKDA----VAANERADELLKQITELSNSNGElfadfETEQELTEA--LLKRAEQQQLEDIELLERAKAAHDK 1378
Cdd:NF041483  209 AEAILRRARKDAerllNAASTQAQEATDHAEQLRSSTAA-----ESDQARRQAaeLSRAAEQRMQEAEEALREARAEAEK 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1379 A-TKAVEQGDNTLKEANNTYEklagfqsdvQRSSESAEKALQTVPNIEKEiqnAESLISQAEEALDGANKNANEAKKNAQ 1457
Cdd:NF041483  284 VvAEAKEAAAKQLASAESANE---------QRTRTAKEEIARLVGEATKE---AEALKAEAEQALADARAEAEKLVAEAA 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1458 E-----------AQL----KYAEQ----ASKDAELIRRKANEtkvAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDN 1518
Cdd:NF041483  352 EkartvaaedtaAQLakaaRTAEEvltkASEDAKATTRAAAE---EAERIRREAEAEADRLRGEAADQAEQLKGAAKDDT 428

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1519 ---------LVDDAKRKVGQA---KADT------------QEAQKQIEKANAdlTAikdelENLKDINTGDLDRLENRlA 1574
Cdd:NF041483  429 keyraktveLQEEARRLRGEAeqlRAEAvaegerirgearREAVQQIEEAAR--TA-----EELLTKAKADADELRST-A 500

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 665410160 1575 TVEGEinRVNlTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQ 1618
Cdd:NF041483  501 TAESE--RVR-TEAIERATTLRRQAEETLERTRAEAERLRAEAE 541
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1086-1555 7.87e-07

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 53.88  E-value: 7.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1086 DDEFeAKLKaVQEkvavLAQDARDNSGDGGQTYAEVIDDLHK----HLDSVREHLVSADKFQADANGEIDRARQNytilD 1161
Cdd:pfam05701   99 DSEL-AKLR-VEE----MEQGIADEASVAAKAQLEVAKARHAaavaELKSVKEELESLRKEYASLVSERDIAIKR----A 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1162 QITENAKKELQQALDLLNDEgaqaLARAKEkSVEFGQQSEQISDISREARALA---DKLESEaqfdlKNAKDAKDAVEKA 1238
Cdd:pfam05701  169 EEAVSASKEIEKTVEELTIE----LIATKE-SLESAHAAHLEAEEHRIGAALAreqDKLNWE-----KELKQAEEELQRL 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1239 HQLAKSAIDLQLKIGTELRSEVGL--EL-----SHVKQSLGTVVQTsKEALRKANEVYDTALTLLNDVNrqtqpeIDISQ 1311
Cdd:pfam05701  239 NQQLLSAKDLKSKLETASALLLDLkaELaaymeSKLKEEADGEGNE-KKTSTSIQAALASAKKELEEVK------ANIEK 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1312 LKKDA----VAANERADELLKQITELSNSNGELFADFETEQELtEALLKRAEQqqleDIELLE-RAKAAHDKATKAVEQG 1386
Cdd:pfam05701  312 AKDEVnclrVAAASLRSELEKEKAELASLRQREGMASIAVSSL-EAELNRTKS----EIALVQaKEKEAREKMVELPKQL 386

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1387 DNTLKEANNTyEKLAGF-QSDVQRSSESAEKALQTVPNIEKEIQNA--ESLISQAEEALDGANKNANEAKKNAQEAQLKY 1463
Cdd:pfam05701  387 QQAAQEAEEA-KSLAQAaREELRKAKEEAEQAKAAASTVESRLEAVlkEIEAAKASEKLALAAIKALQESESSAESTNQE 465

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1464 AEQ------ASKDAELIRRkANETkvaarnlrEEadQLNHRVK--LTEMDIFKLEESSTKDDnlVDDAKRKVGQAKADTQ 1535
Cdd:pfam05701  466 DSPrgvtlsLEEYYELSKR-AHEA--------EE--LANKRVAeaVSQIEEAKESELRSLEK--LEEVNREMEERKEALK 532

                          490       500
                   ....*....|....*....|
gi 665410160  1536 EAQKQIEKANADLTAIKDEL 1555
Cdd:pfam05701  533 IALEKAEKAKEGKLAAEQEL 552
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1057-1555 7.88e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 54.03  E-value: 7.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1057 VQDAADL----HRAKLfNLS----QTLDEIARTPVTNDDEFEAKlKAVQEKVAVLAQDardnsgdggqtyaevIDDLHKH 1128
Cdd:pfam01576  470 LQDTQELlqeeTRQKL-NLStrlrQLEDERNSLQEQLEEEEEAK-RNVERQLSTLQAQ---------------LSDMKKK 532

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1129 LDSVREHLVSADKFQADANGEIDRARQNY----TILDQItENAKKELQQAL-DLLNDEGA----------------QALA 1187
Cdd:pfam01576  533 LEEDAGTLEALEEGKKRLQRELEALTQQLeekaAAYDKL-EKTKNRLQQELdDLLVDLDHqrqlvsnlekkqkkfdQMLA 611

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1188 RAKEKSVEFGQQSEQISDISRE--------ARALADKLESEAQFDLKNAK---------DAKDAVEK-AHQLAKS--AID 1247
Cdd:pfam01576  612 EEKAISARYAEERDRAEAEAREketralslARALEEALEAKEELERTNKQlraemedlvSSKDDVGKnVHELERSkrALE 691

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1248 LQLK-------------IGTE---LRSEVGLEL--SHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQ------- 1302
Cdd:pfam01576  692 QQVEemktqleeledelQATEdakLRLEVNMQAlkAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQraqavaa 771

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1303 -TQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFE----TEQEL------TEALLK--RAEQQQL-EDIEL 1368
Cdd:pfam01576  772 kKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEearaSRDEIlaqskeSEKKLKnlEAELLQLqEDLAA 851

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1369 LERAK--AAHDKATKAVEQGDNTLKEANNTYEK-------------LAGFQSDVQRSSESAEKALQTVPNIEKEI----- 1428
Cdd:pfam01576  852 SERARrqAQQERDELADEIASGASGKSALQDEKrrleariaqleeeLEEEQSNTELLNDRLRKSTLQVEQLTTELaaers 931

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1429 --QNAESLISQAE----------EALDGANKN-------ANEAKKNAQEAQLkyaEQASKD----AELIRRKANETKVA- 1484
Cdd:pfam01576  932 tsQKSESARQQLErqnkelkaklQEMEGTVKSkfkssiaALEAKIAQLEEQL---EQESRErqaaNKLVRRTEKKLKEVl 1008

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1485 ---------ARNLREEADQLNHRVKLTEMDIFKLEESSTKddnlVDDAKRKVgqaKADTQEAQKQIEKANADLTAIKDEL 1555
Cdd:pfam01576 1009 lqvederrhADQYKDQAEKGNSRMKQLKRQLEEAEEEASR----ANAARRKL---QRELDDATESNESMNREVSTLKSKL 1081
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1098-1454 8.53e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 8.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1098 EKVAVLAQDARDNsgdggqtyAEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNytiLDQiTENAKKELQQALDL 1177
Cdd:COG4372    24 ILIAALSEQLRKA--------LFELDKLQEELEQLREELEQAREELEQLEEELEQARSE---LEQ-LEEELEELNEQLQA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1178 LNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLES--EAQFDLKNAKDAKDavEKAHQLAKSAIDLQLKIGTE 1255
Cdd:COG4372    92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQleAQIAELQSEIAERE--EELKELEEQLESLQEELAAL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1256 LRSEVGLELSHVKQSLgtvvqtsKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVaaneRADELLKQITELSN 1335
Cdd:COG4372   170 EQELQALSEAEAEQAL-------DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK----DSLEAKLGLALSAL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1336 SNGELFADFETEQELTEaLLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKL-AGFQSDVQRSSESA 1414
Cdd:COG4372   239 LDALELEEDKEELLEEV-ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLnLAALSLIGALEDAL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 665410160 1415 EKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKK 1454
Cdd:COG4372   318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1104-1567 8.61e-07

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 53.87  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1104 AQDARDNSGDGGQTYAEVIDdlhkhLDSVREHLVSADKFQADANGEIDRARQNYTILDQITENAKKELQQALDLLNDEGA 1183
Cdd:COG5271   416 EEEEADEDASAGETEDESTD-----VTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDD 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1184 QALARAKEKSVEFGQQSEQISDISREARAL-ADKLESEAQFDLKNAKDAKDAVEKAH---QLAKSAIDLQLKIGTELRSE 1259
Cdd:COG5271   491 GDEEEAEEDAEAEADSDELTAEETSADDGAdTDAAADPEDSDEDALEDETEGEENAPgsdQDADETDEPEATAEEDEPDE 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1260 VGLELSHVKQSLGT-VVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDisQLKKDAVAANERADELLKQITELSNSNG 1338
Cdd:COG5271   571 AEAETEDATENADAdETEESADESEEAEASEDEAAEEEEADDDEADADAD--GAADEEETEEEAAEDEAAEPETDASEAA 648

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1339 ELFADFETEQELT--EALLKRAEQQQLEDiellERAKAAHDKATKAVEQGDNTLKEANNTYEKLAG------FQSDVQRS 1410
Cdd:COG5271   649 DEDADAETEAEASadESEEEAEDESETSS----EDAEEDADAAAAEASDDEEETEEADEDAETASEeadaeeADTEADGT 724

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1411 SESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKK--NAQEAQLKYAEQASKDAELIRRKANETKVAARNL 1488
Cdd:COG5271   725 AEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGleEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQ 804

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1489 REEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLD 1567
Cdd:COG5271   805 DTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAET 883
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 1051-1523 9.37e-07

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: 53.70  E-value: 9.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1051 PDCYNLVQDA-ADLHRAKLFNLSQTLDEIARTPvtndDEFEAKLKAVQEKVAVLAQDARDNSGDGGQ---TYAEVIDDLH 1126
Cdd:pfam06160   63 PDIEELLFEAeELNDKYRFKKAKKALDEIEELL----DDIEEDIKQILEELDELLESEEKNREEVEElkdKYRELRKTLL 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1127 KHLDSVREhlvSADKFQAdangEIDRARQNYTILDQITEN-----AKKELQQA---LDLLNDEGAQALARAKEKSVEFGQ 1198
Cdd:pfam06160  139 ANRFSYGP---AIDELEK----QLAEIEEEFSQFEELTESgdyleAREVLEKLeeeTDALEELMEDIPPLYEELKTELPD 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1199 QSEQISDISREAraladkLESEAQFDLKNAKDAKDAVEKAHQLAKSAID-LQLKIGTELRSEVGLELSHVKQSLGTVVQT 1277
Cdd:pfam06160  212 QLEELKEGYREM------EEEGYALEHLNVDKEIQQLEEQLEENLALLEnLELDEAEEALEEIEERIDQLYDLLEKEVDA 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1278 SKEALRKANEVYDtALTLLNDVNRQTQPEIDisqlkkdavaaneradeLLKQITELSNSNGELFADFETEqeltealLKR 1357
Cdd:pfam06160  286 KKYVEKNLPEIED-YLEHAEEQNKELKEELE-----------------RVQQSYTLNENELERVRGLEKQ-------LEE 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1358 AEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANntyEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQ 1437
Cdd:pfam06160  341 LEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE---EEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1438 aeEALDGANknaneakknaqEAQLKYAEQASKDAELIRRKANETKVaarNLreeaDQLNHRVKLTEMDIFKLEESStkdD 1517
Cdd:pfam06160  418 --SNLPGLP-----------ESYLDYFFDVSDEIEDLADELNEVPL---NM----DEVNRLLDEAQDDVDTLYEKT---E 474


                   ....*.
gi 665410160  1518 NLVDDA 1523
Cdd:pfam06160  475 ELIDNA 480
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 299-343 1.11e-06

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 46.96  E-value: 1.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 665410160   299 CKCNGHASK---CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYNDL 343
Cdd:pfam00053    1 CDCNPHGSLsdtCDPETG-------QCLCKPGVTGRHCDRCKPGYYGL 41
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1276-1495 1.16e-06

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: 51.57  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1276 QTSKEALRKANEVYDTALTLLNDVNRQtqpeidISQLKKDAVAANERADELLKQITELSNSNGElfadfeteqelTEALL 1355
Cdd:pfam00261   18 KEAMKKLEEAEKRAEKAEAEVAALNRR------IQLLEEELERTEERLAEALEKLEEAEKAADE-----------SERGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1356 KRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANntyEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNA---- 1431
Cdd:pfam00261   81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVA---RKLVVVEGDLERAEERAELAESKIVELEEELKVVgnnl 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160  1432 ESLISQAEEALDGANKNANEAKknAQEAQLKYAEQASKDAElirRKANEtkvaarnLREEADQL 1495
Cdd:pfam00261  158 KSLEASEEKASEREDKYEEQIR--FLTEKLKEAETRAEFAE---RSVQK-------LEKEVDRL 209
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1271-1619 1.23e-06

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 53.68  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1271 LGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQEL 1350
Cdd:PTZ00440  541 LIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKND 620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1351 TEALLK-------RAEQQQLED--IELLERAKAAHDKAtKAVEQGDNTLKEANNTYEKLAGFQSDV-------------- 1407
Cdd:PTZ00440  621 LQEKVKyilnkfyKGDLQELLDelSHFLDDHKYLYHEA-KSKEDLQTLLNTSKNEYEKLEFMKSDNidniiknlkkelqn 699

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1408 -----------------QRSSESAEKALQTVPNI-------EKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKY 1463
Cdd:PTZ00440  700 llslkeniikkqlnnieQDISNSLNQYTIKYNDLkssieeyKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTY 779

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1464 AE-QASKDAELIRRKA--NETKVAARNLREEADQLNHrvklTEMDIFKLEESSTKDD-NLVD--------DAKRKVGQAK 1531
Cdd:PTZ00440  780 EEfLQYKDTILNKENKisNDINILKENKKNNQDLLNS----YNILIQKLEAHTEKNDeELKQllqkfpteDENLNLKELE 855

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1532 ADTQEAQKQIEKANADLTAIKDELENLKDINTGdLDRLENRLATVEGEI-NRVNLTGRIEKYREQrtIQK-NLIDKYDAE 1609
Cdd:PTZ00440  856 KEFNENNQIVDNIIKDIENMNKNINIIKTLNIA-INRSNSNKQLVEHLLnNKIDLKNKLEQHMKI--INTdNIIQKNEKL 932

                         410
                  ....*....|....*
gi 665410160 1610 -----LRELKDEVQN 1619
Cdd:PTZ00440  933 nllnnLNKEKEKIEK 947
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1272-1492 1.34e-06

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: 51.99  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1272 GTVVQTSKEALRKANEVYDTALTLLNDVN-RQTQPEID---------ISQLKKDAVAANERADELLKQITELSNSNGELF 1341
Cdd:cd22656    76 GDIYNYAQNAGGTIDSYYAEILELIDDLAdATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1342 ADFET-EQELTEALLKRAEQQQLEDIE-LLERAKAAHDKATKAVEqgdNTLKEANNTYEKLAGFQSDVQRSSESAEKALQ 1419
Cdd:cd22656   156 TALETlEKALKDLLTDEGGAIARKEIKdLQKELEKLNEEYAAKLK---AKIDELKALIADDEAKLAAALRLIADLTAADT 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1420 TVPNIEKEIQNAESLISQAEEA-------LDGANKNANEAKKNAqeaqlKYAEQASKDAELIRRKANETKVAARNLREEA 1492
Cdd:cd22656   233 DLDNLLALIGPAIPALEKLQGAwqaiatdLDSLKDLLEDDISKI-----PAAILAKLELEKAIEKWNELAEKADKFRQNA 307
growth_prot_Scy NF041483
polarized growth protein Scy;
1181-1557 1.43e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 53.29  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1181 EGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEaqfdlknakdAKDAVEKAHQLAKSAIDLQLKIGTE----L 1256
Cdd:NF041483  248 ESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAE----------AKEAAAKQLASAESANEQRTRTAKEeiarL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1257 RSEVGLELSHVKQSLGTVVQTSK-EALRKANEVYDTAltllndvnRQTQPEIDISQLKKDAVAANE---RADELLKQITE 1332
Cdd:NF041483  318 VGEATKEAEALKAEAEQALADARaEAEKLVAEAAEKA--------RTVAAEDTAAQLAKAARTAEEvltKASEDAKATTR 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1333 LSNSNGELF---ADFETEQELTEAL-----LKRAEQQQLED-----IELLERAKAAHDKA----TKAVEQGD-------- 1387
Cdd:NF041483  390 AAAEEAERIrreAEAEADRLRGEAAdqaeqLKGAAKDDTKEyraktVELQEEARRLRGEAeqlrAEAVAEGErirgearr 469

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1388 ---NTLKEANNTYEKL---AGFQSDVQRSSESAEKALQTVPNIEKeiqnAESLISQAEEALDGANKNANEAKKNAQEAQL 1461
Cdd:NF041483  470 eavQQIEEAARTAEELltkAKADADELRSTATAESERVRTEAIER----ATTLRRQAEETLERTRAEAERLRAEAEEQAE 545

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1462 KYAEQASKDAELIRRKAnETKVAARnlREEADQLNHRVKL-----------------TEMDIFKLEESSTKDDNLVDDAK 1524
Cdd:NF041483  546 EVRAAAERAARELREET-ERAIAAR--QAEAAEELTRLHTeaeerltaaeealadarAEAERIRREAAEETERLRTEAAE 622

                         410       420       430
                  ....*....|....*....|....*....|....
gi 665410160 1525 R-KVGQAKADtQEAQKQIEKANADLTAIKDELEN 1557
Cdd:NF041483  623 RiRTLQAQAE-QEAERLRTEAAADASAARAEGEN 655
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
847-891 1.52e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 46.54  E-value: 1.52e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410160    847 CDCN--GNVDPNavgnCNRTTGECLkCIHNTAGEHCDQCLSGHFGDP 891
Cdd:smart00180    1 CDCDpgGSASGT----CDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1170-1620 1.59e-06

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 53.13  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1170 ELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEAqfdLKNAKDAKDAVEKAHQLAKSAIDLQ 1249
Cdd:TIGR00606  330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDG---FERGPFSERQIKNFHTLVIERQEDE 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1250 LKIGTELRSEVGLELShVKQSLGTVVQTSKEALRKANEVYDTALTllndvNRQTQPEIDISQLKKdavaANERADELLKQ 1329
Cdd:TIGR00606  407 AKTAAQLCADLQSKER-LKQEQADEIRDEKKGLGRTIELKKEILE-----KKQEELKFVIKELQQ----LEGSSDRILEL 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1330 ITELSNSNGELfaDFETEQELTEALLKRAEQQQLEDIELLERAKAAH------DKATKAVEQGDNTLKEANNTYEKLAGF 1403
Cdd:TIGR00606  477 DQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDqemeqlNHHTTTRTQMEMLTKDKMDKDEQIRKI 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1404 QSdvqRSSESAEKALQTVPN---IEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQlkyAEQASKDAELIRRKANE 1480
Cdd:TIGR00606  555 KS---RHSDELTSLLGYFPNkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN---NELESKEEQLSSYEDKL 628

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1481 TKV-AARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRK----------VGQAKADTQEAQKQIEKAnadLT 1549
Cdd:TIGR00606  629 FDVcGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrVFQTEAELQEFISDLQSK---LR 705

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410160  1550 AIKDELENLKDintgDLDRLENRlatvegeinRVNLTGRIEkyreqrtIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:TIGR00606  706 LAPDKLKSTES----ELKKKEKR---------RDEMLGLAP-------GRQSIIDLKEKEIPELRNKLQKV 756
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 1419-1542 1.93e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 52.04  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1419 QTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKN--AQEAQLKYAEQASKDAE--LIRRKANETKVAARNLREEADQ 1494
Cdd:TIGR04320  247 TPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAAltSAQTAYAAAQAALATAQkeLANAQAQALQTAQNNLATAQAA 326

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 665410160  1495 LnhrvkltemdifkleessTKDDNLVDDAKRKVGQAKADTQEAQKQIE 1542
Cdd:TIGR04320  327 L------------------ANAEARLAKAKEALANLNADLAKKQAALD 356
mukB PRK04863
chromosome partition protein MukB;
1087-1622 1.97e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.04  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1087 DEFEAKLKAVQEKVAVLAQDARDnsgdggqtYAEVIDDLHKH----------LDSVRE-------HLVSADKFQADANGE 1149
Cdd:PRK04863  379 EENEARAEAAEEEVDELKSQLAD--------YQQALDVQQTRaiqyqqavqaLERAKQlcglpdlTADNAEDWLEEFQAK 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1150 IDRARQNYTILDQ---ITENAKKELQQALDLLndegaQALARAKEKSVEFGQQSEQISDiSREARALADKLE------SE 1220
Cdd:PRK04863  451 EQEATEELLSLEQklsVAQAAHSQFEQAYQLV-----RKIAGEVSRSEAWDVARELLRR-LREQRHLAEQLQqlrmrlSE 524

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1221 AQFDLKNAKDA----KDAVEKAHQLAKSAIDLQlkigtELRSEVGLELSHVKQSLGTVVQ----------------TSKE 1280
Cdd:PRK04863  525 LEQRLRQQQRAerllAEFCKRLGKNLDDEDELE-----QLQEELEARLESLSESVSEARErrmalrqqleqlqariQRLA 599

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1281 ALRKANEVYDTALTLLNDvnrQTQPEIDISQ-----------------LKKDAVAANERAdeLLKQITELSNSNG----- 1338
Cdd:PRK04863  600 ARAPAWLAAQDALARLRE---QSGEEFEDSQdvteymqqllerereltVERDELAARKQA--LDEEIERLSQPGGsedpr 674

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1339 --------------ELFADFETEQE-LTEAL------------LKRAEQQ--QLEDI---------------------EL 1368
Cdd:PRK04863  675 lnalaerfggvllsEIYDDVSLEDApYFSALygparhaivvpdLSDAAEQlaGLEDCpedlyliegdpdsfddsvfsvEE 754

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1369 LERA----------------------KAAHDKATKAVEQGDNTLKEAnntYEKLAGFQSDVQRSSESAEK------ALQT 1420
Cdd:PRK04863  755 LEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAER---YATLSFDVQKLQRLHQAFSRfigshlAVAF 831

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1421 VPNIEKEIQNAESLISQAEEAL---DGANKNANEAKKNAQEAQL---KYAEQAS--------KDAELIRRKANETKVAAR 1486
Cdd:PRK04863  832 EADPEAELRQLNRRRVELERALadhESQEQQQRSQLEQAKEGLSalnRLLPRLNlladetlaDRVEEIREQLDEAEEAKR 911

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1487 NLREEADQLNhrvkLTEMDIFKLEESSTKDDNLvddaKRKVGQAKADTQEAQKQI---------------EKANADLTAI 1551
Cdd:PRK04863  912 FVQQHGNALA----QLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKN 983

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160 1552 KDELENLKdintGDLDRLEnrlatVEGEINRVNLTGRIEKYREQRTIQKNLIDKYDA---ELRELKDEVQNIGL 1622
Cdd:PRK04863  984 SDLNEKLR----QRLEQAE-----QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAkrqMLQELKQELQDLGV 1048
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 1218-1620 1.98e-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: 53.13  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1218 ESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSE----VGLElSHVKQSLGTVVQTSKEalrkanEVYDTAL 1293
Cdd:TIGR01612  529 DIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEEnedsIHLE-KEIKDLFDKYLEIDDE------IIYINKL 601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1294 TL--------LNDVNRQTQPEIDisqLKKDAVAANERADELLK----QITELSNSNGELFADFETE-------------Q 1348
Cdd:TIGR01612  602 KLelkekiknISDKNEYIKKAID---LKKIIENNNAYIDELAKispyQVPEHLKNKDKIYSTIKSElskiyeddidalyN 678

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1349 ELTeALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEAN-----NTYEKLAGFQSDVQRS-----SESAEKAL 1418
Cdd:TIGR01612  679 ELS-SIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHlsnieNKKNELLDIIVEIKKHihgeiNKDLNKIL 757

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1419 QTVPNIEKEIQNA--------------ESLIS----QAEEALDGANKNANEAKKNAQEAQlKYAEQASKDAELIRRKANE 1480
Cdd:TIGR01612  758 EDFKNKEKELSNKindyakekdelnkyKSKISeiknHYNDQINIDNIKDEDAKQNYDKSK-EYIKTISIKEDEIFKIINE 836

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1481 TKVAARNLREEADQL-----NHRVKL-TEMDIFKLEESSTKD---DNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAI 1551
Cdd:TIGR01612  837 MKFMKDDFLNKVDKFinfenNCKEKIdSEHEQFAELTNKIKAeisDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL 916

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410160  1552 KDELENLK--DINTGDLDRLENRLATVEGEINRvnltgRIEKYREQRTIQKNLIDKYDAELRELKDEVQNI 1620
Cdd:TIGR01612  917 KKVDEYIKicENTKESIEKFHNKQNILKEILNK-----NIDTIKESNLIEKSYKDKFDNTLIDKINELDKA 982
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1345-1496 2.07e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.69  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1345 ETEQELTEALLKRAE-QQQLEDIE-LLERAKAAHDKATKAVEQGDNTLKEANNTYEklagfqsDVQRSSESAEKALQTVP 1422
Cdd:COG1579    14 ELDSELDRLEHRLKElPAELAELEdELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLGNVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1423 N------IEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQlkyAEQASKDAELIRRKAnETKVAARNLREEADQLN 1496
Cdd:COG1579    87 NnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKA-ELDEELAELEAELEELE 162
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1071-1436 2.15e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1071 LSQTLDEIARTPVTNDDEFEAKLKAVQEKVAVLAQDARDNsgdggQTYAEVIDDLHKHLDSVREHLVSADKFQADANGEI 1150
Cdd:TIGR04523  340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN-----QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1151 DRARQNYTILDQITENAKKE---LQQALDLLNDEGAqalarAKEKSVE-----FGQQSEQISDISREARALADKLEseaq 1222
Cdd:TIGR04523  415 KKLQQEKELLEKEIERLKETiikNNSEIKDLTNQDS-----VKELIIKnldntRESLETQLKVLSRSINKIKQNLE---- 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1223 fdlKNAKDAKDAVEKAHQLAKSAIDLQLKIgTELRSEVglelshvKQSLGTVVQTSKEALRKANEVYDtaltLLNDVNRQ 1302
Cdd:TIGR04523  486 ---QKQKELKSKEKELKKLNEEKKELEEKV-KDLTKKI-------SSLKEKIEKLESEKKEKESKISD----LEDELNKD 550

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1303 TQpEIDISQLKKDAvaaneraDELLKQITELSNSNGELfadfETEQELTEALLKRAEQQQLEDIELLErakaahdKATKA 1382
Cdd:TIGR04523  551 DF-ELKKENLEKEI-------DEKNKEIEELKQTQKSL----KKKQEEKQELIDQKEKEKKDLIKEIE-------EKEKK 611

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410160  1383 VEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTV-----------PNIEKEIQNAESLIS 1436
Cdd:TIGR04523  612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIketikeirnkwPEIIKKIKESKTKID 676
mukB PRK04863
chromosome partition protein MukB;
1087-1621 2.52e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.65  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1087 DEFEAKLKAVQEKVAVLAQDARDnsgdggqtyaevIDDLHKHLDS-VREHLVSAdkFQADANGEIDRARQNYTILD-QIT 1164
Cdd:PRK04863  789 EQLRAEREELAERYATLSFDVQK------------LQRLHQAFSRfIGSHLAVA--FEADPEAELRQLNRRRVELErALA 854

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1165 ENAKKELQQAldllndegaQALARAKEKSVEFGQQSEQISDISREAraLADKLEsEAQFDLKNAKDAKDAVeKAHQLAKS 1244
Cdd:PRK04863  855 DHESQEQQQR---------SQLEQAKEGLSALNRLLPRLNLLADET--LADRVE-EIREQLDEAEEAKRFV-QQHGNALA 921

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1245 AIDLQLKIgteLRSEvglelshvkqslgtvvQTSKEALRKAnevYDTALTLLNDVNRQtqpeidisqlkKDAVAanerad 1324
Cdd:PRK04863  922 QLEPIVSV---LQSD----------------PEQFEQLKQD---YQQAQQTQRDAKQQ-----------AFALT------ 962

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1325 ELLKQITELSNSNGElfADFETEQELTEAL---LKRAEQQQLEDIELLERAKAAHDKATK----------AVEQgdnTLK 1391
Cdd:PRK04863  963 EVVQRRAHFSYEDAA--EMLAKNSDLNEKLrqrLEQAEQERTRAREQLRQAQAQLAQYNQvlaslkssydAKRQ---MLQ 1037

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1392 EANNTYEKLaGFQSDvqrsSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKY------AE 1465
Cdd:PRK04863 1038 ELKQELQDL-GVPAD----SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYhemreqVV 1112

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1466 QASKDAELIRRKANETKVAARNLREEadqlnhrvkLTEMDIFKLEESSTKD---------DN--------LVDDAK---R 1525
Cdd:PRK04863 1113 NAKAGWCAVLRLVKDNGVERRLHRRE---------LAYLSADELRSMSDKAlgalrlavaDNehlrdvlrLSEDPKrpeR 1183

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1526 KVG-----------QAKADTQ------EAQKQIEKANADLTaikDELEnlkdintgdldRLENRLATVEGEINRVnLTGR 1588
Cdd:PRK04863 1184 KVQfyiavyqhlreRIRQDIIrtddpvEAIEQMEIELSRLT---EELT-----------SREQKLAISSESVANI-IRKT 1248

                         570       580       590
                  ....*....|....*....|....*....|...
gi 665410160 1589 IEkyREQRTIqknlidkydaelRELKDEVQNIG 1621
Cdd:PRK04863 1249 IQ--REQNRI------------RMLNQGLQNIS 1267
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1295-1620 2.94e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 52.21  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1295 LLNDVNRQTQPEI-DISQLKKDAVAANERADELLKQITELSNSNgelfADFETEQELTEALLKRAEQQQLEDIELLERAK 1373
Cdd:PRK01156  170 KLKDVIDMLRAEIsNIDYLEEKLKSSNLELENIKKQIADDEKSH----SITLKEIERLSIEYNNAMDDYNNLKSALNELS 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1374 AAHDKATKAVEQgdntLKEANNtyeKLAGFQSDVQRSSESAEKALQTVPN--------IEKEIQNAESLISQAE--EALD 1443
Cdd:PRK01156  246 SLEDMKNRYESE----IKTAES---DLSMELEKNNYYKELEERHMKIINDpvyknrnyINDYFKYKNDIENKKQilSNID 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1444 GANKNANEAKKNAQEAQLKYAEQASKdaeliRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDA 1523
Cdd:PRK01156  319 AEINKYHAIIKKLSVLQKDYNDYIKK-----KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1524 KRKVGQAKADTQEAQKQIEKANADLTAIKDELENL---KDINTGDLDRLENRLATVEGEiNRVNLTGRI---EKYREQRT 1597
Cdd:PRK01156  394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLnqrIRALRENLDELSRNMEMLNGQ-SVCPVCGTTlgeEKSNHIIN 472

                         330       340
                  ....*....|....*....|...
gi 665410160 1598 IQKNLIDKYDAELRELKDEVQNI 1620
Cdd:PRK01156  473 HYNEKKSRLEEKIREIEIEVKDI 495
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1246-1422 2.96e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1246 IDLQlKIGTELRsevglELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQtqpeidISQLKKDAVAANERADE 1325
Cdd:COG1579    10 LDLQ-ELDSELD-----RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE------IKRLELEIEEVEARIKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1326 LLKQITELSNSngELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEK-LAGFQ 1404
Cdd:COG1579    78 YEEQLGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAELE 155

                         170
                  ....*....|....*...
gi 665410160 1405 SDVQRSSESAEKALQTVP 1422
Cdd:COG1579   156 AELEELEAEREELAAKIP 173
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1065-1570 3.23e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 52.10  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1065 RAKLFNLSQTLDEIARtpvtnddEFEAKLKAVQEKVAVLAQDARDnsgdggqtYAEVIDDLHKHLDsvrehlvsadkfqa 1144
Cdd:pfam01576   63 RARLAARKQELEEILH-------ELESRLEEEEERSQQLQNEKKK--------MQQHIQDLEEQLD-------------- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1145 dangEIDRARQNYTiLDQITENAK-KELQQALDLLNDEGAQALARAK---EKSVEFGQQSEQISDISREARALADKLE-- 1218
Cdd:pfam01576  114 ----EEEAARQKLQ-LEKVTTEAKiKKLEEDILLLEDQNSKLSKERKlleERISEFTSNLAEEEEKAKSLSKLKNKHEam 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1219 -SEAQFDLKNAKDAKDAVEKA-HQLAKSAIDLQLKIgtelrSEVGLELSHVKQSLGtvvqtskealRKANEVyDTALTLL 1296
Cdd:pfam01576  189 iSDLEERLKKEEKGRQELEKAkRKLEGESTDLQEQI-----AELQAQIAELRAQLA----------KKEEEL-QAALARL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1297 NDvnrqtqpeidiSQLKKDAvaaneradeLLKQITELSNSNGELFADFETEQ----------------------ELTEAL 1354
Cdd:pfam01576  253 EE-----------ETAQKNN---------ALKKIRELEAQISELQEDLESERaarnkaekqrrdlgeelealktELEDTL 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1355 LKRAEQQQLE---DIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNA 1431
Cdd:pfam01576  313 DTTAAQQELRskrEQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1432 ESLISQAeealdganKNANEAKKNAQEAQLKYAEQASKDAELIRRKANEtKVAarNLREEADQLNHrvkltemdifKLEE 1511
Cdd:pfam01576  393 LRTLQQA--------KQDSEHKRKKLEGQLQELQARLSESERQRAELAE-KLS--KLQSELESVSS----------LLNE 451

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160  1512 SSTKDDNLVDDakrkVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLE 1570
Cdd:pfam01576  452 AEGKNIKLSKD----VSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1156-1627 3.81e-06

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 52.14  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1156 NYTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQqsEQISDIsrearalADKLEseaqFDLKNAKDAKDAV 1235
Cdd:PTZ00440  259 PSNNYDNYLNRAKELLESGSDLINKIKKELGDNKTIYSINFIQ--EEIGDI-------IKRYN----FHLKKIEKGKEYI 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1236 EKahqLAKSAIDLQLKIgTELRS---EVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQL 1312
Cdd:PTZ00440  326 KR---IQNNNIPPQVKK-DELKKkyfESAKHYASFKFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETLLDSEYF 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1313 KKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIE------------------LLERAKA 1374
Cdd:PTZ00440  402 ISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEIIEIKKKYDEKINELKksinqlktlisimksfydLIISEKD 481

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1375 AHDKATK-------AVEQGD------NTLKEANNT-----------YEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQN 1430
Cdd:PTZ00440  482 SMDSKEKkessdsnYQEKVDellqiiNSIKEKNNIvnnnfkniedyYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKL 561

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1431 AESLISQAEEALDGANKNANEAKK--NAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFK 1508
Cdd:PTZ00440  562 KRSMKNDIKNKIKYIEENVDHIKDiiSLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELL 641

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1509 LEESSTKDDNLV----DDAKRKVGQAKADTQEAQKQIEKANAD-----LTAIKDELENLKDINTGDLDRLENRLatvege 1579
Cdd:PTZ00440  642 DELSHFLDDHKYlyheAKSKEDLQTLLNTSKNEYEKLEFMKSDnidniIKNLKKELQNLLSLKENIIKKQLNNI------ 715

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 665410160 1580 inRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGLISKAL 1627
Cdd:PTZ00440  716 --EQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEF 761
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 1283-1545 5.15e-06

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 51.16  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1283 RKANEVYDTALTLLNDVNRQTQP-------EIDISQLKKDAVAANERADE----------LLKQIteLSNSNGELFADFE 1345
Cdd:pfam05262  100 RSDAETIAKFITIYNAVYRGDLDyfkefykEVVTKSLTKENAGLARRYDQwpgktqivipLKKNI--LSGNVSDVDTDSI 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1346 TEQELTEALL--------KRAEQQQLEDIELLERAKAAHDKAtkaveqgdntlKEANNTYEKLAGFQSDVQRSSESAEKA 1417
Cdd:pfam05262  178 SDKKVVEALRednekgvnFRRDMTDLKERESQEDAKRAQQLK-----------EELDKKQIDADKAQQKADFAQDNADKQ 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1418 LQTVPNIEKEIQNAEslisqaeealDGANKNANEAKKNAQEAQLKYAEQASKDAElirrKANETkvAARNLREEADQLNH 1497
Cdd:pfam05262  247 RDEVRQKQQEAKNLP----------KPADTSSPKEDKQVAENQKREIEKAQIEIK----KNDEE--ALKAKDHKAFDLKQ 310

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 665410160  1498 RVKLTE-MDIFKLEESSTKDDNLVDDAKRKVGQAKAD-TQEAQKQIEKAN 1545
Cdd:pfam05262  311 ESKASEkEAEDKELEAQKKREPVAEDLQKTKPQVEAQpTSLNEDAIDSSN 360
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1142-1367 5.20e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.44  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1142 FQADANGEIDRARQNYTILDQITENAKKELQQALdllndegaQALAR--AKEKSVEfgQQSEqisdisrEARALADKLES 1219
Cdd:COG1842    10 IRANINALLDKAEDPEKMLDQAIRDMEEDLVEAR--------QALAQviANQKRLE--RQLE-------ELEAEAEKWEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1220 EAQFDLKNAKD--AKDAVEKAHQLAKSAIDLQlkigTELrsevglelshvkQSLGTVVQTSKEALRKANEVYDTALTlln 1297
Cdd:COG1842    73 KARLALEKGREdlAREALERKAELEAQAEALE----AQL------------AQLEEQVEKLKEALRQLESKLEELKA--- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1298 dvnrqtqpeidisqlKKDAVAANERADELLKQITEL-----SNSNGELFADFETEQELTEAllkRAE-----------QQ 1361
Cdd:COG1842   134 ---------------KKDTLKARAKAAKAQEKVNEAlsgidSDDATSALERMEEKIEEMEA---RAEaaaelaagdslDD 195


                  ....*.
gi 665410160 1362 QLEDIE 1367
Cdd:COG1842   196 ELAELE 201
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 1116-1558 5.60e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 50.99  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1116 QTYAEVIDdlhKHLDSVREHLVSA----DKFQ-ADANGEIDRARQnytILDQITENAKKELQQALDLLNDEgaqalarak 1190
Cdd:PRK04778   71 QKWDEIVT---NSLPDIEEQLFEAeelnDKFRfRKAKHEINEIES---LLDLIEEDIEQILEELQELLESE--------- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1191 EKSVEfgqQSEQISDISREARAlaDKLESEAQFDlknakDAKDAVEKahQLAKsaIDLQLKIGTELrSEVGlelSHVKqs 1270
Cdd:PRK04778  136 EKNRE---EVEQLKDLYRELRK--SLLANRFSFG-----PALDELEK--QLEN--LEEEFSQFVEL-TESG---DYVE-- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1271 lgtvvqtskealrkANEVYDTALTLLNDVNRQTQ--PEIdISQLKKdavaaneradELLKQITELSN------SNGELFA 1342
Cdd:PRK04778  196 --------------AREILDQLEEELAALEQIMEeiPEL-LKELQT----------ELPDQLQELKAgyrelvEEGYHLD 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1343 DFETEQELT---------EALLKRAE----QQQLEDI--------ELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLa 1401
Cdd:PRK04778  251 HLDIEKEIQdlkeqidenLALLEELDldeaEEKNEEIqeridqlyDILEREVKARKYVEKNSDTLPDFLEHAKEQNKEL- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1402 gfQSDVQRSSES---AEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNaQEAQLKYAEQASKDAElirrka 1478
Cdd:PRK04778  330 --KEEIDRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEE-LEEILKQLEEIEKEQE------ 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1479 nETKVAARNLREEADQLNHRVkltemDIFKLEESSTK------------DD-----NLVDDAKRKVG----QAKADTQEA 1537
Cdd:PRK04778  401 -KLSEMLQGLRKDELEAREKL-----ERYRNKLHEIKryleksnlpglpEDylemfFEVSDEIEALAeeleEKPINMEAV 474

                         490       500
                  ....*....|....*....|.
gi 665410160 1538 QKQIEKANADLTAIKDELENL 1558
Cdd:PRK04778  475 NRLLEEATEDVETLEEETEEL 495
mukB PRK04863
chromosome partition protein MukB;
1055-1444 5.66e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.50  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1055 NLVQDAADLhRAKLFNLSQTLDEIARTPVtnddEFEAKLKAVQEKVAVLAQD---ARD--NSGDGGQTYAEVIDDLHKHL 1129
Cdd:PRK04863  283 VHLEEALEL-RRELYTSRRQLAAEQYRLV----EMARELAELNEAESDLEQDyqaASDhlNLVQTALRQQEKIERYQADL 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1130 DSVREHLVSADKFQADANGEIDRARQNYTILDQITENAKKEL---QQALDLLN------DEGAQALARAKE--------- 1191
Cdd:PRK04863  358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQtraiqyQQAVQALERAKQlcglpdlta 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1192 KSV-----EFGQQSEQISDisrEARALADKLESeaqfdlknAKDAKDAVEKAHQLAKsaidlqlKIGTEL-RSEVGlels 1265
Cdd:PRK04863  438 DNAedwleEFQAKEQEATE---ELLSLEQKLSV--------AQAAHSQFEQAYQLVR-------KIAGEVsRSEAW---- 495

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1266 hvkqslgtvvQTSKEALRKANEvydtaltLLNDVNRQTQPEIDISQLKKDaVAANERADELLKQITELSNSNGELFADFE 1345
Cdd:PRK04863  496 ----------DVARELLRRLRE-------QRHLAEQLQQLRMRLSELEQR-LRQQQRAERLLAEFCKRLGKNLDDEDELE 557

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1346 TEQELTEALLKRAEQQQLEDIellERAKAAHDKaTKAVEQGDNTLK-------EANNTYEKLAGFQSDVQRSSESAEKAL 1418
Cdd:PRK04863  558 QLQEELEARLESLSESVSEAR---ERRMALRQQ-LEQLQARIQRLAarapawlAAQDALARLREQSGEEFEDSQDVTEYM 633

                         410       420
                  ....*....|....*....|....*.
gi 665410160 1419 QTVPNIEKEIQNAESLISQAEEALDG 1444
Cdd:PRK04863  634 QQLLERERELTVERDELAARKQALDE 659
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 1328-1614 6.94e-06

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: 50.91  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1328 KQITELSNSNGELFADFETEQEL-----TEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEK--- 1399
Cdd:pfam09731   67 LQPSVVSAVTGESKEPKEEKKQVkiprqSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESata 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1400 -LAGFQSDVQRSSESAEKALQTVPNIEKE-IQNAESLISQAEEALDGANKNANEAKKNAQEAQLKY---AEQASKDAELI 1474
Cdd:pfam09731  147 vAKEAKDDAIQAVKAHTDSLKEASDTAEIsREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPlldAAPETPPKLPE 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1475 RRKANETKV-AARNLREEADQLNHRVKlTEMDIFKLE-----------------ESSTKDDNLVDDAKRKVGQA------ 1530
Cdd:pfam09731  227 HLDNVEEKVeKAQSLAKLVDQYKELVA-SERIVFQQElvsifpdiipvlkednlLSNDDLNSLIAHAHREIDQLskklae 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1531 --KADTQEAQKQIEKANADL-TAIKDELENLKDINTGDL----------------------------------DRLENRL 1573
Cdd:pfam09731  306 lkKREEKHIERALEKQKEELdKLAEELSARLEEVRAADEaqlrleferereeiresyeeklrtelerqaeaheEHLKDVL 385

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 665410160  1574 ATVEGEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELK 1614
Cdd:pfam09731  386 VEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLE 426
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1392-1620 7.27e-06

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: 49.26  E-value: 7.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1392 EANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQ--LKYAE-QAS 1468
Cdd:pfam00261    9 ELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESErgRKVLEnRAL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1469 KDAELIRRKANETKvAARNLREEAD----QLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKA 1544
Cdd:pfam00261   89 KDEEKMEILEAQLK-EAKEIAEEADrkyeEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1545 NADLTAIKDELENLKDintgDLDRLENR-------LATVEGEINRvnLTGRIEKYREqrtiqknlidKYDAELRELKDEV 1617
Cdd:pfam00261  168 SEREDKYEEQIRFLTE----KLKEAETRaefaersVQKLEKEVDR--LEDELEAEKE----------KYKAISEELDQTL 231


                   ...
gi 665410160  1618 QNI 1620
Cdd:pfam00261  232 AEL 234
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1424-1495 7.27e-06

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 47.05  E-value: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAE-------SLISQAEEALDGANKNA----NEAKKNAQEAQLKYAEQASKDAELIRRKAN-----ETKVAARN 1487
Cdd:cd06503    35 IAESLEEAEkakeeaeELLAEYEEKLAEARAEAqeiiEEARKEAEKIKEEILAEAKEEAERILEQAKaeieqEKEKALAE 114


                  ....*...
gi 665410160 1488 LREEADQL 1495
Cdd:cd06503   115 LRKEVADL 122
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1165-1600 8.14e-06

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: 50.74  E-value: 8.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1165 ENAKKELQQALDLLNDEGAQALARAKEKS--VEFGQQSEQISDISREA-RALADKLESEAQfDLKNAKDAKDAVEKAHQL 1241
Cdd:TIGR00618  534 EQTYAQLETSEEDVYHQLTSERKQRASLKeqMQEIQQSFSILTQCDNRsKEDIPNLQNITV-RLQDLTEKLSEAEDMLAC 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1242 AKSAIDLQLKIGTELRsEVGLELSHVKQSLgtvvQTSKEALRKanevydTALTLLNDvnRQTQPEIDISQLKKDAVAANE 1321
Cdd:TIGR00618  613 EQHALLRKLQPEQDLQ-DVRLHLQQCSQEL----ALKLTALHA------LQLTLTQE--RVREHALSIRVLPKELLASRQ 679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1322 RAdellkqITELSNSNGELFADFET-EQELTeaLLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKL 1400
Cdd:TIGR00618  680 LA------LQKMQSEKEQLTYWKEMlAQCQT--LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ 751

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1401 AGFQ-----SDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEaldganknaneakkNAQEAQLKYAE--QASKDAEL 1473
Cdd:TIGR00618  752 ARTVlkartEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE--------------DTHLLKTLEAEigQEIPSDED 817

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1474 IRRKANETKVaarnlREEADQLNhrvkltemdifKLEESSTKDDNLvddaKRKVGQaKADTQEAQKQIEKANADLTAIKD 1553
Cdd:TIGR00618  818 ILNLQCETLV-----QEEEQFLS-----------RLEEKSATLGEI----THQLLK-YEECSKQLAQLTQEQAKIIQLSD 876

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 665410160  1554 ELENLKDINtgdLDRLENRLATVEGEINRVNLTGRIEKYREQRTIQK 1600
Cdd:TIGR00618  877 KLNGINQIK---IQFDGDALIKFLHEITLYANVRLANQSEGRFHGRY 920
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1501-1629 9.73e-06

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: 49.29  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1501 LTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEI 1580
Cdd:cd22656    97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAI 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1581 NRVN---LTGRIEKYRE------QRTIQ--KNLIDKYDAELRELKDEVQNIGLISKALPD 1629
Cdd:cd22656   177 ARKEikdLQKELEKLNEeyaaklKAKIDelKALIADDEAKLAAALRLIADLTAADTDLDN 236
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1117-1596 1.23e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 50.35  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1117 TYAEViDDLHKHLDSVREHLVSADkFQADANGEIDRARQNYTIldqiTENAKK-ELQQALDLLNDEGAQALARAKEKSVE 1195
Cdd:TIGR00618   56 RRSEV-IRSLNSLYAAPSEAAFAE-LEFSLGTKIYRVHRTLRC----TRSHRKtEQPEQLYLEQKKGRGRILAAKKSETE 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1196 fgqqsEQISDISrearaladKLESEAqfdlknakdakdaVEKAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQ--SLGT 1273
Cdd:TIGR00618  130 -----EVIHDLL--------KLDYKT-------------FTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQytQLAL 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1274 VVQTSKEALRKANEVYDTALTLLND-VNRQTQPEIDISQLKKDavaaneradeLLKQITELSNSNGELFADFETEQELTE 1352
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEK----------ELKHLREALQQTQQSHAYLTQKREAQE 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1353 ALLK--RAEQQQLEDIELLERAKAAHDKATKAVEQgdntlkeaNNTYEKLAGFQSDVQRSSESAEKALQtvpniekEIQN 1430
Cdd:TIGR00618  254 EQLKkqQLLKQLRARIEELRAQEAVLEETQERINR--------ARKAAPLAAHIKAVTQIEQQAQRIHT-------ELQS 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1431 AESLISQAEEaldganKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLE 1510
Cdd:TIGR00618  319 KMRSRAKLLM------KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1511 ESSTKDDNLVDDAKRKVGQAKADTQ------------EAQKQIEKANADL--TAIKDELENLKDINTG------DLDRLE 1570
Cdd:TIGR00618  393 QKLQSLCKELDILQREQATIDTRTSafrdlqgqlahaKKQQELQQRYAELcaAAITCTAQCEKLEKIHlqesaqSLKERE 472

                          490       500
                   ....*....|....*....|....*.
gi 665410160  1571 NRLATVEGEINRVNLTGRIEKYREQR 1596
Cdd:TIGR00618  473 QQLQTKEQIHLQETRKKAVVLARLLE 498
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1455-1621 1.42e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 48.75  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1455 NAQEAQLK-YAEQASKDAELIRRKANETKVAARNLREEADQLNHRVK-LTEmdifKLEESSTKDDNLVDdakrKVGQAKA 1532
Cdd:COG1340     7 SSSLEELEeKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKeLRE----EAQELREKRDELNE----KVKELKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1533 DTQEAQKQIEKANADLTAIKDELENLKDiNTGDLDRLENRLA-----------TVEGE---INRV-NLTGRIEKYREQRT 1597
Cdd:COG1340    79 ERDELNEKLNELREELDELRKELAELNK-AGGSIDKLRKEIErlewrqqtevlSPEEEkelVEKIkELEKELEKAKKALE 157

                         170       180
                  ....*....|....*....|....
gi 665410160 1598 IQKNLIDKYdAELRELKDEVQNIG 1621
Cdd:COG1340   158 KNEKLKELR-AELKELRKEAEEIH 180
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
1147-1501 1.42e-05

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 49.27  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1147 NGEIDRARQNYTILDQITENAKKEL--QQALDLLNDEGAQ-ALARAKEKSVEFGQQSEQIsDISREARaladklesEAQF 1223
Cdd:COG1538    13 NPDLRAARARVEAARAQLRQARAGLlpSQELDLGGKRRARiEAAKAQAEAAEADLRAARL-DLAAEVA--------QAYF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1224 DLKNAKDAKDAVEKAHQLAKSAIDLqlkigTELRSEVG----LELSHVKQSLGTVvQTSKEALRKANEVYDTALTLLndV 1299
Cdd:COG1538    84 DLLAAQEQLALAEENLALAEELLEL-----ARARYEAGlasrLDVLQAEAQLAQA-RAQLAQAEAQLAQARNALALL--L 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1300 NRQTQPEIDISQLKKDAVAANERADELLKQiteLSNSNGELFAdFETEQELTEALLKRAEQQQLEDIELlerakaahdKA 1379
Cdd:COG1538   156 GLPPPAPLDLPDPLPPLPPLPPSLPGLPSE---ALERRPDLRA-AEAQLEAAEAEIGVARAAFLPSLSL---------SA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1380 TKAVEQGDNTLKEANNTYekLAGF------------QSDVQRSSESAEKAL----QTVPNIEKEIQNAESLISQAEEALD 1443
Cdd:COG1538   223 SYGYSSSDDLFSGGSDTW--SVGLslslplfdggrnRARVRAAKAQLEQAEaqyeQTVLQALQEVEDALAALRAAREQLE 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1444 GANKNANEAKKNAQEAQLKYAEQASKDAELI--RRKANETKVAARNLReeADQLNHRVKL 1501
Cdd:COG1538   301 ALEEALEAAEEALELARARYRAGLASLLDVLdaQRELLQAQLNLIQAR--YDYLLALVQL 358
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1274-1557 1.68e-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: 49.79  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1274 VVQTSKEALRKANEVYDTALTLLNDV-NRQTQPEIDISQLKKDAVAANE---RADE----LLKQITELSNSNGELFADFE 1345
Cdd:pfam01576    6 EMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNALQEQLQAETElcaEAEEmrarLAARKQELEEILHELESRLE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1346 TEQELTEALL--KRAEQQQLEDIE-LLERAKAAHDKAtkaveQGDNTLKEAnntyeKLAGFQSDV-----QRSSESAEKA 1417
Cdd:pfam01576   86 EEEERSQQLQneKKKMQQHIQDLEeQLDEEEAARQKL-----QLEKVTTEA-----KIKKLEEDIllledQNSKLSKERK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1418 LqtvpnIEKEIQNAESLISQAEEALDGANK--NANEAKKNAQEAQLKYAEQASKDAELIRRKanetkvaarnLREEADQL 1495
Cdd:pfam01576  156 L-----LEERISEFTSNLAEEEEKAKSLSKlkNKHEAMISDLEERLKKEEKGRQELEKAKRK----------LEGESTDL 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665410160  1496 NHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELEN 1557
Cdd:pfam01576  221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1201-1612 1.90e-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: 49.66  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1201 EQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAhQLAKSAIDLQLKIGTELRSEVglelshvkQSLGTVVQTSKE 1280
Cdd:TIGR00606  695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA-PGRQSIIDLKEKEIPELRNKL--------QKVNRDIQRLKN 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1281 ALRKANEVYDT-------ALTLLNDVN--RQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELT 1351
Cdd:TIGR00606  766 DIEEQETLLGTimpeeesAKVCLTDVTimERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1352 EALLKRAEQQQlEDIELLEraKAAHDKATKAVEQGDNTLKE---ANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEI 1428
Cdd:TIGR00606  846 ELNRKLIQDQQ-EQIQHLK--SKTNELKSEKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1429 QNAESLISQAEEALDGANKNANEAKKNAQE--AQLKYAEQASKDAELIRRKANETKVAARNLREEADQlNHRVKLTEmDI 1506
Cdd:TIGR00606  923 QEKEELISSKETSNKKAQDKVNDIKEKVKNihGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECE-KHQEKINE-DM 1000

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1507 FKLEESstkddnlvddakrkvgqakADTQEAQKQIEKANADLTAIKDELENL--------KDINTGDLDRLENRLATVEG 1578
Cdd:TIGR00606 1001 RLMRQD-------------------IDTQKIQERWLQDNLTLRKRENELKEVeeelkqhlKEMGQMQVLQMKQEHQKLEE 1061

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 665410160  1579 EI-----NRVNLTGRIEKYREQRTIQKnlidkydAELRE 1612
Cdd:TIGR00606 1062 NIdlikrNHVLALGRQKGYEKEIKHFK-------KELRE 1093
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 359-414 2.15e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160   359 CNCNGLA---DKCFFdanlfnrtgHGGHCLdCRENRDGPNCERCKENFYMRDDGYCVNC 414
Cdd:pfam00053    1 CDCNPHGslsDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 1166-1562 2.19e-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: 49.44  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1166 NAKKE----LQQALDLLNdegaqalARAKEKSVEFGQQSEQISDISREARALADKLEseaqfDLKNAKDAKDavEKAHQL 1241
Cdd:pfam10174  334 TAKEQraaiLQTEVDALR-------LRLEEKESFLNKKTKQLQDLTEEKSTLAGEIR-----DLKDMLDVKE--RKINVL 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1242 AKSAIDLQL------KIGTELRSEVglelshvkQSLGTVVQTSkealrkanevyDTALTLLNDV---------------- 1299
Cdd:pfam10174  400 QKKIENLQEqlrdkdKQLAGLKERV--------KSLQTDSSNT-----------DTALTTLEEAlsekeriierlkeqre 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1300 --NRQTQPEIDisQLKKDAVAANERADELLKQITELSNSNGELFadfETEQELTEALLKRAEQQQLEDIELLERAkaahD 1377
Cdd:pfam10174  461 reDRERLEELE--SLKKENKDLKEKVSALQPELTEKESSLIDLK---EHASSLASSGLKKDSKLKSLEIAVEQKK----E 531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1378 KATKAVEQgdntLKEANNTYE----------KLAGFQSDVQRSSESAEKA----------LQTVPN----IEKEIQNAES 1433
Cdd:pfam10174  532 ECSKLENQ----LKKAHNAEEavrtnpeindRIRLLEQEVARYKEESGKAqaeverllgiLREVENekndKDKKIAELES 607

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1434 LISQA--EEALDGANKNAN---EAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMdifK 1508
Cdd:pfam10174  608 LTLRQmkEQNKKVANIKHGqqeMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQ---S 684

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160  1509 LEESSTKDDNLvddakrkvgqakadTQEAQKQIE-----KANADLTAIKDelenlKDIN 1562
Cdd:pfam10174  685 LAEKDGHLTNL--------------RAERRKQLEeilemKQEALLAAISE-----KDAN 724
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1309-1567 2.51e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.65  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1309 ISQLKKDAVAANERADELLKQITElsnsngELFADFETEQELtealLKRAEQQQLEDielLERAKAAHDKATKAVEQGDN 1388
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQAE------ELQQKQAAEQER----LKQLEKERLAA---QEQKKQAEEAAKQAALKQKQ 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1389 TLKEANNTYE--KLAGfQSDVQRSSESAEKAlqtvpniEKEiqnaesliSQAEEALDGANKNANEAKKNAQ-EAQLKYAE 1465
Cdd:PRK09510  134 AEEAAAKAAAaaKAKA-EAEAKRAAAAAKKA-------AAE--------AKKKAEAEAAKKAAAEAKKKAEaEAAAKAAA 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1466 QASKDAElirrkANETKVAARNLREEADQlnhrvkltemdifkleesstkddnlvdDAKRKVGQAKADTQE-AQKQIEKA 1544
Cdd:PRK09510  198 EAKKKAE-----AEAKKKAAAEAKKKAAA---------------------------EAKAAAAKAAAEAKAaAEKAAAAK 245

                         250       260
                  ....*....|....*....|...
gi 665410160 1545 NADLTAIKDELENLKDInTGDLD 1567
Cdd:PRK09510  246 AAEKAAAAKAAAEVDDL-FGGLD 267
COG4995 COG4995
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
1055-1520 2.81e-05

Uncharacterized conserved protein, contains CHAT domain [Function unknown];


Pssm-ID: 444019 [Multi-domain]  Cd Length: 711  Bit Score: 48.81  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1055 NLVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEFEAKLKAVQEKVAVLAQDARDNSGDGGQTYAEVIDDLHKHLDSVRE 1134
Cdd:COG4995     4 LALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1135 HLVSADKFQADANGEIDRARQNYTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALA 1214
Cdd:COG4995    84 ALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1215 DKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALT 1294
Cdd:COG4995   164 ALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLAL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1295 LLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKA 1374
Cdd:COG4995   244 AAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAAL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1375 AHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKA-LQTVPNIEKEIQNAESLISQAEEALDGANKNANEAK 1453
Cdd:COG4995   324 LLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAAlLLLLAALLALLLEALLLLLLALLAALLLLAAALLAL 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160 1454 KNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLV 1520
Cdd:COG4995   404 AAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAELPGIKRLV 470
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1435-1619 2.84e-05

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: 47.33  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1435 ISQAEEALDGANKNANEAKKNAQEAQlKYAEQASKDAELIRRKanetkvaARNLREEADQLNHRV-----KLTEMD---- 1505
Cdd:pfam00261    3 MQQIKEELDEAEERLKEAMKKLEEAE-KRAEKAEAEVAALNRR-------IQLLEEELERTEERLaealeKLEEAEkaad 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1506 ----IFK-LEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDintgDLDRLENRLATVEGEI 1580
Cdd:pfam00261   75 eserGRKvLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEE----RAELAESKIVELEEEL 150

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 665410160  1581 NRV-----NLTGRIEKYREQRtiqknliDKYDAELRELKDEVQN 1619
Cdd:pfam00261  151 KVVgnnlkSLEASEEKASERE-------DKYEEQIRFLTEKLKE 187
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 1090-1457 3.44e-05

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 48.18  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1090 EAKLKAVQEKVAVLAQDARDNSGDGGQTYaeVIDDLHKHLDSvrEHLVSADKFQADANGEIDRARQNYTI---------- 1159
Cdd:TIGR04320    6 QAELNQAQAKVDKANALAGVNTITLPANY--NIDALKNIYES--GDFDNSDAAKAEAEKAAAEAKSLNNYksnaadknrt 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1160 --LDQITENAKKELQQ-ALDLLND-------------EGAQALARA------KEKSVEFGQQSEQISDIsreARALADKL 1217
Cdd:TIGR04320   82 vdINNLTDEQQNELSQyAADLINQvrkqlglppvvvtEGSLDFAQAvakaykKDNSGTGGHDETAINKA---AAENGLDN 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1218 ESE------AQFDLKNAKDAKDAVEKAhqlaksaidlqlkIGTELRSEVGLELSHVKQSLGTVVQTSKEALrkanevydt 1291
Cdd:TIGR04320  159 TYEnlgsisSNNENTTMDDLKRAIYDS-------------ILGMLFNDADSNWGHAQNLLGDDKINAGAYL--------- 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1292 ALTLLNDVNRQTQPEIdisqlkkdaVAANERADELLKQITELSNSNGELfADFETEQELTEALLKRAEQQQLEDIELLER 1371
Cdd:TIGR04320  217 GVSISNDGGVTIHFVN---------FNDSYIADGNKFDKTPIPNPPNSL-AALQAKLATAQADLAAAQTALNTAQAALTS 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1372 AKAAHDKATKAVEQGDNTLKEANNTYEKLAgfqsdvQRSSESAEKALQtvpniekeiqNAESLISQAEEALdgANKNANE 1451
Cdd:TIGR04320  287 AQTAYAAAQAALATAQKELANAQAQALQTA------QNNLATAQAALA----------NAEARLAKAKEAL--ANLNADL 348


                   ....*.
gi 665410160  1452 AKKNAQ 1457
Cdd:TIGR04320  349 AKKQAA 354
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 1310-1590 3.79e-05

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 48.14  E-value: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1310 SQLKKDAVAANERADELLKQITELSNSNGEL---FADFET---EQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAV 1383
Cdd:pfam19220   58 AQERAAYGKLRRELAGLTRRLSAAEGELEELvarLAKLEAalrEAEAAKEELRIELRDKTAQAEALERQLAAETEQNRAL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1384 EQGDNTLKEANNTYEKlagfqsDVQRssesAEKALQTVPN----IEKEIQNAESLI-SQAEEALDGANKNA-NEAKKNAQ 1457
Cdd:pfam19220  138 EEENKALREEAQAAEK------ALQR----AEGELATARErlalLEQENRRLQALSeEQAAELAELTRRLAeLETQLDAT 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1458 EAQLKYAEQaskdaelirRKANETKVAARNLREEADQLN-HRVKLTEMDIfKLEESSTKddnlVDDAKRKVGQAKA---D 1533
Cdd:pfam19220  208 RARLRALEG---------QLAAEQAERERAEAQLEEAVEaHRAERASLRM-KLEALTAR----AAATEQLLAEARNqlrD 273

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 665410160  1534 TQEAQKQIEKANADLTAIKDELE-NLKDINTgDLDRLENRLAtvEGEINRVNLTGRIE 1590
Cdd:pfam19220  274 RDEAIRAAERRLKEASIERDTLErRLAGLEA-DLERRTQQFQ--EMQRARAELEERAE 328
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1073-1630 4.24e-05

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 48.47  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1073 QTLDEIARTPVTNDDEfEAKLKAVQEKVAVLAQDARDNSGDGGQTYAEVIDDLhkhlDSVREHLVSADKF-QADANgEID 1151
Cdd:COG5271   455 EEEEAEAELDTEEDTE-SAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADS----DELTAEETSADDGaDTDAA-ADP 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1152 RARQNYTILDqitENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQ-------------SEQISDISREARALADKLE 1218
Cdd:COG5271   529 EDSDEDALED---ETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAetedatenadadeTEESADESEEAEASEDEAA 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1219 SEAQFDLKNAK-DAKDAVEKAHQLAKSAIDLQLKIGTElrsevglelshvkQSLGTVVQTSKEALRKANEvyDTALTLLN 1297
Cdd:COG5271   606 EEEEADDDEADaDADGAADEEETEEEAAEDEAAEPETD-------------ASEAADEDADAETEAEASA--DESEEEAE 670

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1298 DvnrQTQPEIDISQLKKDAVAANERADEllkqitelsNSNGELFADFETEQELTEALLKRAEQQ-QLEDIELLERAKAAH 1376
Cdd:COG5271   671 D---ESETSSEDAEEDADAAAAEASDDE---------EETEEADEDAETASEEADAEEADTEADgTAEEAEEAAEEAESA 738

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1377 DKATKAVEQGDNTLKEANNTYEKLagfQSDVQRSSESAEkalqtvpniekeiqnaESLISQAEEALDGANKNANEAKKNA 1456
Cdd:COG5271   739 DEEAASLPDEADAEEEAEEAEEAE---EDDADGLEEALE----------------EEKADAEEAATDEEAEAAAEEKEKV 799

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1457 QEAQLkyaeQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQE 1536
Cdd:COG5271   800 ADEDQ----DTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEA 875

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1537 AQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDE 1616
Cdd:COG5271   876 EEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEA 955

                         570
                  ....*....|....
gi 665410160 1617 VQNIGLISKALPDS 1630
Cdd:COG5271   956 GDEESDDAAADDAG 969
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1445-1586 4.45e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 47.35  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1445 ANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEEsstkddnlVDDAK 1524
Cdd:COG1566    83 AALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQE--------LDEAR 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1525 RKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDIN--TGDLDRLENRL------ATVEGEINRVNLT 1586
Cdd:COG1566   155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAqaEAALAQAELNLarttirAPVDGVVTNLNVE 224
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1142-1392 5.35e-05

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 46.21  E-value: 5.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1142 FQADANGEIDRARQNYTILDQITENAKKELQQALDLLndegAQALARAKEKSVEFGQQSEQISDisREARAladklesEA 1221
Cdd:pfam04012    9 VRANIHEGLDKAEDPEKMLEQAIRDMQSELVKARQAL----AQTIARQKQLERRLEQQTEQAKK--LEEKA-------QA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1222 QFDLKNAKDAKDAVEKAHQLAKSAidlqlkigTELRSEVGLELSHVKQslgtvVQTSKEALrkanevydtaltllndvnr 1301
Cdd:pfam04012   76 ALTKGNEELAREALAEKKSLEKQA--------EALETQLAQQRSAVEQ-----LRKQLAAL------------------- 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1302 qtqpEIDISQL--KKDAVAANE---RADELLKQIT-ELSN-SNGELFADFETEQELTEALLKRAEqqQLEDIELLErAKA 1374
Cdd:pfam04012  124 ----ETKIQQLkaKKNLLKARLkaaKAQEAVQTSLgSLSTsSATDSFERIEEKIEEREARADAAA--ELASAVDLD-AKL 196

                          250
                   ....*....|....*....
gi 665410160  1375 AHDKATKAV-EQGDNTLKE 1392
Cdd:pfam04012  197 EQAGIQMEVsEDVLARLKA 215
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 1165-1575 5.45e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.16  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1165 ENAKKELQQALDL-LNDEGAQA-LARAKEKSVEFGQ---QSEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAH 1239
Cdd:TIGR02917   73 AAAEKELRKALSLgYPKNQVLPlLARAYLLQGKFQQvldELPGKTLLDDEGAAELLALRGLAYLGLGQLELAQKSYEQAL 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1240 QLAKSAIDLQLkigtelrsevGL-ELSHVKQSLGTVVQTSKEALRKANEVYDtALTLLNDVNR-QTQPEIDISQLKKdAV 1317
Cdd:TIGR02917  153 AIDPRSLYAKL----------GLaQLALAENRFDEARALIDEVLTADPGNVD-ALLLKGDLLLsLGNIELALAAYRK-AI 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1318 AANER--ADELLkqiteLSNSNGELFADFETEQELtEALLKRAEQQ-QLEDIE-LLERAKAAHDKATKAVEQgdnTLKEA 1393
Cdd:TIGR02917  221 ALRPNniAVLLA-----LATILIEAGEFEEAEKHA-DALLKKAPNSpLAHYLKaLVDFQKKNYEDARETLQD---ALKSA 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1394 NNTYEK--LAGFQSDVQRSSESAE----KALQTVPN----------IEKEIQNAESLISQAEEALDGANKN--------- 1448
Cdd:TIGR02917  292 PEYLPAllLAGASEYQLGNLEQAYqylnQILKYAPNshqarrllasIQLRLGRVDEAIATLSPALGLDPDDpaalsllge 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1449 ---ANEAKKNAQEAQLKYAEQASKDAELIRRKA------NETKVAARNLrEEADQLN------------HRVKLTEMD-- 1505
Cdd:TIGR02917  372 aylALGDFEKAAEYLAKATELDPENAAARTQLGisklsqGDPSEAIADL-ETAAQLDpelgradlllilSYLRSGQFDka 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1506 --IFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKA----NADLTAIKdELENLkDINTGDLD----RLENRLAT 1575
Cdd:TIGR02917  451 laAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKAlsiePDFFPAAA-NLARI-DIQEGNPDdaiqRFEKVLTI 528
Caldesmon pfam02029
Caldesmon;
1301-1633 6.14e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 47.55  E-value: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1301 RQTQPEIDISQLKKDAVAANERADELLKQITElsNSNGELfadfETEQELTEALLKRAEQQQLEDIELLERAKAAHDKAT 1380
Cdd:pfam02029   21 RQKEEEEPSGQVTESVEPNEHNSYEEDSELKP--SGQGGL----DEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1381 kavEQGDNT-LKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQ--NAESLISQAEEALDGANKNANEAKKNAQ 1457
Cdd:pfam02029   95 ---DEKESVaERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQenKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1458 EAQLKY---AEQASKDAE-------LIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESStKDDNLVDDAKRKV 1527
Cdd:pfam02029  172 ENFAKEevkDEKIKKEKKvkyeskvFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE-EEAEVFLEAEQKL 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1528 GQ-----AKADTQEA----QKQIEKANadltaikdELENLKDIntgdldRLENRLATVEGEINRvnltGRIEKYR----- 1593
Cdd:pfam02029  251 EElrrrrQEKESEEFeklrQKQQEAEL--------ELEELKKK------REERRKLLEEEEQRR----KQEEAERklree 312

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 665410160  1594 EQRTIQKNLIDKYDAELRELKDEVQNIGLISKALPDSCFS 1633
Cdd:pfam02029  313 EEKRRMKEEIERRRAEAAEKRQKLPEDSSSEGKKPFKCFS 352
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 1373-1552 6.37e-05

Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.


Pssm-ID: 398808 [Multi-domain]  Cd Length: 180  Bit Score: 45.25  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1373 KAAHDkATKAVEqgdntlkeANNTYEKLAGFQSDVQ------RSSESAEKAL----QTVPNIEKEIQNAESLISQAEEAL 1442
Cdd:pfam05335   12 KAAQE-AKAAND--------AQAAAAEAAARQVKNQladkalQAAKAAEAALagkqQIVEQLEQELREAEAVVQEESASL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1443 DGANKNANEAKKNAQEAQ-----LKYAEQASKDA-ELIRRKANEtkvAARNLREEADqlnhrvkltemdifkleesstkd 1516
Cdd:pfam05335   83 QQSQANANAAQRAAQQAQqqleaLTAALKAAQANlENAEQVAAG---AQQELAEKTQ----------------------- 136

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 665410160  1517 dnLVDDAKRKVgqakadtQEAQKQIEKANADLTAIK 1552
Cdd:pfam05335  137 --LLEAAKKRV-------ERLQRQLAEARADLEKTK 163
PRK11281 PRK11281
mechanosensitive channel MscK;
1346-1601 6.79e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 47.98  E-value: 6.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1346 TEQELTEALlKRAEQQQLED----IELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAekalQTV 1421
Cdd:PRK11281   49 NKQKLLEAE-DKLVQQDLEQtlalLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLST----LSL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1422 PNIEKEIQNAESLISQAEEALDGANK---NANEAKKNAQeAQLkYAEQASKDAelIRRKANETKVAARNLREEA-DQLNh 1497
Cdd:PRK11281  124 RQLESRLAQTLDQLQNAQNDLAEYNSqlvSLQTQPERAQ-AAL-YANSQRLQQ--IRNLLKGGKVGGKALRPSQrVLLQ- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1498 rvklTEmdifkleesstkddnlvddakrkvgQAKADTQEAQKQIEKANADLtaIKDELENLKDINTGDLDRLENRLATVE 1577
Cdd:PRK11281  199 ----AE-------------------------QALLNAQNDLQRKSLEGNTQ--LQDLLQKQRDYLTARIQRLEHQLQLLQ 247

                         250       260
                  ....*....|....*....|....
gi 665410160 1578 GEINRVNLTGRIEKYREQRTIQKN 1601
Cdd:PRK11281  248 EAINSKRLTLSEKTVQEAQSQDEA 271
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1194-1493 6.97e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1194 VEFGQQSEQISDISREARALADkLESEAQFdLKNAKDAKDAVEKAH--QLAKSAIDLQLKIGTELRSevGLELSHVKQSl 1271
Cdd:COG3206    61 VEPQSSDVLLSGLSSLSASDSP-LETQIEI-LKSRPVLERVVDKLNldEDPLGEEASREAAIERLRK--NLTVEPVKGS- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1272 gTVVQTS------KEALRKANEVYDTALTLLNDVNRQTQPEIdISQLKKDAVAANERADELLKQITELSNSNGelFADFE 1345
Cdd:COG3206   136 -NVIEISytspdpELAAAVANALAEAYLEQNLELRREEARKA-LEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLS 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1346 TEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVEQGDNTLKE--ANNTYEKLAGFQSDVQRssESAEKALQ---- 1419
Cdd:COG3206   212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEA--ELAELSARytpn 289

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160 1420 --TVPNIEKEIQNAESLISQ-AEEALDGANKNANEAKknAQEAQLKyAEQASKDAELirRKANETKVAARNLREEAD 1493
Cdd:COG3206   290 hpDVIALRAQIAALRAQLQQeAQRILASLEAELEALQ--AREASLQ-AQLAQLEARL--AELPELEAELRRLEREVE 361
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1292-1500 7.33e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 7.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1292 ALTLLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELsnsNGELfADFETEQELTEALLKRAEQQQLEDIELLER 1371
Cdd:COG4942    12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQL-AALERRIAALARRIRALEQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1372 AKAAHDKATKAVEQGDNTLKE--------ANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEK---EIQNAESLISQAEE 1440
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAEllralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1441 ALDGANKNANEAKKNAQEAQLKYAEQASKDAEL---IRRKANETKVAARNLREEADQLNHRVK 1500
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQEAEELEALIA 230
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1394-1623 7.71e-05

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: 46.59  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1394 NNTYEKLAGFQSDVqrsSESAEKALQTVPNIEKEIQNaesLISQAEEALDgaNKNANEAKKNAQ---EAQLKYAEQASKD 1470
Cdd:cd22656    65 DDTYPSIVSLAGDI---YNYAQNAGGTIDSYYAEILE---LIDDLADATD--DEELEEAKKTIKallDDLLKEAKKYQDK 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1471 AELIRRK----ANETKVAARNLREEADQLNhrvkltemDIFKLEESSTKDDNL------VDDAKRKVG-QAKADTQEAQK 1539
Cdd:cd22656   137 AAKVVDKltdfENQTEKDQTALETLEKALK--------DLLTDEGGAIARKEIkdlqkeLEKLNEEYAaKLKAKIDELKA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1540 QIEKAN----------ADLTAIKDELENLKD-----INT------------GDLDRLENRLATVEGEINRVNLTgrieky 1592
Cdd:cd22656   209 LIADDEaklaaalrliADLTAADTDLDNLLAligpaIPAleklqgawqaiaTDLDSLKDLLEDDISKIPAAILA------ 282

                         250       260       270
                  ....*....|....*....|....*....|.
gi 665410160 1593 reqRTIQKNLIDKYdAELRELKDEVQNIGLI 1623
Cdd:cd22656   283 ---KLELEKAIEKW-NELAEKADKFRQNAYI 309
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1153-1252 7.99e-05

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 43.97  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1153 ARQNYtILDQItENAKKELQQALDLLNdEGAQALARAKEKSVEFGQQS-----EQISDISREARALADKLESEAQFDLKN 1227
Cdd:cd06503    30 EREEK-IAESL-EEAEKAKEEAEELLA-EYEEKLAEARAEAQEIIEEArkeaeKIKEEILAEAKEEAERILEQAKAEIEQ 106

                          90       100
                  ....*....|....*....|....*.
gi 665410160 1228 AKD-AKDAVEKahQLAKSAIDLQLKI 1252
Cdd:cd06503   107 EKEkALAELRK--EVADLAVEAAEKI 130
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1191-1470 8.38e-05

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 47.52  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1191 EKSVEFGQQSEQISDISREARALADKLESEAqfDLKNAKDakdavEKAHQLAKSAidlqlkiGTELRSEvglelSHVKQS 1270
Cdd:NF012221 1539 ESSQQADAVSKHAKQDDAAQNALADKERAEA--DRQRLEQ-----EKQQQLAAIS-------GSQSQLE-----STDQNA 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1271 LGTVVQTSKEALR-KANEVYDTALTLLNDVNrqtqpeidisQLKKDAVAANERADELLKQitelsnsngelFAD--FETE 1347
Cdd:NF012221 1600 LETNGQAQRDAILeESRAVTKELTTLAQGLD----------ALDSQATYAGESGDQWRNP-----------FAGglLDRV 1658

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1348 QE-LTEAllKRAEQQQLEDIEllERAKAAHDKATKAVEQGDNTLKeanNTYEKLAGFQSDVQRSSESAEKALQTVPNIEK 1426
Cdd:NF012221 1659 QEqLDDA--KKISGKQLADAK--QRHVDNQQKVKDAVAKSEAGVA---QGEQNQANAEQDIDDAKADAEKRKDDALAKQN 1731

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1427 EIQNAES----LISQAEEALD----GANKNANEAKKNAQEAQLKYAEQASKD 1470
Cdd:NF012221 1732 EAQQAESdanaAANDAQSRGEqdasAAENKANQAQADAKGAKQDESDKPNRQ 1783
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1149-1638 8.56e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.59  E-value: 8.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1149 EIDRARQNYTILDQITENAKKELQQALDLLNDegaqalarAKEKSVEFGQQSEQISDISREARALADKLEsEAQFDLKNA 1228
Cdd:PRK01156  160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEK--------LKSSNLELENIKKQIADDEKSHSITLKEIE-RLSIEYNNA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1229 KDAKDAVEKAHQLAKSAIDLQLKIGTELRS---------EVGLELSHVKQSLGTVvqTSKEALRKANEVYDTaLTLLNDV 1299
Cdd:PRK01156  231 MDDYNNLKSALNELSSLEDMKNRYESEIKTaesdlsmelEKNNYYKELEERHMKI--INDPVYKNRNYINDY-FKYKNDI 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1300 nrqtqpeIDISQLKKDAVAANERADELLKQITELsnsngelfadfetEQELTEALLKRAEQQQLED-IELLERAKAAHDK 1378
Cdd:PRK01156  308 -------ENKKQILSNIDAEINKYHAIIKKLSVL-------------QKDYNDYIKKKSRYDDLNNqILELEGYEMDYNS 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1379 ATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPN-IEKEIQNAESLISQAEEALDGANKNANEAKKNAQ 1457
Cdd:PRK01156  368 YLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNeINVKLQDISSKVSSLNQRIRALRENLDELSRNME 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1458 --EAQLK-------------------YAEQASKDAELIRRKANETKV---AARNLREEADQLN----------------- 1496
Cdd:PRK01156  448 mlNGQSVcpvcgttlgeeksnhiinhYNEKKSRLEEKIREIEIEVKDideKIVDLKKRKEYLEseeinksineynkiesa 527

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1497 -HRVKLTEMDIFKLEESSTKDDNLVD----------DAKRK-------------VGQAKADTQEAQKQIEKANADLTAIK 1552
Cdd:PRK01156  528 rADLEDIKIKINELKDKHDKYEEIKNrykslkledlDSKRTswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIE 607

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1553 DELENLKDINTGDLDRLENRLATVEGEIN--------RVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNIGLIS 1624
Cdd:PRK01156  608 IGFPDDKSYIDKSIREIENEANNLNNKYNeiqenkilIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687

                         570
                  ....*....|....
gi 665410160 1625 KALPDSCFSRNRLE 1638
Cdd:PRK01156  688 KALDDAKANRARLE 701
46 PHA02562
endonuclease subunit; Provisional
 1427-1630 9.05e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.93  E-value: 9.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1427 EIQNAESLISQAEEALDGANKNANEAKK----NAQEAQLKYaEQASKDAELIRRKANETKVAARNL-REEADQLNHRVKL 1501
Cdd:PHA02562  182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKY-DELVEEAKTIKAEIEELTDELLNLvMDIEDPSAALNKL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1502 TeMDIFKLE---ESSTKDDNL-------------VDDAKRKVGQAKADTQEAQKQIEKAN---ADLTAIKDELE----NL 1558
Cdd:PHA02562  261 N-TAAAKIKskiEQFQKVIKMyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNeqskKL 339

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1559 KDINTgDLDRLENRLATVEGEINRVNltGRIEKYREQRTIQKNLIDKYDAELRELKDEVQNI-------GLISKALPDS 1630
Cdd:PHA02562  340 LELKN-KISTNKQSLITLVDKAKKVK--AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELvkekyhrGIVTDLLKDS 415
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 1300-1620 1.05e-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: 46.77  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1300 NRQTQPEIDISQLKKDAVAANERADEL--LKQItelsNSNGELFADFETE----QELTEallkraeqQQLEDIE-LLERA 1372
Cdd:pfam06160    5 RKKIYKEIDELEERKNELMNLPVQEELskVKKL----NLTGETQEKFEEWrkkwDDIVT--------KSLPDIEeLLFEA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1373 KAAHD-----KATKAVEQGDNTLKEANNTYEK-LAGFQ----SDvQRSSESAEKAL------------------QTVPNI 1424
Cdd:pfam06160   73 EELNDkyrfkKAKKALDEIEELLDDIEEDIKQiLEELDelleSE-EKNREEVEELKdkyrelrktllanrfsygPAIDEL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1425 EKEIQNAESLISQAEEALDgaNKNANEAKKNAQEaqlkyaeqaskdaelirrkanetkvaarnLREEADQLNHRVKltem 1504
Cdd:pfam06160  152 EKQLAEIEEEFSQFEELTE--SGDYLEAREVLEK-----------------------------LEEETDALEELME---- 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1505 DIFKLeesstkddnlVDDAKRKVGQAKADTQEAQKQIEKAN---------ADLTAIKDELE-NLKDINTGDLDRLENRLA 1574
Cdd:pfam06160  197 DIPPL----------YEELKTELPDQLEELKEGYREMEEEGyalehlnvdKEIQQLEEQLEeNLALLENLELDEAEEALE 266

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 665410160  1575 TVEGEINrvNLTGRIEK-YREQRTIQKNL------IDKYDAELRELKDEVQNI 1620
Cdd:pfam06160  267 EIEERID--QLYDLLEKeVDAKKYVEKNLpeiedyLEHAEEQNKELKEELERV 317
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1122-1601 1.06e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 47.52  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1122 IDDLHKHLDSVREHLVSADKFQADANGEIDRARQNyTILDQItENAKKELQQALDLLndegaqalaRAKEKSVEfgqqse 1201
Cdd:PTZ00440 2152 IDKANKLSSELSEAVTNSEEIIENIKKEIIEINEN-TEMNTL-ENTADKLKELYENL---------KKKKNIIN------ 2214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1202 QISDISREARALADKLESEAQFDLknAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGlELSHVKQSLgtvvqtSKEA 1281
Cdd:PTZ00440 2215 NIYKKINFIKLQEIENSSEKYNDI--SKLFNNVVETQKKKLLDNKNKINNIKDKINDKEK-ELINVDSSF------TLES 2285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1282 LRKANEVYDTALTLLNDVnrQTQPEIDISQLKKDAVAAnERADELLKQITELSNSngelFADFETEQEL--TEALLKRAE 1359
Cdd:PTZ00440 2286 IKTFNEIYDDIKSNIGDL--YKLEDTNNDELKKVKLYI-ENITHLLNRINTLIND----LDNYQDENYGkdKNIELNNEN 2358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1360 QQQLEDI-ELLERAKAAHDKATKAVEQgDNTLKEANNTYEklagFQSDVQRSSES-AEKALQTVPNIEKEIQNAESLI-- 1435
Cdd:PTZ00440 2359 NSYIIKTkEKINNLKEEFSKLLKNIKR-NNTLCNNNNIKD----FISNIGKSVETiKQRFSSNLPEKEKLHQIEENLNei 2433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1436 -SQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARNLREEADQLNH---RVKLTEMDIFKLEE 1511
Cdd:PTZ00440 2434 kNIMNETKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDLIENVTSHNEKIKSELLIINDalrRVKEKKDEMNKLFN 2513

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1512 SSTKD-DNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEinrvnltgRIE 1590
Cdd:PTZ00440 2514 SLTENnNNNNNSAKNIVDNSTYIINELESHVSKLNELLSYIDNEIKELENEKLKLLEKAKIEESRKERE--------RIE 2585

                         490
                  ....*....|....
gi 665410160 1591 KYRE---QRTIQKN 1601
Cdd:PTZ00440 2586 SETQednTDEEQIN 2599
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1159-1443 1.08e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1159 ILDQITE--NAKKELQQALDLLNDEgaqaLARAKEKSVEFGQQSEQISDISREARALADKLESEAQfDLKNAKDakdave 1236
Cdd:COG1340    13 LEEKIEElrEEIEELKEKRDELNEE----LKELAEKRDELNAQVKELREEAQELREKRDELNEKVK-ELKEERD------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1237 kahQLAKSAIDLQLKIgTELRSEVGlELSHVKQSLGTVV----------QTSKEALRKANEVYDTALTL---LNDVNRQT 1303
Cdd:COG1340    82 ---ELNEKLNELREEL-DELRKELA-ELNKAGGSIDKLRkeierlewrqQTEVLSPEEEKELVEKIKELekeLEKAKKAL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1304 QPEIDISQLKKDAVAANERADELLKQITELSNSNGELfadfetEQELTEaLLKRAEqqqlediELLERAKAAHDKATKAV 1383
Cdd:COG1340   157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL------HEEMIE-LYKEAD-------ELRKEADELHKEIVEAQ 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1384 EQGDNTLKEANNTYEKLAGFQsdvqrssESAEKALQTVPNIEKEiQNAESLISQAEEALD 1443
Cdd:COG1340   223 EKADELHEEIIELQKELRELR-------KELKKLRKKQRALKRE-KEKEELEEKAEEIFE 274
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1517-1620 1.11e-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: 45.69  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1517 DNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELENLKDintgDLDRLENRLATVEGEINRVN-LTGRIEKYREQ 1595
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEeQLGNVRNNKEY 91

                          90       100
                  ....*....|....*....|....*
gi 665410160 1596 RTIQKNlIDKYDAELRELKDEVQNI 1620
Cdd:COG1579    92 EALQKE-IESLKRRISDLEDEILEL 115
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1301-1492 1.15e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1301 RQTQPEIDISQLKKDAVAANERADELLKQitelsnsngELFADFETEQELTEALLKRAEQQQLEDiellERAKAAHDKAT 1380
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKE---------RLAAQEQKKQAEEAAKQAALKQKQAEE----AAAKAAAAAKA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1381 KAVEQGDNTLKEAnntyeKLAGFQSDVQRSSESAEKALQTVpnieKEIQNAESLISQAEEA-----LDGANKNANEAKKN 1455
Cdd:PRK09510  148 KAEAEAKRAAAAA-----KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAEAAAKAAAEAkkkaeAEAKKKAAAEAKKK 218

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 665410160 1456 AQEAQLKYAEQASKDAELIRRKANETKVAARNLREEA 1492
Cdd:PRK09510  219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1056-1456 1.29e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 47.14  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1056 LVQDAADLHRAKLFNLSQTLDEIARTPVTNDDEF----------EAKLKAVQEKVAVLAQDARDN----SGDGGQTYAEV 1121
Cdd:NF012221 1450 LYQDLSNLTAGEVIALSFDFARRAGLSTNNGIEVlwngevvfasSGDASAWQQKTLKLTAKAGSNrlefKGTGHNDGLGY 1529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1122 IDD-------LHKHLDSVREHlVSADKFQADANGEIDRARQNYTILDQitenakkELQQALDLLNdeGAQALARAKEKSV 1194
Cdd:NF012221 1530 ILDnvvatseSSQQADAVSKH-AKQDDAAQNALADKERAEADRQRLEQ-------EKQQQLAAIS--GSQSQLESTDQNA 1599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1195 EFGQQSEQISDISREARALADKLESEAQ-FDLKNAkDAKDAVEKAHQLAKsaidlqlkigtelRSEVGLeLSHVKQSLGT 1273
Cdd:NF012221 1600 LETNGQAQRDAILEESRAVTKELTTLAQgLDALDS-QATYAGESGDQWRN-------------PFAGGL-LDRVQEQLDD 1664

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1274 VVQTSKEALRKANEVYdtaltllndVNRQTQpeidisqlKKDAVAANE----RADELLKQITELSNSngelfADFETEQE 1349
Cdd:NF012221 1665 AKKISGKQLADAKQRH---------VDNQQK--------VKDAVAKSEagvaQGEQNQANAEQDIDD-----AKADAEKR 1722

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1350 LTEALLKRAEQQQledielleRAKAAHDKATKAVEQGDNTLKEANNTYEK-------------------------LAGFQ 1404
Cdd:NF012221 1723 KDDALAKQNEAQQ--------AESDANAAANDAQSRGEQDASAAENKANQaqadakgakqdesdkpnrqgaagsgLSGKA 1794

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1405 SDVQRSSESAEkALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNA 1456
Cdd:NF012221 1795 YSVEGVAEPGS-HINPDSPAAADGRFSEGLTEQEQEALEGATNAVNRLQINA 1845
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1309-1558 1.47e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1309 ISQLKKDA-VAANERADELLKQITElsnSNGELfADFETEQELTEALLKRAEQQ---QLEDIELLERAKAAHDKATKAVE 1384
Cdd:COG2268   194 IAEIIRDArIAEAEAERETEIAIAQ---ANREA-EEAELEQEREIETARIAEAEaelAKKKAEERREAETARAEAEAAYE 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1385 qgdntLKEANNtyeklagfQSDVQRSSESAEKalqtvpniEKEIQnaeslISQAEEALDGANKNANEAKKNAQEAQlKYA 1464
Cdd:COG2268   270 -----IAEANA--------EREVQRQLEIAER--------EREIE-----LQEKEAEREEAELEADVRKPAEAEKQ-AAE 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1465 EQASKDAELIRRKAnETKVAARNLREEADQLNHRVKLTEMDIFKLEE---------SSTKDDNLVDDAKRKVGQAKADTq 1535
Cdd:COG2268   323 AEAEAEAEAIRAKG-LAEAEGKRALAEAWNKLGDAAILLMLIEKLPEiaeaaakplEKIDKITIIDGGNGGNGAGSAVA- 400

                         250       260
                  ....*....|....*....|....*
gi 665410160 1536 EAQKQIEKANADLTAI--KDELENL 1558
Cdd:COG2268   401 EALAPLLESLLEETGLdlPGLLKGL 425
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1091-1392 1.62e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.59  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1091 AKLKAVQE-KVAVLAQDARDNSGDGGQTYAEVIDDLHKHLDSVREHLVSADKFQADANGEIDRARQNYTIL---DQITEN 1166
Cdd:PRK10929   42 AQAEIVEAlQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILqvsSQLLEK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1167 AKkELQQALDllndegaqalaRAKEKSVEF----GQQSE---QISDISREARALADKLESEAQfdlknakdAKDAVEKAH 1239
Cdd:PRK10929  122 SR-QAQQEQD-----------RAREISDSLsqlpQQQTEarrQLNEIERRLQTLGTPNTPLAQ--------AQLTALQAE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1240 QLAKSAIDLQLKIgTELRSEVGLELSHVKQslgtvvqtskEALRKANEVYDTALTLL-NDVNRQTQpeidisqlkKDAVA 1318
Cdd:PRK10929  182 SAALKALVDELEL-AQLSANNRQELARLRS----------ELAKKRSQQLDAYLQALrNQLNSQRQ---------REAER 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160 1319 ANERADELLKQITELSNSngeLFADFETEQELTEALLKRAeqQQLEDIELLERAKAAHdkaTKAVEQGDNTLKE 1392
Cdd:PRK10929  242 ALESTELLAEQSGDLPKS---IVAQFKINRELSQALNQQA--QRMDLIASQQRQAASQ---TLQVRQALNTLRE 307
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1424-1527 1.63e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 43.62  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAESLISQAEEALDGANKNANEAKKNAQ--------EAQLKYAE---QASKDAELIRRKA-----NETKVAARN 1487
Cdd:COG0711    36 IADGLAEAERAKEEAEAALAEYEEKLAEARAEAAeiiaearkEAEAIAEEakaEAEAEAERIIAQAeaeieQERAKALAE 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 665410160 1488 LREEADQLNhrVKLTEmDIFKLEESSTKDDNLVDDAKRKV 1527
Cdd:COG0711   116 LRAEVADLA--VAIAE-KILGKELDAAAQAALVDRFIAEL 152
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1119-1334 1.63e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1119 AEVIDDLHKHLDSVREHLVSADK----FQADaNGEIDRARQNYTILDQITEnakkeLQQALDLLNDEGAQALARAKEKSV 1194
Cdd:COG3206   174 RKALEFLEEQLPELRKELEEAEAaleeFRQK-NGLVDLSEEAKLLLQQLSE-----LESQLAEARAELAEAEARLAALRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1195 EFGQQSEQISDISrEARALADKLESEAQFDLKNAKDAKDAVEKAHQLaksaIDLQLKIgTELRSEVGLELSHVKQSLGTV 1274
Cdd:COG3206   248 QLGSGPDALPELL-QSPVIQQLRAQLAELEAELAELSARYTPNHPDV----IALRAQI-AALRAQLQQEAQRILASLEAE 321

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1275 VQTSKEALRKANEVYDTALTLLNDVNRQtqpEIDISQLKKDAVAANERADELLKQITELS 1334
Cdd:COG3206   322 LEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVARELYESLLQRLEEAR 378
Alanine_zipper pfam11839
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ...
 1413-1478 1.72e-04

Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.


Pssm-ID: 432118 [Multi-domain]  Cd Length: 69  Bit Score: 41.21  E-value: 1.72e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665410160  1413 SAEKALQ-TVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQlKYAEQASKDAELIRRKA 1478
Cdd:pfam11839    1 AQVEELQsKADQAEQDAAAAQSAADSAKAKADEAAARANAAEAAAEEAQ-QAAEEANEKADRMFEKS 66
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1129-1475 1.86e-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: 46.48  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1129 LDSVREHLVSADKFQADANGEIDRARQNYtilDQITE--NAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQIsdI 1206
Cdd:COG3096   838 LAALRQRRSELERELAQHRAQEQQLRQQL---DQLKEqlQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAF--I 912

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1207 SREARALAdKLESEAQFdLKNAKDAKDAVEKAHQLAKSaidlqlkigtelrsevglELSHVKQ---SLGTVVQtskealR 1283
Cdd:COG3096   913 QQHGKALA-QLEPLVAV-LQSDPEQFEQLQADYLQAKE------------------QQRRLKQqifALSEVVQ------R 966

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1284 KANEVYDTALTLLN---DVNRQTQpeidiSQLKkDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQ 1360
Cdd:COG3096   967 RPHFSYEDAVGLLGensDLNEKLR-----ARLE-QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQ 1040

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1361 QqLEDIELleraKAAHDKATKAVEQGDNTlkeanntYEKLAgfQSDVQRSSesAEKALQTvpnIEKEIQNAESLISQAEE 1440
Cdd:COG3096  1041 E-LEELGV----QADAEAEERARIRRDEL-------HEELS--QNRSRRSQ--LEKQLTR---CEAEMDSLQKRLRKAER 1101

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 665410160 1441 ALDGANKNANEAKK-----------NAQEAQLKYAEQASKDAELIR 1475
Cdd:COG3096  1102 DYKQEREQVVQAKAgwcavlrlardNDVERRLHRRELAYLSADELR 1147
Alanine_zipper pfam11839
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ...
 1426-1481 1.86e-04

Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.


Pssm-ID: 432118 [Multi-domain]  Cd Length: 69  Bit Score: 41.21  E-value: 1.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160  1426 KEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKDAELIRRKANET 1481
Cdd:pfam11839    1 AQVEELQSKADQAEQDAAAAQSAADSAKAKADEAAAR-ANAAEAAAEEAQQAAEEA 55
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1409-1618 1.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1409 RSSESAEKALQTVPNIEK-----------------EIQNAESLISQAE--EALDGANKNANEAKKN----------AQEA 1459
Cdd:PRK03918  142 ESDESREKVVRQILGLDDyenayknlgevikeikrRIERLEKFIKRTEniEELIKEKEKELEEVLReineisselpELRE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1460 QLKYAEQASKDAELIRRKANETKV-------AARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAK--RKVGQA 1530
Cdd:PRK03918  222 ELEKLEKEVKELEELKEEIEELEKeleslegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIKLSEF 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1531 KADTQEAQKQIEKANADLT----AIKDELENLKDINTgDLDRLENRLATVEGEINRvnLTGRIEKYREQRTIQKNL---- 1602
Cdd:PRK03918  302 YEEYLDELREIEKRLSRLEeeinGIEERIKELEEKEE-RLEELKKKLKELEKRLEE--LEERHELYEEAKAKKEELerlk 378

                         250       260
                  ....*....|....*....|....*.
gi 665410160 1603 -------IDKYDAELREL---KDEVQ 1618
Cdd:PRK03918  379 krltgltPEKLEKELEELekaKEEIE 404
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 1308-1469 2.16e-04

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


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 44.27  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1308 DISQLKKDAVAAnerADELLKQITELSNSNGEL------FADFETE--QELTEALLKRAeqQQLEDIELLERAKAAHDKA 1379
Cdd:cd07596    15 KLEEQLKKLSKQ---AQRLVKRRRELGSALGEFgkalikLAKCEEEvgGELGEALSKLG--KAAEELSSLSEAQANQELV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1380 TKAVEQGD---------NTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNAN 1450
Cdd:cd07596    90 KLLEPLKEylrycqavkETLDDRADALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYE 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 665410160 1451 EAKKNAQ----------------------EAQLKYAEQASK 1469
Cdd:cd07596   170 EISERLKeelkrfheerardlkaalkefaRLQVQYAEKIAE 210
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1303-1584 2.49e-04

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.19  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1303 TQPEIDISqlKKDAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQ-QQLEDIEllERAKAAHDKATK 1381
Cdd:pfam15905   37 SQPNLNNS--KDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQdKRLQALE--EELEKVEAKLNA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1382 AVEQgDNTLKEANNTYEKLagfQSDVQRSSESAEKALQTVPNiEKEIQNAESLISQAEEALDGANKNA-----------N 1450
Cdd:pfam15905  113 AVRE-KTSLSASVASLEKQ---LLELTRVNELLKAKFSEDGT-QKKMSSLSMELMKLRNKLEAKMKEVmakqegmegklQ 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1451 EAKKNAQEAQLKYAEQASKDAELIRRKaNETKVAARNLREEADQLN---HRVKLTEMDIFKLEES-STKDDNLVDdAKRK 1526
Cdd:pfam15905  188 VTQKNLEHSKGKVAQLEEKLVSTEKEK-IEEKSETEKLLEYITELScvsEQVEKYKLDIAQLEELlKEKNDEIES-LKQS 265

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410160  1527 VgqaKADTQEAQKQIEKANADLTAIKDELENL------KDIN-TGDLDRLENRLATVEGEINRVN 1584
Cdd:pfam15905  266 L---EEKEQELSKQIKDLNEKCKLLESEKEELlreyeeKEQTlNAELEELKEKLTLEEQEHQKLQ 327
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 1424-1541 2.67e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 42.53  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAESLISQAEEALDGANK---NANEAKKNAQEAQLKYAEQASKDAELIRRKAnetkvaarnlREEADQlnhrvk 1500
Cdd:COG3599    39 LIRENKELKEKLEELEEELEEYREleeTLQKTLVVAQETAEEVKENAEKEAELIIKEA----------ELEAEK------ 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 665410160 1501 ltemdifkleesstkddnLVDDAKRKVGQAKADTQEAQKQI 1541
Cdd:COG3599   103 ------------------IIEEAQEKARKIVREIEELKRQR 125
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
299-342 2.70e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.99  E-value: 2.70e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 665410160    299 CKCN--GHASK-CVPSTGmhgertlVCECRHNTDGPDCDRCLPLYND 342
Cdd:smart00180    1 CDCDpgGSASGtCDPDTG-------QCECKPNVTGRRCDRCAPGYYG 40
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1070-1614 2.89e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 45.98  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1070 NLSQTLDEIARTPVTNDDEFEAKLKAVQEKVAVLAQDARDnsGDGGQTYAEVIDDLHKHLDSVREHLVSAD--KFQADAN 1147
Cdd:PTZ00440  595 NIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYK--GDLQELLDELSHFLDDHKYLYHEAKSKEDlqTLLNTSK 672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1148 GEIDRARQ-NYTILDQITENAKKELQQALDLlndegaqalaraKEKSVEfgqqsEQISDISREARALADKLESEAQfDLK 1226
Cdd:PTZ00440  673 NEYEKLEFmKSDNIDNIIKNLKKELQNLLSL------------KENIIK-----KQLNNIEQDISNSLNQYTIKYN-DLK 734

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1227 NAKDAKDAVEKAHQLAKSAIDLQLK--IGTELRSEVglELSHVKQSLGTVVQTSKEALRKANEVYDTALTLlNDVNRQTQ 1304
Cdd:PTZ00440  735 SSIEEYKEEEEKLEVYKHQIINRKNefILHLYENDK--DLPDGKNTYEEFLQYKDTILNKENKISNDINIL-KENKKNNQ 811

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1305 PEIDISQLKKDAVAAN-ERADELLKQITELSNSNGELFADFETEQELTEAllKRAEQQQLEDIELLerakaahDKATKAV 1383
Cdd:PTZ00440  812 DLLNSYNILIQKLEAHtEKNDEELKQLLQKFPTEDENLNLKELEKEFNEN--NQIVDNIIKDIENM-------NKNINII 882

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1384 EQGDNTLKEANNT---YEKLAGFQSDVQRSSESAEKALQTVPNIEKEiqNAESLISQAEEALDGANKNANEAKKNaqeaQ 1460
Cdd:PTZ00440  883 KTLNIAINRSNSNkqlVEHLLNNKIDLKNKLEQHMKIINTDNIIQKN--EKLNLLNNLNKEKEKIEKQLSDTKIN----N 956

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1461 LKYaeqaskdaelirrKANETKVAARNLREEADQlNHRVKLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADT---QEA 1537
Cdd:PTZ00440  957 LKM-------------QIEKTLEYYDKSKENING-NDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDlikKQH 1022

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1538 QKQIEKANADLTAIKDELENLKDINTGDLDRLENRLATVEGEINRVN-----LTGRIEKYREQRTIQKNLIDKYDAELRE 1612
Cdd:PTZ00440 1023 DDIIELIDKLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKyknpkIKEEIKLLEEKVEALLKKIDENKNKLIE 1102


                  ..
gi 665410160 1613 LK 1614
Cdd:PTZ00440 1103 IK 1104
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1423-1495 3.14e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 42.30  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1423 NIEKEIQNAE-------SLISQAEEALDGANKNANE----AKKNAQEAQLKYAEQASKDAELIRRKANETKVAARN---- 1487
Cdd:pfam00430   34 LIADEIAEAEerrkdaaAALAEAEQQLKEARAEAQEiienAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDrala 113


                   ....*....
gi 665410160  1488 -LREEADQL 1495
Cdd:pfam00430  114 eLRQQVVAL 122
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 1071-1599 3.39e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 45.59  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1071 LSQTLDEIARTPVTNDDEFEAKLKAVQEKVAVLAQDARDNSGDGGQTYAEVIDDLHKHL-----DSVREHLVSADKFQAD 1145
Cdd:PTZ00440  913 LEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQLSDTKINNLKMQIEKTLEYYDKSkeninGNDGTHLEKLDKEKDE 992

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1146 ---ANGEIDRARQNYTILDQITENA-KKELQQALDLLNDegaqalaRAKEKSVEFGQQSEQ-ISDISRearaLADKLES- 1219
Cdd:PTZ00440  993 wehFKSEIDKLNVNYNILNKKIDDLiKKQHDDIIELIDK-------LIKEKGKEIEEKVDQyISLLEK----MKTKLSSf 1061

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1220 EAQFDLKNAKDAKDAvEKAHQLAKSAIDLQLKIgtelrSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDV 1299
Cdd:PTZ00440 1062 HFNIDIKKYKNPKIK-EEIKLLEEKVEALLKKI-----DENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKI 1135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1300 NRQtqpeidISQLKKDAVAANERaDELLKQITELSNSNGELFADFETEQELTEAllKRAEqQQLEDIELLErakaahdka 1379
Cdd:PTZ00440 1136 YKQ------MEKTLKELENMNLE-DITLNEVNEIEIEYERILIDHIVEQINNEA--KKSK-TIMEEIESYK--------- 1196

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1380 tKAVEQGDNTLKEANNtyEKLAGFQSDVQRssesaEKALQTVPNIEKEIQNAESLISQAEealdgANKNANEAKKNAQEA 1459
Cdd:PTZ00440 1197 -KDIDQVKKNMSKERN--DHLTTFEYNAYY-----DKATASYENIEELTTEAKGLKGEAN-----RSTNVDELKEIKLQV 1263

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1460 qLKYAEQASKDAELIRRKANETKvaarNLREEADQLNHRVKLTEmdifkLEESSTKDDNLVDDAKRKVGQAKADTQEAQK 1539
Cdd:PTZ00440 1264 -FSYLQQVIKENNKMENALHEIK----NMYEFLISIDSEKILKE-----ILNSTKKAEEFSNDAKKELEKTDNLIKQVEA 1333

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410160 1540 QIEKANADLTAIKDELENLK-DINTGDLDRLENRLATVEGEINrvNLTGRIEKYREQRTIQ 1599
Cdd:PTZ00440 1334 KIEQAKEHKNKIYGSLEDKQiDDEIKKIEQIKEEISNKRKEIN--KYLSNIKSNKEKCDLH 1392
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1421-1556 4.38e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1421 VPNIEKEIQNAEslISQAEEALDG------ANKNANEAKKnAQEAQLKYAEQASKDAELIRRKANETKVAARNlREEADQ 1494
Cdd:COG2268   191 RRKIAEIIRDAR--IAEAEAERETeiaiaqANREAEEAEL-EQEREIETARIAEAEAELAKKKAEERREAETA-RAEAEA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1495 ------------LNHRVKLTEMD-IFKLEESStkddnlvddAKRKVGQAKADTQ-----EAQKQIEKANADLTAIKDELE 1556
Cdd:COG2268   267 ayeiaeanaereVQRQLEIAERErEIELQEKE---------AEREEAELEADVRkpaeaEKQAAEAEAEAEAEAIRAKGL 337
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1306-1485 5.26e-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: 43.37  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1306 EID--ISQLKKDAVAANERADELLKQITELSNSngelFADFETEQELTEALLKRAEQQqledielLERAKAAHDKATKAV 1383
Cdd:COG1579    14 ELDseLDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELE-------IEEVEARIKKYEEQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1384 EQGDNTlKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGAnKNANEAKKNAQEAQLKY 1463
Cdd:COG1579    83 GNVRNN-KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-KAELDEELAELEAELEE 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 665410160 1464 AEQASK------DAEL------IRRKANETKVAA 1485
Cdd:COG1579   161 LEAEREelaakiPPELlalyerIRKRKNGLAVVP 194
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1087-1245 5.95e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1087 DEFEAKLKAVQEKVA----VLAQDARDNSGDGGQ-TYAEViddlhkhldsvrehLVSADKFqADAngeIDRA-------R 1154
Cdd:COG3883    68 DKLQAEIAEAEAEIEerreELGERARALYRSGGSvSYLDV--------------LLGSESF-SDF---LDRLsalskiaD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1155 QNYTILDQIT------ENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLES-EAQFDLKN 1227
Cdd:COG3883   130 ADADLLEELKadkaelEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAElEAELAAAE 209

                         170
                  ....*....|....*...
gi 665410160 1228 AKDAKDAVEKAHQLAKSA 1245
Cdd:COG3883   210 AAAAAAAAAAAAAAAAAA 227
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1360-1481 6.75e-04

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 42.74  E-value: 6.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1360 QQQLEDIE-LLER----AKAAHDKATKAVEQgdnTLKEANNTYEKLAGFQSDVQRSSESAEKAL-QTVPNIEKE----IQ 1429
Cdd:pfam04012   17 LDKAEDPEkMLEQairdMQSELVKARQALAQ---TIARQKQLERRLEQQTEQAKKLEEKAQAALtKGNEELAREalaeKK 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160  1430 NAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASKDAELIRR----KANET 1481
Cdd:pfam04012   94 SLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARlkaaKAQEA 149
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 1470-1620 6.87e-04

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: 43.92  E-value: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1470 DAELIRRKANETKVAARNLREEADQLNHRVKLtemdIFKleesSTKD-----DNLVDDAKRKVGQAKADTQEAQKQIEKA 1544
Cdd:pfam04108    4 SAQDLCRWANELLTDARSLLEELVVLLAKIAF----LRR----GLSVqlanlEKVREGLEKVLNELKKDFKQLLKDLDAA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1545 NADLTAIKDELENLKDINTGDLDRLENR-----LATVEGEINRVNLTGRIEKYREQRTIQKNLIDKYDAELRELKDEVQN 1619
Cdd:pfam04108   76 LERLEETLDKLRNTPVEPALPPGEEKQKtlldfIDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELES 155


                   .
gi 665410160  1620 I 1620
Cdd:pfam04108  156 L 156
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1279-1596 8.26e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1279 KEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDAVAANERADELLKQITELSNSNGELFADFETE----------- 1347
Cdd:pfam13868   31 KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEreqmdeiveri 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1348 --QELTEALLKRAEQQQL-EDIELLERAKAAHdKATKAVEQgdntlKEANntyEKLAGFQSDVQRSSESAEKALQTVpNI 1424
Cdd:pfam13868  111 qeEDQAEAEEKLEKQRQLrEEIDEFNEEQAEW-KELEKEEE-----REED---ERILEYLKEKAEREEEREAEREEI-EE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1425 EKEIQNAEsLISQAEEALD-GANKNANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAarnlREEadQLNHRVKLTE 1503
Cdd:pfam13868  181 EKEREIAR-LRAQQEKAQDeKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA----REE--QIELKERRLA 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1504 MDIFKLEEsstkddnLVDDAKRKvgQAKADTQEAQKQiEKANADLTAIKDELENLkdINtgdlDRLENRLATVEGEINRV 1583
Cdd:pfam13868  254 EEAEREEE-------EFERMLRK--QAEDEEIEQEEA-EKRRMKRLEHRRELEKQ--IE----EREEQRAAEREEELEEG 317

                          330
                   ....*....|...
gi 665410160  1584 NLTGRIEKYREQR 1596
Cdd:pfam13868  318 ERLREEEAERRER 330
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1087-1287 8.26e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1087 DEFEAKLKAVQEKVAVLAQDARDNSGDggqtyaevIDDLHKHLDSVREHLVSADKFQADANGEI-DRARQNY------TI 1159
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAE--------LEALQAEIDKLQAEIAEAEAEIEERREELgERARALYrsggsvSY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1160 LDQITENakKELQQALDllndeGAQALARAKEksvefgQQSEQISDIsREARALADKLESEAQFDLKNAKDAKDAVEKAH 1239
Cdd:COG3883   105 LDVLLGS--ESFSDFLD-----RLSALSKIAD------ADADLLEEL-KADKAELEAKKAELEAKLAELEALKAELEAAK 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 665410160 1240 QLAKSAIDLQLKIGTELRSEVGLELSHvKQSLGTVVQTSKEALRKANE 1287
Cdd:COG3883   171 AELEAQQAEQEALLAQLSAEEAAAEAQ-LAELEAELAAAEAAAAAAAA 217
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 1300-1616 8.33e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1300 NRQTQPEIDISQLKKDAVAANERADELLKqITELsNSNGELFADFET-EQELTEALLKraeqqQLEDIE-LLERAKAAHD 1377
Cdd:PRK04778   24 RKRNYKRIDELEERKQELENLPVNDELEK-VKKL-NLTGQSEEKFEEwRQKWDEIVTN-----SLPDIEeQLFEAEELND 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1378 -----KATKAVEQGDNTLKEANNTYEK-LAGFQ----SDVQRSSESAE---------KAL--------QTVPNIEKEIQN 1430
Cdd:PRK04778   97 kfrfrKAKHEINEIESLLDLIEEDIEQiLEELQelleSEEKNREEVEQlkdlyrelrKSLlanrfsfgPALDELEKQLEN 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1431 AESLISQAEEaldgANKNAN--EAKK--NAQEAQLKYAEQASKD-AELIRRKANETKVAARNLREEADQL-NHRVKLTEM 1504
Cdd:PRK04778  177 LEEEFSQFVE----LTESGDyvEAREilDQLEEELAALEQIMEEiPELLKELQTELPDQLQELKAGYRELvEEGYHLDHL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1505 DIfkLEEsstkddnlVDDAKRKVGQAKADTQEAqkQIEKANADLTAIKDELENL-----------------KDINTGDLD 1567
Cdd:PRK04778  253 DI--EKE--------IQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilerevkarkyveknSDTLPDFLE 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665410160 1568 RLENRLATVEGEINRVNLT-----GRIEKYRE-QRTIqKNLIDKYDAELRELKDE 1616
Cdd:PRK04778  321 HAKEQNKELKEEIDRVKQSytlneSELESVRQlEKQL-ESLEKQYDEITERIAEQ 374
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1309-1559 9.85e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1309 ISQLKKDAVAANERADELLKQItelsnsngelfadfeteQELTEALLKRAEQQQLEDiellERAKAAHdkatkaVEQgdn 1388
Cdd:COG0497   174 LEELRADEAERARELDLLRFQL-----------------EELEAAALQPGEEEELEE----ERRRLSN------AEK--- 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1389 tLKEA-NNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDganknanEAkknAQEAQlKYAEQA 1467
Cdd:COG0497   224 -LREAlQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELE-------EA---ASELR-RYLDSL 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1468 SKDAE----------LIRRkanetkvAARNLREEADQL-NHRVKLTEmdifKLEESSTKDDNLvDDAKRKVGQAKADTQE 1536
Cdd:COG0497   292 EFDPErleeveerlaLLRR-------LARKYGVTVEELlAYAEELRA----ELAELENSDERL-EELEAELAEAEAELLE 359

                         250       260
                  ....*....|....*....|....*...
gi 665410160 1537 AQKQI----EKANADL-TAIKDELENLK 1559
Cdd:COG0497   360 AAEKLsaarKKAAKKLeKAVTAELADLG 387
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1165-1270 1.00e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 41.30  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1165 ENAKKELQQALdllnDEGAQALARAKEKSVEFGQQ-----SEQISDISREARALADKLESEAQFDLKNAKD-AKDAVEKa 1238
Cdd:PRK05759   48 ERAKKELELAQ----AKYEAQLAEARAEAAEIIEQakkraAQIIEEAKAEAEAEAARIKAQAQAEIEQERKrAREELRK- 122

                          90       100       110
                  ....*....|....*....|....*....|..
gi 665410160 1239 hQLAKSAIDLQLKIgtelrseVGLELSHVKQS 1270
Cdd:PRK05759  123 -QVADLAVAGAEKI-------LGRELDAAAQS 146
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 1122-1443 1.07e-03

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 43.10  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1122 IDDLHK--HLDSVREHLVSADKFqadanGEIDRARQNYTILDQITENAKKELQQALDLLNDEGAQ-ALARAKeksveFGQ 1198
Cdd:cd08915    47 IDDLQKpeNLPDSIQHSQEIIEE-----GGLDNIEQSFKELSKLRQNVEELLQECEELLEEEAAEdDQLRAK-----FGT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1199 QSEQISDISREARALADKLESEAQFdLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTS 1278
Cdd:cd08915   117 LRWRRPSSDEAAKELYEKVTKLRGY-LEQASNSDNEVLQCYESIDPNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSL 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1279 KEALRKANEVYDtaltllndvnrqtQPEIDISQLKKDAvaaneRADELLKQITELSNSNGEL-FAD-FETEQELTEALLK 1356
Cdd:cd08915   196 RPLLNEVSELEK-------------ERERFISELEIKS-----RNNDILPKLITEYKKNGTTeFEDlFEEHLKKFDKDLT 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1357 RAEQQQLEDIELLERAKAAHDKaTKAVEQGDNTLKEANNTYEKLAgfqsdvqrssESAEKALQTVPNIEKEIQNAESLIS 1436
Cdd:cd08915   258 YVEKTKKKQIELIKEIDAANQE-FSQVKNSNDSLDPREEALQDLE----------ASYKKYLELKENLNEGSKFYNDLIE 326


                  ....*..
gi 665410160 1437 QAEEALD 1443
Cdd:cd08915   327 KVNRLLE 333
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 1165-1252 1.31e-03

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 40.85  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1165 ENAKKELQQAL----DLLN---DEGAQALARAKEKsvefgqQSEQISDISREARALADKLESEAQFDL-KNAKDAKDAVE 1236
Cdd:TIGR01144   39 ERAKKEAALAQkkaqVILKeakDEAQEIIENANKR------GSEILEEAKAEAREEREKIKAQARAEIeAEKEQAREELR 112

                           90
                   ....*....|....*.
gi 665410160  1237 KahQLAKSAIDLQLKI 1252
Cdd:TIGR01144  113 K--QVADLSVLGAEKI 126
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 1448-1610 1.39e-03

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 40.85  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1448 NANEAKKNAQEAQLKYAEQASKDAELIRRKANETKVAARnlrEEADQLnhrvkltemdifkLEESSTKDDNLVDDAKrkv 1527
Cdd:TIGR01144   22 KAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAK---DEAQEI-------------IENANKRGSEILEEAK--- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1528 gqAKADtQEAQKQIEKANADLTAIKDE-LENL-KDINTgdldrlenrLAtvegeinrVNLTGRIEKYREQRTIQKNLIDK 1605
Cdd:TIGR01144   83 --AEAR-EEREKIKAQARAEIEAEKEQaREELrKQVAD---------LS--------VLGAEKIIERNIDKQAQKDLIDK 142


                   ....*
gi 665410160  1606 YDAEL 1610
Cdd:TIGR01144  143 LVAEL 147
MCP2201-like_sensor cd19411
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
 1274-1417 1.40e-03

ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.


Pssm-ID: 438629 [Multi-domain]  Cd Length: 138  Bit Score: 40.70  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1274 VVQTSKEALRKANEVYDtaltLLNDVNRQTQ-------PEiDISQLKKDAVAANERADELLKQITELSNSngelfadfet 1346
Cdd:cd19411     1 IVEDRYPKVRLANEWKD----NVNANARRTRnlllstdPA-ERAKELARIAAARARITELLKKLEKLITS---------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1347 EQELteALLKRAEQQqledielleRAK--AAHDKATKAVEQGD---------NTLKEANNTY----EKLAGFQSdvQRSS 1411
Cdd:cd19411    66 PEGK--ALLAAIAEA---------RAAylAARDKVLELKKAGDreearalllGELRPAQAAYlaalDALVDYQE--ELMD 132


                  ....*.
gi 665410160 1412 ESAEKA 1417
Cdd:cd19411   133 AAAAEA 138
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1070-1271 1.42e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 41.48  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1070 NLSQTLDEIartpvtnddefEAKLKAVQEKVAVLAQDARDNSGDGGQtyaEVIDDLHKHLDSVREHLV-SADKFQADANG 1148
Cdd:pfam01442    1 LLEDSLDEL-----------STYAEELQEQLGPVAQELVDRLEKETE---ALRERLQKDLEEVRAKLEpYLEELQAKLGQ 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1149 EIDRARQnytILDQITENAKKELQQALDLLNDEGAQALARAKEKSVE-FGQQSEQISDISREARA-LADKLEseaqfDLK 1226
Cdd:pfam01442   67 NVEELRQ---RLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQnVDALRARLAPYAEELRQkLAERLE-----ELK 138

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 665410160  1227 NAkdAKDAVEKAHQLAKSAIDlqlkigtELRSEVGLELSHVKQSL 1271
Cdd:pfam01442  139 ES--LAPYAEEVQAQLSQRLQ-------ELREKLEPQAEDLREKL 174
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 1423-1554 1.65e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 41.09  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1423 NIEKEIQNAESLISQAEEALDganknaneakknaqEAQLKYAeQASKDAELIRRKANETKVAARnlREEADQlnhrvklT 1502
Cdd:PRK07352   54 AILQALKEAEERLRQAAQALA--------------EAQQKLA-QAQQEAERIRADAKARAEAIR--AEIEKQ-------A 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1503 EMDIFKLEESSTKDdnLVDDAKRKVGQAKAdtQEAQKQIEKANADLTAIKDE 1554
Cdd:PRK07352  110 IEDMARLKQTAAAD--LSAEQERVIAQLRR--EAAELAIAKAESQLPGRLDE 157
PRK12704 PRK12704
phosphodiesterase; Provisional
 1309-1481 1.68e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1309 ISQLKKDAV----AANERADELLKQ-ITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAV 1383
Cdd:PRK12704   33 IKEAEEEAKrileEAKKEAEAIKKEaLLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1384 EQGDNTLKEANNTYEKLagfQSDVQRSSESAEKALQTVPNIEKEiQNAESLISQAEEaldganknanEAKKNAQEAQLKY 1463
Cdd:PRK12704  113 EKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAE-EAKEILLEKVEE----------EARHEAAVLIKEI 178

                         170
                  ....*....|....*...
gi 665410160 1464 AEQASKDAElirRKANET 1481
Cdd:PRK12704  179 EEEAKEEAD---KKAKEI 193
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1416-1617 1.86e-03

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


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 42.01  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1416 KALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQlKYAEQASKDAELIRRKANET-------KVAARNL 1488
Cdd:pfam06008   16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQ-KKATQTLAKAQQVNAESERTlghakelAEAIKNL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1489 REEADQLNHRVKLTEMDIFKLeeSSTKDDNLVDDAKRKVGQ------------AKADTQEAQKQIEKANADLTAIKDELE 1556
Cdd:pfam06008   95 IDNIKEINEKVATLGENDFAL--PSSDLSRMLAEAQRMLGEirsrdfgtqlqnAEAELKAAQDLLSRIQTWFQSPQEENK 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160  1557 NLKDINTGDLDRLENRLATVEG----------EINRVNLT-----GRIEKYREQRTIQKNLIDKYDAELRELKDEV 1617
Cdd:pfam06008  173 ALANALRDSLAEYEAKLSDLREllreaaaktrDANRLNLAnqanlREFQRKKEEVSEQKNQLEETLKTARDSLDAA 248
PhaF COG3937
Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport ...
 1508-1582 1.93e-03

Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport and catabolism, Signal transduction mechanisms];


Pssm-ID: 443138 [Multi-domain]  Cd Length: 103  Bit Score: 39.40  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1508 KLEESStkdDNLVDDAKRKVGQAKADTQEAQKQIEKANADL-TAIKDELEN-LKDINT---GDLDRLENRLATVEGEINR 1582
Cdd:COG3937    22 KAEELV---DELVEKGELTEEEAKKFVDELVEKGEEEKEELeEKIEEQVEEaLEKLGLatkEEVDELEERIDRLEKQLRE 98
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 1303-1480 1.96e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 41.20  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1303 TQPEID--ISQLKKDAVAANERADELLKQITELSNSNGEL---FADFE--TEQELTEA----LLKRAEQQQLedieLLER 1371
Cdd:pfam05010    2 SQKDMDaaLEKARNEIEEKELEINELKAKYEELRRENLEMrkiVAEFEktIAQMIEEKqkqkELEHAEIQKV----LEEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1372 AKAAHD-----KATKAVEQGDNTLKEAnntyekLAGFQSDVQRSSESAEKALQTvpnIEKEIQNAESLISQAEEALDGAN 1446
Cdd:pfam05010   78 DQALADlnsveKSFSDLFKRYEKQKEV------ISGYKKNEESLKKCAQDYLAR---IKKEEQRYQALKAHAEEKLDQAN 148

                          170       180       190
                   ....*....|....*....|....*....|....
gi 665410160  1447 KNANEAKKNAQEAQLKYaeQASKDAELIRRKANE 1480
Cdd:pfam05010  149 EEIAQVRSKAKAETAAL--QASLRKEQMKVQSLE 180
RNase_Y_N pfam12072
RNase Y N-terminal region;
1424-1561 1.97e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.41  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1424 IEKEIQNAESLisqAEEALDGANKNANEAKKnaqEAQLKYAEQASKdaelIRRKAnETKVAARnlREEADQLNHRvklte 1503
Cdd:pfam12072   25 AEAKIGSAEEL---AKRIIEEAKKEAETKKK---EALLEAKEEIHK----LRAEA-ERELKER--RNELQRQERR----- 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160  1504 mdIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTA-IKDELENLKDI 1561
Cdd:pfam12072   87 --LLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEElIEEQRQELERI 143
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
793-836 2.24e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.24e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 665410160    793 CPCPNDGA----ClqiNEDTVICtECPKGYFGSRCEQCSDGFFGDPTG 836
Cdd:smart00180    1 CDCDPGGSasgtC---DPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPP 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
359-411 2.24e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.24e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160    359 CNCNG---LADKCFFDanlfnrtghGGHCLdCRENRDGPNCERCKENFYMRDDGYC 411
Cdd:smart00180    1 CDCDPggsASGTCDPD---------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPGC 46
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1439-1560 2.35e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1439 EEALDGANKNANEAKKNAQEAQLKYAEQ---ASKDAELIRRKANETkvaARNLREEAdqlnhrvkltemdifkleesstk 1515
Cdd:cd06503    32 EEKIAESLEEAEKAKEEAEELLAEYEEKlaeARAEAQEIIEEARKE---AEKIKEEI----------------------- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 665410160 1516 ddnlVDDAKrkvgqakadtQEAQKQIEKANADLTAIKDE-LENLKD 1560
Cdd:cd06503    86 ----LAEAK----------EEAERILEQAKAEIEQEKEKaLAELRK 117
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1210-1494 2.86e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1210 ARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGtelrsevglelshvkqslgtvvqtskEALRKANEvY 1289
Cdd:COG2956     6 AAALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALG--------------------------NLYRRRGE-Y 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1290 DTALTLL-NDVNRQTQPEIDISQLKKDAVAAN--ERADELLKQITELSNSNGE----LFADFETEQELTEAL--LKRAEQ 1360
Cdd:COG2956    59 DRAIRIHqKLLERDPDRAEALLELAQDYLKAGllDRAEELLEKLLELDPDDAEalrlLAEIYEQEGDWEKAIevLERLLK 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1361 QQLEDIE-LLERAKAAH-----DKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRsSESAEKALQTVPNIEKEIQNAESL 1434
Cdd:COG2956   139 LGPENAHaYCELAELYLeqgdyDEAIEALEKALKLDPDCARALLLLAELYLEQGD-YEEAIAALERALEQDPDYLPALPR 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665410160 1435 ISQAEEALDgankNANEAKKNAQEAQLKYAEQASKD--AELIRRKaNETKVAARNLREEADQ 1494
Cdd:COG2956   218 LAELYEKLG----DPEEALELLRKALELDPSDDLLLalADLLERK-EGLEAALALLERQLRR 274
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1315-1546 2.88e-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: 41.13  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1315 DAVAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQ--QQLEDI-ELLERAKAAHDKATKAV------EQ 1385
Cdd:pfam12795    3 DELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDapAELRELrQELAALQAKAEAAPKEIlaslslEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1386 GDNTLKEANN----TYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQ---AEEALDGANKNANEAKKNAQE 1458
Cdd:pfam12795   83 LEQRLLQTSAqlqeLQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGpapPGEPLSEAQRWALQAELAALK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1459 AQLKY--AEQASKDA--ELIRRKANEtkvaarnLREEADQLNHRVKLtemdifkLEEsstkddnlVDDAKRkvgQAKADT 1534
Cdd:pfam12795  163 AQIDMleQELLSNNNrqDLLKARRDL-------LTLRIQRLEQQLQA-------LQE--------LLNEKR---LQEAEQ 217

                          250
                   ....*....|..
gi 665410160  1535 QEAQKQIEKANA 1546
Cdd:pfam12795  218 AVAQTEQLAEEA 229
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1484-1610 2.98e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 40.14  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1484 AARNLREEADQLNHRVKLTemdifkLEESSTKDDNLVDDAKRK----VGQAKAD-TQEAQKQIEKANADLTAIKDE-LEN 1557
Cdd:PRK05759   46 AAERAKKELELAQAKYEAQ------LAEARAEAAEIIEQAKKRaaqiIEEAKAEaEAEAARIKAQAQAEIEQERKRaREE 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1558 LKDiNTGDLDrlenrlatvegeinrVNLTGRIEKYREQRTIQKNLIDKYDAEL 1610
Cdd:PRK05759  120 LRK-QVADLA---------------VAGAEKILGRELDAAAQSDLIDKLIAEL 156
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1100-1557 3.08e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 42.31  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1100 VAVLAQDARDNSGDGGQTYAEVIDDLHKHLDSVREHLVSADKF-QADANGEIDRARQNYTILDQITENAKKELQQALDLL 1178
Cdd:COG5271     3 NDDRTVILDLDNSLAGRDLEDDDADLAGLDTQSETASEREDKLpDTDKDLLILTDADAASDEGKLLDLKSADGAALSAES 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1179 NDEGAQALARAKEKSVEfgqqsEQISDISREARALADKLESEAQFDLKNAKDAKDAVEKAHQLAKSAIDLQLKIGTELRS 1258
Cdd:COG5271    83 DAGASLITAANLEEGDI-----AGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLGGGDLDLATKDGDELLP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1259 EVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDIsQLKKDAVAANERADELLKQITELSNSNG 1338
Cdd:COG5271   158 SLADNDEAAADEGDELAADGDDTLAVADAIEATPGGTDAVELTATLGATVT-TDPGDSVAADDDLAAEEGASAVVEEEDA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1339 ELFADFETEQELTEALlkraeQQQLEDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKAL 1418
Cdd:COG5271   237 SEDAVAAADETLLADD-----DDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDST 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1419 QTVPNIEKEIQNAESLISQAEEAlDGANKNANEAKKNAQEAQlkyAEQASKDAELIRRKANETKVAARNLREEADQLNHR 1498
Cdd:COG5271   312 LAALEGAAEDTEIATADELAAAD-DEDDDDSAAEDAAEEAAT---AEDSAAEDTQDAEDEAAGEAADESEGADTDAAADE 387

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1499 VKLTEMDIFKLEESSTKDDNLVDDAKRKVgQAKADTQEAQKQIEKANADLTAIKDELEN 1557
Cdd:COG5271   388 ADAAADDSADDEEASADGGTSPTSDTDEE-EEEADEDASAGETEDESTDVTSAEDDIAT 445
OspD pfam03207
Borrelia outer surface protein D (OspD);
1383-1570 3.41e-03

Borrelia outer surface protein D (OspD);


Pssm-ID: 367392 [Multi-domain]  Cd Length: 254  Bit Score: 40.99  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1383 VEQGDNTLKEANNTYEKLagfqsdvqRSSESAEKALQTVPniekeiqNAESLISQAEEALDGANKNANEakknaqeaqlk 1462
Cdd:pfam03207   64 LKQTTNSLKEAKNTTDNL--------NASNEANKVVEAVI-------NAVNLISSAADQVKSATKNMHD----------- 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1463 YAEQASKDAELIRRKANETkVAARNLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDDAKrkvgqaKADTQEAQKQIE 1542
Cdd:pfam03207  118 LAQMAEIDLEKIKNSSDKA-IFASNLAKEAYSLTKAAEQNMQKLYKEQQKISESESESDYSD------SAEIKQAKEAVE 190

                          170       180
                   ....*....|....*....|....*...
gi 665410160  1543 KANADLTAIKDELENLKDINTGDLDRLE 1570
Cdd:pfam03207  191 IAWKATVEAKDKLIDVENTVKETLDKIK 218
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1423-1521 3.46e-03

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 41.12  E-value: 3.46e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160   1423 NIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKDAELIRRKANETKVAARNLREEADQLNHRVKLT 1502
Cdd:smart00283    1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAAN-ADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEA 79

                            90
                    ....*....|....*....
gi 665410160   1503 EMDIFKLEESSTKDDNLVD 1521
Cdd:smart00283   80 VSAVEELEESSDEIGEIVS 98
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1157-1536 3.48e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 41.93  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1157 YTILDQITENAKKELQQALDLLNDEGAQALARAKEKSVEFGQQSEQISDISREARALADKLESEAQFDLKNAKDAKDAVE 1236
Cdd:COG0840     4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1237 KAHQLAKSAIDLQLKIGTELRSEVGLELSHVKQSLGTVVQTSKEALRKANEVYDTALTLLNDVNRQTQPEIDISQLKKDA 1316
Cdd:COG0840    84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1317 VAANERADELLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIEllerakaahdKATKAVEQGDNTLK---EA 1393
Cdd:COG0840   164 AALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELL----------EVLERIAEGDLTVRidvDS 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1394 NNTYEKLAgfqSDVQRSSESAEKALQTVpniekeIQNAESLISQAEEALDGANKNANEAKKNAQEAQ--LKYAEQASKDA 1471
Cdd:COG0840   234 KDEIGQLA---DAFNRMIENLRELVGQV------RESAEQVASASEELAASAEELAAGAEEQAASLEetAAAMEELSATV 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665410160 1472 ELIRRKANETKVAARNLREEADQLNHRVKLTEMDIFKLEESstkddnlVDDAKRKVGQAKADTQE 1536
Cdd:COG0840   305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRES-------VEETAETIEELGESSQE 362
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1149-1437 3.64e-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: 40.75  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1149 EIDRARQNyTILDQITENAKKELQQALDLLnDEGAQALARAKeksvefgQQSEQISDISREARALADKLESEaqfdlkna 1228
Cdd:pfam12795    1 KLDELEKA-KLDEAAKKKLLQDLQQALSLL-DKIDASKQRAA-------AYQKALDDAPAELRELRQELAAL-------- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1229 kDAKDAVEKAHQLAKSAIDlqlkigtELRSEVGLELSHVkqslgtvvQTSKEALRKANevydtalTLLndVNRQTQPEid 1308
Cdd:pfam12795   64 -QAKAEAAPKEILASLSLE-------ELEQRLLQTSAQL--------QELQNQLAQLN-------SQL--IELQTRPE-- 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1309 isQLKKDAVAANERADE----LLKQITELSNSNGELFADFETEQELTEALLKRAEQQQLEDIELLERAKAAHDKATKAVE 1384
Cdd:pfam12795  117 --RAQQQLSEARQRLQQirnrLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQ 194

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160  1385 QGD---NTLKEANNTyeklagfqsdvQRSSEsAEKALQTVPNIEKEIQNAESLISQ 1437
Cdd:pfam12795  195 RLEqqlQALQELLNE-----------KRLQE-AEQAVAQTEQLAEEAAGDHPLVQQ 238
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 721-848 3.69e-03

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 39.98  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  721 CESCAPGYRHSPARGGPfMPCIPC-DCHGHAdicdSETGRCICQHNTHgdnCDqCAKGFYGNALGGTPNDCKRCPcPNDG 799
Cdd:cd13416    35 CEPCLDGVTFSDVVSHT-EPCQPCtRCPGLM----SMRAPCTATHDTV---CE-CAYGYYLDEDSGTCEPCTVCP-PGQG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665410160  800 A---ClQINEDTVictecpkgyfgsrCEQCSDGFFGDPTGLLGEVQTCKSCD 848
Cdd:cd13416   105 VvqsC-GPNQDTV-------------CEACPEGTYSDEDSSTDPCLPCTVCE 142
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 1354-1500 3.77e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.95  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1354 LLKRAEQQQLEDIELLERAK-----AAHDKATKaveqgdntLKEANNTYEKLAGFQSDVQRSSESAEKALQtvpNIEKEI 1428
Cdd:pfam10168  565 LLKLQKEQQLQELQSLEEERkslseRAEKLAEK--------YEEIKDKQEKLMRRCKKVLQRLNSQLPVLS---DAEREM 633

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410160  1429 QNAESLISQAEEALDGANKNANEaKKNAQEAQL-KYAEQASKDAelIRRKANETKVAARNLREEADQLNHRVK 1500
Cdd:pfam10168  634 KKELETINEQLKHLANAIKQAKK-KMNYQRYQIaKSQSIRKKSS--LSLSEKQRKTIKEILKQLGSEIDELIK 703
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1403-1620 3.96e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 41.94  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1403 FQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQASK-DAELIRRKANET 1481
Cdd:pfam05667  256 LRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKvETEEELQQQREE 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1482 KVAArnLREEADQLNHRVKLTEMDIFKLEESSTKDDNLVDdakrkvgQAKADTQEAQKQIEKANADLTAIKDELENLKDI 1561
Cdd:pfam05667  336 ELEE--LQEQLEDLESSIQELEKEIKKLESSIKQVEEELE-------ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKL 406

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665410160  1562 NtGDLDRLENRLATVEGEIN--RVNLtgrIEKYREQRTIQKNLIDKYD---AELRELKDEVQNI 1620
Cdd:pfam05667  407 Q-ALVDASAQRLVELAGQWEkhRVPL---IEEYRALKEAKSNKEDESQrklEEIKELREKIKEV 466
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1310-1634 4.77e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1310 SQLKKDAVAANERADELLKQITE-LSNSNGELFAD--FETEQELTEALLKRAEQQQ--LEDIELLERAKAAHDKATKAVE 1384
Cdd:PRK01156   97 AYIKKDGSIIAEGFDDTTKYIEKnILGISKDVFLNsiFVGQGEMDSLISGDPAQRKkiLDEILEINSLERNYDKLKDVID 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1385 QGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNANEAkkNAQEAQLKYA 1464
Cdd:PRK01156  177 MLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEL--SSLEDMKNRY 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1465 EQASKDAELIRRKANETKVAARNLREEADQL-NHRVKLTEMDIfkleESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEK 1543
Cdd:PRK01156  255 ESEIKTAESDLSMELEKNNYYKELEERHMKIiNDPVYKNRNYI----NDYFKYKNDIENKKQILSNIDAEINKYHAIIKK 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1544 AnADLTAIKDELENLKDintgDLDRLENRLATVEG-EINRVNLTGRIEKyreqrtiQKNLIDKYDAELRELKDEVQNIGL 1622
Cdd:PRK01156  331 L-SVLQKDYNDYIKKKS----RYDDLNNQILELEGyEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEILK 398

                         330
                  ....*....|..
gi 665410160 1623 ISKALPDSCFSR 1634
Cdd:PRK01156  399 IQEIDPDAIKKE 410
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 1370-1482 4.90e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 41.25  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1370 ERAKAAHDKATKAVEQGDNTLKEANNTyeKLAGFQSDVQRSSESAEKALQTVPNIEKEIQNAESLISQAEEALDGANKNA 1449
Cdd:TIGR04320  235 DSYIADGNKFDKTPIPNPPNSLAALQA--KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQA 312

                           90       100       110
                   ....*....|....*....|....*....|....
gi 665410160  1450 -NEAKKNAQEAQlkyaeQASKDAELIRRKANETK 1482
Cdd:TIGR04320  313 lQTAQNNLATAQ-----AALANAEARLAKAKEAL 341
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 1427-1499 5.26e-03

Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun's lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.


Pssm-ID: 468572 [Multi-domain]  Cd Length: 90  Bit Score: 37.66  E-value: 5.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410160 1427 EIQNAESLISQAEEALDGANKNANEAKKNAQEAQLKyAEQASKDAElirrkanetkvAARnlrEEADQLNHRV 1499
Cdd:NF040598   23 DLENLQSQVQELDAKVDQASSDAAAAQSRADEAAAK-AEQAEAAAN-----------AAQ---QEADEANERA 80
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 1148-1271 5.35e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 39.55  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1148 GEIDRARQNyTILDQITEnAKKELQQAldllndegAQALARAKEKSVEFGQQSEQISDiSREARALADKLESEAQfdlkn 1227
Cdd:PRK07352   45 GKILEERRE-AILQALKE-AEERLRQA--------AQALAEAQQKLAQAQQEAERIRA-DAKARAEAIRAEIEKQ----- 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 665410160 1228 akdAKDAVEKAHQLAksAIDL---QLKIGTELRSE-VGLELSHVKQSL 1271
Cdd:PRK07352  109 ---AIEDMARLKQTA--AADLsaeQERVIAQLRREaAELAIAKAESQL 151
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 358-408 5.66e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.56  E-value: 5.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 665410160  358 ACNCNGLADK---CFFdanlfnrtgHGGHCLdCRENRDGPNCERCKENFYMRDD 408
Cdd:cd00055     1 PCDCNGHGSLsgqCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYGLPS 44
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1282-1556 6.30e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1282 LRKANEVYDTALtllnDVNRQTQPEIDISQLKKDA-----------VAAN-----ERADELLKQITELsnsngelfadfe 1345
Cdd:COG3096   227 VRKAFQDMEAAL----RENRMTLEAIRVTQSDRDLfkhliteatnyVAADymrhaNERRELSERALEL------------ 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1346 tEQELTEALLKRAEQQQL-----EDIELLERAKAAHDKATKAVEQGDNTLKEANNTYEKLAGFQSDVQRSSESAEKALQT 1420
Cdd:COG3096   291 -RRELFGARRQLAEEQYRlvemaRELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEV 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1421 VPNIEKEIQNAESLISQAEEALDganknanEAKknaqeAQLKYAEQAskdAELIRRKANETKVAARNLrEEADQLNHRVK 1500
Cdd:COG3096   370 VEEAAEQLAEAEARLEAAEEEVD-------SLK-----SQLADYQQA---LDVQQTRAIQYQQAVQAL-EKARALCGLPD 433

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665410160 1501 LTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLTAIKDELE 1556
Cdd:COG3096   434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVE 489
OEP pfam02321
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ...
 1448-1548 6.79e-03

Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.


Pssm-ID: 396757 [Multi-domain]  Cd Length: 181  Bit Score: 39.43  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1448 NANEAKKNAQEAQLKYAEQASKDAEL-IRRKANETKVAARNLREEADQLNHRVKLTEMDI------FKLEESSTKDdnlV 1520
Cdd:pfam02321   72 GKRRARVKAAKAQVEAAEAQLEQARQqLRLEVAQAYLQLLAAKEQLELAEQALELAEEALelaearYEAGLISLLD---V 148

                           90       100
                   ....*....|....*....|....*...
gi 665410160  1521 DDAKRKVGQAKADTQEAQKQIEKANADL 1548
Cdd:pfam02321  149 LQAEVELLEARLELLNAEADLELALAQL 176
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 1471-1609 7.77e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 39.21  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1471 AELIRRKANETkvaARNLREEADQLNHRVkltemdifkLEESSTKDDNLVDDAKRKvgqAKADTQEAQKQiEKANADLTA 1550
Cdd:PRK02292    7 VEDIRDEARAR---ASEIRAEADEEAEEI---------IAEAEADAEEILEDREAE---AEREIEQLREQ-ELSSAKLEA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1551 IKDELENLKDINTGDLDRLENRLATVEGEinrvnltgriekyrEQRTIQKNLIDKYDAE 1609
Cdd:PRK02292   71 KRERLNARKEVLEDVRNQVEDEIASLDGD--------------KREELTKSLLDAADAD 115
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1451-1561 7.95e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1451 EAKKNAQEAQLKYAEQASKDAELIRRKANEtkvAARNLREEADQLnhrvkltemdifkLEESstkddnlVDDAKRKVGQA 1530
Cdd:COG0711    30 DERQEKIADGLAEAERAKEEAEAALAEYEE---KLAEARAEAAEI-------------IAEA-------RKEAEAIAEEA 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 665410160 1531 KADTQ-EAQKQIEKANADLTAIKDE-LENLKDI 1561
Cdd:COG0711    87 KAEAEaEAERIIAQAEAEIEQERAKaLAELRAE 119
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1140-1246 8.03e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1140 DKFQADANGEIDRARQNYTILDQITENAKKELQQAldllNDEGAQALARAKEksvefgQQSEQISDISREARALADKLES 1219
Cdd:COG0711    30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA----RAEAAEIIAEARK------EAEAIAEEAKAEAEAEAERIIA 99

                          90       100       110
                  ....*....|....*....|....*....|...
gi 665410160 1220 EAQFDLKNAKDA------KDAVEKAHQLAKSAI 1246
Cdd:COG0711   100 QAEAEIEQERAKalaelrAEVADLAVAIAEKIL 132
PRK12704 PRK12704
phosphodiesterase; Provisional
 1424-1558 8.44e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160 1424 IEKEIQNAESlisQAEEALDGANKNANEAKK----NAQEAQLKYAEQASKDaelIRRKanetkvaarnlREEADQLNHRV 1499
Cdd:PRK12704   29 AEAKIKEAEE---EAKRILEEAKKEAEAIKKeallEAKEEIHKLRNEFEKE---LRER-----------RNELQKLEKRL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 665410160 1500 KLTEMDIFKLEESSTKDDNLVDDAKRKVGQAKADTQEAQKQIEKANADLtaiKDELENL 1558
Cdd:PRK12704   92 LQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ---LQELERI 147
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1321-1493 9.55e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.78  E-value: 9.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1321 ERADELLKQITELSNSNG----ELFADFETEQELTEALLkraeQQQLEDIE--LLERAKAAHDKATKAVEQGDNTLKEAN 1394
Cdd:pfam01442    4 DSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERL----QKDLEEVRakLEPYLEELQAKLGQNVEELRQRLEPYT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410160  1395 NTYEKLAGFQSD------VQRSSESAEKALQTVpnieKEIQnaESLISQAEEALDGANKNANEAKKNAQEAQLKYAEQAS 1468
Cdd:pfam01442   80 EELRKRLNADAEelqeklAPYGEELRERLEQNV----DALR--ARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLS 153

                          170       180
                   ....*....|....*....|....*
gi 665410160  1469 KDAELIRRKAnetKVAARNLREEAD 1493
Cdd:pfam01442  154 QRLQELREKL---EPQAEDLREKLD 175
 
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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