NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564365344|ref|XP_006243771|]
View 

laminin subunit beta-2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
50-284 8.61e-106

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 337.25  E-value: 8.61e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055    1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055   72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055  151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228


                   ..
gi 564365344   283 RG 284
Cdd:pfam00055  229 GG 230
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
 1730-1801 4.52e-37

C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.


:

Pssm-ID: 411970 [Multi-domain]  Cd Length: 72  Bit Score: 134.11  E-value: 4.52e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22299     1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1448-1793 1.10e-22

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 106.17  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196   320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1767
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528

                         330       340
                  ....*....|....*....|....*.
gi 564365344 1768 ELEVKAAQLDGLEARMRSVLQAINLQ 1793
Cdd:COG1196   529 LIGVEAAYEAALEAALAAALQNIVVE 554
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
786-831 2.74e-14

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.49  E-value: 2.74e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344    786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 831
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1146-1193 1.73e-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: 1.73e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564365344  1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1193
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 524-565 2.04e-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: 2.04e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 564365344  524 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 413-470 8.45e-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: 58.52  E-value: 8.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344   413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 470
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1098-1146 1.11e-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: 58.13  E-value: 1.11e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1041-1095 2.90e-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: 56.98  E-value: 2.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344  1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 1095
Cdd:pfam00053    1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 834-882 3.04e-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: 56.98  E-value: 3.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344   834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 882
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 472-523 8.37e-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: 55.82  E-value: 8.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365344  472 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055     1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 989-1031 1.21e-08

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 52.36  E-value: 1.21e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564365344   989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 880-927 3.87e-07

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 3.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564365344   880 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 927
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 929-987 2.93e-06

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: 45.81  E-value: 2.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344  929 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 987
Cdd:cd00055     1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 350-402 1.54e-05

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: 43.88  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055     2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 286-338 1.97e-05

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: 43.50  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055     2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
50-284 8.61e-106

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 337.25  E-value: 8.61e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055    1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055   72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055  151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228


                   ..
gi 564365344   283 RG 284
Cdd:pfam00055  229 GG 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 44-284 4.95e-84

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: 275.39  E-value: 4.95e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344     44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136   73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136  151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230


                    ....*...
gi 564365344    277 LYELVIRG 284
Cdd:smart00136  231 ISDIAVGG 238
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
 1730-1801 4.52e-37

C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.


Pssm-ID: 411970 [Multi-domain]  Cd Length: 72  Bit Score: 134.11  E-value: 4.52e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22299     1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1448-1793 1.10e-22

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 106.17  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196   320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1767
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528

                         330       340
                  ....*....|....*....|....*.
gi 564365344 1768 ELEVKAAQLDGLEARMRSVLQAINLQ 1793
Cdd:COG1196   529 LIGVEAAYEAALEAALAAALQNIVVE 554
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1465-1790 5.55e-17

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 87.40  E-value: 5.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1465 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1536
Cdd:PRK02224  210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1537 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:PRK02224  290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1609 TVQAALEEAQRAQGAAQGAIR--------------GAVVDTKNTE-------QTLQQVQERMAGTEQSLNSASERARQLH 1667
Cdd:PRK02224  367 ELESELEEAREAVEDRREEIEeleeeieelrerfgDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1714
Cdd:PRK02224  447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344 1715 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEaRMRSVLQAI 1790
Cdd:PRK02224  527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1199-1796 4.23e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 4.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1199 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1276
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1277 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1354
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1355 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1414
Cdd:TIGR02168  518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1415 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1484
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1564
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1565 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK----NTEQ 1640
Cdd:TIGR02168  752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRE 824

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1641 TLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKQLreqvgdqyqtVRALA 1720
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--------------ELEELIEELESEL----------EALLN 880

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1721 ERKAegvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:TIGR02168  881 ERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
786-831 2.74e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.49  E-value: 2.74e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344    786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 831
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 785-832 4.64e-14

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: 67.76  E-value: 4.64e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344  785 PCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGF--GPAGCQ 832
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 786-834 5.04e-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: 67.76  E-value: 5.04e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344   786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 834
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1448-1756 7.14e-14

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 77.56  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1514
Cdd:NF041483  478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1515 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDA- 1593
Cdd:NF041483  558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADAr 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1594 ---QRARSRA--EGERQKAE------TVQA-ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQvqERMAGTEQSLNSASE 1661
Cdd:NF041483  600 aeaERIRREAaeETERLRTEaaerirTLQAqAEQEAERLRTEAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQE 677

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1662 RARQLHALLEALKLK---RAGNSLAAST---------AEETAGSAQS-------RAREAEKQL----REQVGD-QYQTVR 1717
Cdd:NF041483  678 SADRVRAEAAAAAERvgtEAAEALAAAQeeaarrrreAEETLGSARAeadqereRAREQSEELlasaRKRVEEaQAEAQR 757

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 564365344 1718 ALAE---RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ 1756
Cdd:NF041483  758 LVEEadrRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
growth_prot_Scy NF041483
polarized growth protein Scy;
1446-1790 1.39e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 73.32  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1446 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1524
Cdd:NF041483  909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1525 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1591
Cdd:NF041483  984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1592 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1654
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1655 SLNsasERARQLHAllEALKlkRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AA 1730
Cdd:NF041483 1136 ELH---ERARRESA--EQMK--SAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAE 1204

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344 1731 QARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1790
Cdd:NF041483 1205 QKKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
growth_prot_Scy NF041483
polarized growth protein Scy;
1458-1776 1.37e-11

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 69.85  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1458 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1529
Cdd:NF041483  158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1530 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1607
Cdd:NF041483  234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 ETVQAALEEAQRAQGAAQGAIRGAvvdtknTEQTLQQVQERMAGTEqSLNSASERARQlHALLEALKL-KRAGNSLAAST 1686
Cdd:NF041483  287 EAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTVA 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1687 AEETAGSAQSRAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDE----ARGLLQAAQD--KLQRLQELE 1759
Cdd:NF041483  359 AEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE-EAERIRReAEAEADRLRGEaadqAEQLKGAAKDdtKEYRAKTVE 437

                         330
                  ....*....|....*..
gi 564365344 1760 gtYEENERELEVKAAQL 1776
Cdd:NF041483  438 --LQEEARRLRGEAEQL 452
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1146-1193 1.73e-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: 1.73e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564365344  1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1193
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 524-565 2.04e-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: 2.04e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 564365344  524 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
525-564 2.84e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.02  E-value: 2.84e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 564365344    525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 1463-1784 4.06e-11

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 68.24  E-value: 4.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1463 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1521
Cdd:pfam07111  354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1522 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1592
Cdd:pfam07111  434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1593 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1672
Cdd:pfam07111  508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1673 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1736
Cdd:pfam07111  562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1737 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1784
Cdd:pfam07111  634 rLQDEARK--EEGQRLARRVQEL-----ERDKNLMLATLQQEGLLSRYK 675
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 413-470 8.45e-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: 58.52  E-value: 8.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344   413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 470
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1098-1146 1.11e-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: 58.13  E-value: 1.11e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1446-1770 1.56e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 66.39  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1446 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1521
Cdd:NF041483  720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1522 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1600
Cdd:NF041483  787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1601 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1670
Cdd:NF041483  843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1671 --EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1748
Cdd:NF041483  923 tsEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002

                         330       340
                  ....*....|....*....|..
gi 564365344 1749 QDKLQRLQelEGTYEENERELE 1770
Cdd:NF041483 1003 AAEAERLR--TEAREEADRTLD 1022
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1145-1194 2.15e-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: 2.15e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344 1145 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1194
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1041-1095 2.90e-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: 56.98  E-value: 2.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344  1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 1095
Cdd:pfam00053    1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 834-882 3.04e-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: 56.98  E-value: 3.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344   834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 882
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1146-1190 7.37e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.78  E-value: 7.37e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344   1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1190
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 472-523 8.37e-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: 55.82  E-value: 8.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365344  472 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055     1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1040-1096 8.87e-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: 55.82  E-value: 8.87e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1040 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 1096
Cdd:cd00055     1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 473-527 1.20e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.44  E-value: 1.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1556-1778 2.10e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 62.92  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1556 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1618
Cdd:NF041483  130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1619 RAQGAAQGAIRGAVVDTknteqtlqqvqERMagteqsLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSR 1697
Cdd:NF041483  204 SARAEAEAILRRARKDA-----------ERL------LNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQR 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1698 AREAEKQLREqvgdqyqtvralaerkaegvlaAQARAEQLRDEARgllQAAQdklQRLQELEGTYEENERELEVKAAQLD 1777
Cdd:NF041483  267 MQEAEEALRE----------------------ARAEAEKVVAEAK---EAAA---KQLASAESANEQRTRTAKEEIARLV 318


                  .
gi 564365344 1778 G 1778
Cdd:NF041483  319 G 319
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 412-471 2.23e-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: 54.67  E-value: 2.23e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 471
Cdd:cd00055     1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 525-564 3.09e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.28  E-value: 3.09e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564365344   525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1098-1143 3.67e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.85  E-value: 3.67e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344   1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1143
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1097-1144 4.21e-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: 53.90  E-value: 4.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344 1097 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1144
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1041-1095 8.26e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 8.26e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 1095
Cdd:smart00180    1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 989-1031 1.21e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 52.36  E-value: 1.21e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564365344   989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 833-875 3.35e-08

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: 51.20  E-value: 3.35e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564365344  833 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
834-875 5.42e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.77  E-value: 5.42e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 564365344    834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
growth_prot_Scy NF041483
polarized growth protein Scy;
1554-1770 5.94e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.91  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1554 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1627
Cdd:NF041483   44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1628 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRArEAEK---Q 1704
Cdd:NF041483  121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARA-EAERlaeE 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1705 LREQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQEL 1758
Cdd:NF041483  194 ARQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEA 270

                         250
                  ....*....|..
gi 564365344 1759 EGTYEENERELE 1770
Cdd:NF041483  271 EEALREARAEAE 282
growth_prot_Scy NF041483
polarized growth protein Scy;
1459-1789 6.04e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.91  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1459 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1533
Cdd:NF041483  252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1534 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1598
Cdd:NF041483  326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1599 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1650
Cdd:NF041483  401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1651 GTEQSLNSA--------------SERARQlHALLEALKLKRagnslaasTAEETAgsaqSRAREAEKQLREQVGDQYQTV 1716
Cdd:NF041483  481 TAEELLTKAkadadelrstataeSERVRT-EAIERATTLRR--------QAEETL----ERTRAEAERLRAEAEEQAEEV 547

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1717 RALAERKA-----EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSv 1786
Cdd:NF041483  548 RAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT- 626


                  ...
gi 564365344 1787 LQA 1789
Cdd:NF041483  627 LQA 629
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
413-470 8.67e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 8.67e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344    413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 470
Cdd:smart00180    1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 989-1035 9.11e-08

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: 50.05  E-value: 9.11e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 564365344  989 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 1035
Cdd:cd00055     2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
473-516 9.95e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 9.95e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 564365344    473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 516
Cdd:smart00180    1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 880-927 3.87e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 3.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564365344   880 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 927
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 879-924 5.64e-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: 47.73  E-value: 5.64e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564365344  879 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 924
Cdd:cd00055     1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 929-987 2.93e-06

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: 45.81  E-value: 2.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344  929 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 987
Cdd:cd00055     1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
989-1031 2.99e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 45.77  E-value: 2.99e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 564365344    989 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:smart00180    1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 350-402 1.54e-05

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: 43.88  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055     2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1476-1747 1.67e-05

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: 48.44  E-value: 1.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1476 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1553
Cdd:smart00283    2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1554 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRArsraeGERQK-----AETVQaAL 1614
Cdd:smart00283   75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARA-----GEAGRgfavvADEVR-KL 138

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1615 eeAQRAQGAAqgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTaEETAGSA 1694
Cdd:smart00283  139 --AERSAESA-----------KEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE--ETGDALEEIVDSV-EEIADLV 202

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   1695 QSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1747
Cdd:smart00283  203 QEIAAATDEQAAgsEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 350-401 1.67e-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: 43.50  E-value: 1.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   350 CECNGH---SHSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 401
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 956-986 1.90e-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: 43.50  E-value: 1.90e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 564365344   956 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 986
Cdd:pfam00053   19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 286-338 1.97e-05

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: 43.50  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055     2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
930-979 3.44e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 42.68  E-value: 3.44e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 564365344    930 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 979
Cdd:smart00180    1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 1684-1795 3.72e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 46.09  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1684 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:PRK14475   36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564365344 1760 GTYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1795
Cdd:PRK14475  115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1696-1791 8.37e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1696 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKL----QRLQELEGTYEENERELE 1770
Cdd:COG4913   238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312

                          90       100
                  ....*....|....*....|.
gi 564365344 1771 VKAAQLDGLEARMRSVLQAIN 1791
Cdd:COG4913   313 RLEARLDALREELDELEAQIR 333
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 1585-1620 3.03e-04

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: 41.52  E-value: 3.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564365344 1585 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1620
Cdd:NF040598   37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
880-919 4.02e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 4.02e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 564365344    880 CVCNGR---ADECDAHTGACLgCRDYTGGEHCERCIAGFHGDP 919
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1469-1756 4.76e-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: 45.21  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1469 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1548
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1549 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1625
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1626 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALL---EALKLKRAGNSLA----------ASTAEET 1690
Cdd:NF012221 1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1691 AGSAQSRAR-----EAEKQLREQV------GDQYqTVRALAER----KAEGVLAAQAR-AEQLRDEARGLLQAAQDKLQR 1754
Cdd:NF012221 1762 ANQAQADAKgakqdESDKPNRQGAagsglsGKAY-SVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNR 1840


                  ..
gi 564365344 1755 LQ 1756
Cdd:NF012221 1841 LQ 1842
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 1571-1770 4.79e-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: 43.50  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1571 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1650
Cdd:cd07596     1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1651 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKQlREQVGDQYQTV-------RALAE 1721
Cdd:cd07596    71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDD-RADALLTLQSLkkdlaskKAQLE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564365344 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1770
Cdd:cd07596   135 KLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
350-403 1.21e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.45  E-value: 1.21e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344    350 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 403
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
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 ...
 1720-1796 2.23e-03

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: 39.99  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1720 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1791
Cdd:pfam00430   42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121


                   ....*
gi 564365344  1792 LQVQI 1796
Cdd:pfam00430  122 LAVQI 126
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 309-341 3.64e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.95  E-value: 3.64e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 564365344   309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053   16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
50-284 8.61e-106

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 337.25  E-value: 8.61e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    50 CYPATGDLLVGRadRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQRRTaWWQS 129
Cdd:pfam00055    1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPH------NSHPPSNLTDSNNGTNET-WWQS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   130 ENGVPM---VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVV 204
Cdd:pfam00055   72 ETGVIQyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   205 CESRYSEIEPSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVI 282
Cdd:pfam00055  151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228


                   ..
gi 564365344   283 RG 284
Cdd:pfam00055  229 GG 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 44-284 4.95e-84

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: 275.39  E-value: 4.95e-84
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344     44 GCSRGSCYPATGDLLVGRadRLTASSTCGLHSPQPYCI-VSHLQDEKKCFLCDSRRPFsardnpNSHRIQNVVTSFAPQR 122
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPR------RSHPAENLTDGNNPNN 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    123 RTaWWQSEN---GVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR 199
Cdd:smart00136   73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344    200 --WDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYA 276
Cdd:smart00136  151 gnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230


                    ....*...
gi 564365344    277 LYELVIRG 284
Cdd:smart00136  231 ISDIAVGG 238
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
 1730-1801 4.52e-37

C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.


Pssm-ID: 411970 [Multi-domain]  Cd Length: 72  Bit Score: 134.11  E-value: 4.52e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22299     1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
 1731-1800 2.48e-24

C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.


Pssm-ID: 411969 [Multi-domain]  Cd Length: 70  Bit Score: 97.73  E-value: 2.48e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1731 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22295     1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1448-1793 1.10e-22

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 106.17  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196   320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1767
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528

                         330       340
                  ....*....|....*....|....*.
gi 564365344 1768 ELEVKAAQLDGLEARMRSVLQAINLQ 1793
Cdd:COG1196   529 LIGVEAAYEAALEAALAAALQNIVVE 554
cc_LAMB1_C cd22300
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ...
 1730-1800 7.49e-22

C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.


Pssm-ID: 411971 [Multi-domain]  Cd Length: 73  Bit Score: 91.00  E-value: 7.49e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365344 1730 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22300     2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1452-1782 2.34e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 101.94  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1452 ADLALGRARHTQAELQRAlvegggilsrvSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLSQEga 1531
Cdd:COG1196   227 AELLLLKLRELEAELEEL-----------EAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEE-- 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1532 dpdsiemvatRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1611
Cdd:COG1196   291 ----------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1612 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETA 1691
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1692 GSAQSRAREAEKQLREQvgdQYQTVRALAERKAEgvlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERelEV 1771
Cdd:COG1196   441 EEALEEAAEEEAELEEE---EEALLELLAELLEE-----AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE--GV 510

                         330
                  ....*....|.
gi 564365344 1772 KAAQLDGLEAR 1782
Cdd:COG1196   511 KAALLLAGLRG 521
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1554-1790 7.88e-20

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 96.93  E-value: 7.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1554 QIQRLA--SEIAERVRSLADVDTILAHTM---------GDVRRAEQLLQDAQRARSRAEGERQKAET----VQAALEEAQ 1618
Cdd:COG1196   201 QLEPLErqAEKAERYRELKEELKELEAELlllklreleAELEELEAELEELEAELEELEAELAELEAeleeLRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1619 RAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA 1698
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1699 REAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDG 1778
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                         250
                  ....*....|..
gi 564365344 1779 LEARMRSVLQAI 1790
Cdd:COG1196   440 EEEALEEAAEEE 451
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1492-1794 1.39e-18

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 92.39  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1492 QRAQAALDKANASRGQVEQANQELRELIQNVKdflsqegadpdsIEMVA-TRVLDISIPA-SPEQIQRLASEIAErvrsl 1569
Cdd:COG3206    97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLT------------VEPVKgSNVIEISYTSpDPELAAAVANALAE----- 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1570 ADVDTILAHTMGDVRRAEQLLQDaqrarsRAEGERQKAETVQAALEEAQRAQGAAqgairgavvdtkNTEQTLQQVQERM 1649
Cdd:COG3206   160 AYLEQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLLQQL 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1650 AGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE-----KQLREQVGDQYQTVRALAERKA 1724
Cdd:COG3206   222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEleaelAELSARYTPNHPDVIALRAQIA 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1725 E-----------GVLAAQARAEQLR---DEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3206   302 AlraqlqqeaqrILASLEAELEALQareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381


                  ....
gi 564365344 1791 NLQV 1794
Cdd:COG3206   382 ALTV 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1448-1755 3.98e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 91.15  E-value: 3.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLS 1527
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 QEGADPDSIEMVATRVLDISipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 EtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1687
Cdd:COG1196   427 E---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRL 1755
Cdd:COG1196   504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1465-1790 5.55e-17

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 87.40  E-value: 5.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1465 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1536
Cdd:PRK02224  210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1537 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:PRK02224  290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1609 TVQAALEEAQRAQGAAQGAIR--------------GAVVDTKNTE-------QTLQQVQERMAGTEQSLNSASERARQLH 1667
Cdd:PRK02224  367 ELESELEEAREAVEDRREEIEeleeeieelrerfgDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1714
Cdd:PRK02224  447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344 1715 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEaRMRSVLQAI 1790
Cdd:PRK02224  527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1245-1789 1.18e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.53  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1245 QAIVAARNTSAASTAKLVEAtEGLRHEIGKTTERLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDIL 1324
Cdd:COG1196   208 QAEKAERYRELKEELKELEA-ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1325 KHSNFLGAYDSIRHAHSQSTEAERRANAstfaipspvsnsADTRRRAEvlmgAQRENFNRQHLANQQALGRLSThthtls 1404
Cdd:COG1196   287 QAEEYELLAELARLEQDIARLEERRREL------------EERLEELE----EELAELEEELEELEEELEELEE------ 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1405 ltgvnelvcgapgdapcatspcggagcrdedgqprcgglgcsgAAATADLALGRARHTQAELQRALVEgggILSRVSETR 1484
Cdd:COG1196   345 -------------------------------------------ELEEAEEELEEAEAELAEAEEALLE---AEAELAEAE 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASpEQIQRLASEIAE 1564
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEE 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1565 RVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQG-AAQGAIRGAVVDTKNTEQTLQ 1643
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYE 537

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1644 QVQE-RMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER 1722
Cdd:COG1196   538 AALEaALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344 1723 KAEGV------------LAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1789
Cdd:COG1196   616 YVLGDtllgrtlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1564-1782 1.54e-16

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 86.12  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1564 ERVRSLADVDTILAHtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGA-IRGAVVDTKNTEQTL 1642
Cdd:COG4913   219 EEPDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1643 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQT-VRAL-- 1719
Cdd:COG4913   298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----REIERLERELEERERRRARLEAlLAALgl 373

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365344 1720 -AERKAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENERELEVKAAQLDGLEAR 1782
Cdd:COG4913   374 pLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1199-1791 3.93e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1199 DWDRVVQDLAARTRRLEQWAQELQQT-GVLGAFESSFLNLQgklgmvQAIVAARNTSAASTAKLVEATEGLRHEigktTE 1277
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELeAELEELRLELEELE------LELEEAQAEEYELLAELARLEQDIARL----EE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1278 RLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDILKH--SNFLGAYDSIRHAHSQSTEAERRANASTF 1355
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELAEAEEELEELAEELL 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1356 AIpspVSNSADTRRRAEVLMGAQRENFNRQHLANQQALGRLSTHTHTLSLtgvnelvcgapgdapcatspcggagcRDED 1435
Cdd:COG1196   390 EA---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------------------------EEEE 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1436 GQprcgglgcsgAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQEL 1515
Cdd:COG1196   441 EE----------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1516 RELIQNVKDF-LSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVD-----TILAHTMGDVRRAEQL 1589
Cdd:COG1196   511 KAALLLAGLRgLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAA 590

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1590 LQDA---QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMA----------GTEQSL 1656
Cdd:COG1196   591 ALARgaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltgGSRREL 670

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1657 NSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAA 1730
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleellEEEELLEE 750

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1731 QARAEQLRDEARGLLQAAQDKLQR------------LQELEgtyEENER--ELEvkaAQLDGLEARMRSVLQAIN 1791
Cdd:COG1196   751 EALEELPEPPDLEELERELERLEReiealgpvnllaIEEYE---ELEERydFLS---EQREDLEEARETLEEAIE 819
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1199-1796 4.23e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 4.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1199 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1276
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1277 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1354
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1355 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1414
Cdd:TIGR02168  518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1415 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1484
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1564
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1565 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK----NTEQ 1640
Cdd:TIGR02168  752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRE 824

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1641 TLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKQLreqvgdqyqtVRALA 1720
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--------------ELEELIEELESEL----------EALLN 880

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1721 ERKAegvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:TIGR02168  881 ERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
cc_DmLAMB1-like_C cd22302
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ...
 1731-1800 8.19e-15

C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.


Pssm-ID: 411973 [Multi-domain]  Cd Length: 70  Bit Score: 70.72  E-value: 8.19e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1731 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22302     1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
786-831 2.74e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.49  E-value: 2.74e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344    786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 831
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 785-832 4.64e-14

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: 67.76  E-value: 4.64e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344  785 PCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGF--GPAGCQ 832
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1204-1791 4.78e-14

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 78.17  E-value: 4.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1204 VQDLAARTRRLEQWAQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEATEGLRHEIGKTTERLTQLE 1283
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1284 AELTDVQD-------------ENFNANHALSGL-----------ERDGLALNLTLRQLDQHL------------DILKHS 1327
Cdd:TIGR02168  489 ARLDSLERlqenlegfsegvkALLKNQSGLSGIlgvlselisvdEGYEAAIEAALGGRLQAVvvenlnaakkaiAFLKQN 568

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1328 N-----FLgAYDSIRHAHSQSTEAERRANASTFAipSPVSNSADTRRRAEVLMGAQrenFNR----QHLANQQALGRLST 1398
Cdd:TIGR02168  569 ElgrvtFL-PLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKFDPKLRKALSYL---LGGvlvvDDLDNALELAKKLR 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1399 HTHTL-SLTGvnELV--CG--APGDAPCATspcgGAGCRD---EDGQPRCGGLGcsGAAATADLALGRARHTQAELQ--- 1467
Cdd:TIGR02168  643 PGYRIvTLDG--DLVrpGGviTGGSAKTNS----SILERRreiEELEEKIEELE--EKIAELEKALAELRKELEELEeel 714

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1468 -----------RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASR----GQVEQANQELRELIQNVKDFlsQEGAD 1532
Cdd:TIGR02168  715 eqlrkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEEL--EAQIE 792

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1533 PDSIEMVATRvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvqA 1612
Cdd:TIGR02168  793 QLKEELKALR----------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---A 859

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1613 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAG 1692
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-------QLELRLE 932

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1693 SAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRdeargllqaaqDKLQRL--------QELEgtyEE 1764
Cdd:TIGR02168  933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----------NKIKELgpvnlaaiEEYE---EL 998

                          650       660
                   ....*....|....*....|....*..
gi 564365344  1765 NEReLEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:TIGR02168  999 KER-YDFLTAQKEDLTEAKETLEEAIE 1024
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 786-834 5.04e-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: 67.76  E-value: 5.04e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344   786 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 834
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1448-1756 7.14e-14

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 77.56  E-value: 7.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1514
Cdd:NF041483  478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1515 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDA- 1593
Cdd:NF041483  558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADAr 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1594 ---QRARSRA--EGERQKAE------TVQA-ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQvqERMAGTEQSLNSASE 1661
Cdd:NF041483  600 aeaERIRREAaeETERLRTEaaerirTLQAqAEQEAERLRTEAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQE 677

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1662 RARQLHALLEALKLK---RAGNSLAAST---------AEETAGSAQS-------RAREAEKQL----REQVGD-QYQTVR 1717
Cdd:NF041483  678 SADRVRAEAAAAAERvgtEAAEALAAAQeeaarrrreAEETLGSARAeadqereRAREQSEELlasaRKRVEEaQAEAQR 757

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 564365344 1718 ALAE---RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ 1756
Cdd:NF041483  758 LVEEadrRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1477-1792 1.52e-13

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 75.96  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQ 1556
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1557 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLL-----QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgA 1631
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-Q 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1632 VVDTKNTEQTLQQVQERM------------AGTEQSLNSASERARQLHALLEAL------KLKRAGNSLAASTAEETAGS 1693
Cdd:COG4717   232 LENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALP 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1694 AQSRAREAE-KQLREQVG--------------DQYQTVRALAERKAEgvLAAQARAEQLRDEARGLLQAAQ----DKLQR 1754
Cdd:COG4717   312 ALEELEEEElEELLAALGlppdlspeellellDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAGvedeEELRA 389

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 564365344 1755 LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINL 1792
Cdd:COG4717   390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1440-1736 1.68e-13

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 74.48  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1440 CGGLGCSGAAATADLALGRARHTQAELQRALVEgggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELI 1519
Cdd:COG3883     2 LALALAAPTPAFADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1520 QNVKD----------FLSQEGADPDSIEMVATrvldisipaspeqiqrlASEIAERVRSLADVDTILAHTMGDVRRAEQL 1589
Cdd:COG3883    79 AEIEErreelgerarALYRSGGSVSYLDVLLG-----------------SESFSDFLDRLSALSKIADADADLLEELKAD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1590 LQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlhal 1669
Cdd:COG3883   142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA---- 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344 1670 lEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQ 1736
Cdd:COG3883   218 -AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1456-1789 1.74e-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: 76.26  E-value: 1.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1456 LGRARHTQAELQRALVEGGGILSRVSETRRQAE-------EAQQRAQ----AALDKANASRGQVEQANQELRELIQNVKD 1524
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYEGyellKEKEALERQKEAIERQLASLEEELEKLTE 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1525 FLSQEGADPDSIEmvatRVLDisipASPEQIQRLASEIAERVRS-LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGE 1603
Cdd:TIGR02169  259 EISELEKRLEEIE----QLLE----ELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1604 RQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL----QQVQERMAGTEQSLNSASERarqlhalLEALKLKRag 1679
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETRDELKDYREK-------LEKLKREI-- 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1680 NSLAAStaeetagsaQSRAREAEKQLREQVGDqyqtVRALAERKAEGVLAAQARAEQLRDE---ARGLLQAAQDKL---- 1752
Cdd:TIGR02169  402 NELKRE---------LDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEikkQEWKLEQLAADLskye 468

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 564365344  1753 QRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1789
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
mukB PRK04863
chromosome partition protein MukB;
1449-1796 1.76e-13

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 76.15  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1449 AATADLALGRARHtQAELQRALVEGGGILSRVSETRRQAEEAQQRA---QAALDKANASRGQVEQANQELRELIQNVKDF 1525
Cdd:PRK04863  265 ESTNYVAADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNLVQTA 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1526 LSQEGAdpdsIEMVATRVLDISIPA-SPEQIQRLASEIAERVRSLA-----DVDTiLAHTMGDVRRAEQLLQdaqrarSR 1599
Cdd:PRK04863  344 LRQQEK----IERYQADLEELEERLeEQNEVVEEADEQQEENEARAeaaeeEVDE-LKSQLADYQQALDVQQ------TR 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1600 AeGERQKAetvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlHAllEALKLKRag 1679
Cdd:PRK04863  413 A-IQYQQA---VQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ-FE--QAYQLVR-- 483

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1680 nSLAASTAEETAgsaQSRAREAEKQLREQ--VGDQYQTVRA-LAErkAEGVLAAQARAEQLRDEArglLQAAQDKLQRLQ 1756
Cdd:PRK04863  484 -KIAGEVSRSEA---WDVARELLRRLREQrhLAEQLQQLRMrLSE--LEQRLRQQQRAERLLAEF---CKRLGKNLDDED 554

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 564365344 1757 ELEGTYEENERELEVKAAQLDGLEARmRSVLQAINLQVQI 1796
Cdd:PRK04863  555 ELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQA 593
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1452-1784 6.04e-13

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: 74.60  E-value: 6.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1452 ADLALGRARhtQAELQRALVEGGGILSRVSETRRQAEEAQQ-----RAQAAL-------DKANASRGQVEQANQELRELI 1519
Cdd:COG3096   836 AELAALRQR--RSELERELAQHRAQEQQLRQQLDQLKEQLQllnklLPQANLladetlaDRLEELREELDAAQEAQAFIQ 913

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1520 QN------VKDFLSQEGADPDSIEMVATRVLDISipASPEQIQRLA---SEIAERVRSLA--DVDTILAHTMGDVRRAEQ 1588
Cdd:COG3096   914 QHgkalaqLEPLVAVLQSDPEQFEQLQADYLQAK--EQQRRLKQQIfalSEVVQRRPHFSyeDAVGLLGENSDLNEKLRA 991

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1589 LLQDAQRARSRAegeRQKAETVQAALEEAQRAQGAAQGAIrgavvDTKNteQTLQQVQERMAGTEQSLNS-ASERAR--- 1664
Cdd:COG3096   992 RLEQAEEARREA---REQLRQAQAQYSQYNQVLASLKSSR-----DAKQ--QTLQELEQELEELGVQADAeAEERARirr 1061

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1665 -QLHALLEALKLKRagNSLAASTA--EETAGSAQSRAREAEK---QLREQV---GDQYQTVRALA-----ERK-AEGVLA 1729
Cdd:COG3096  1062 dELHEELSQNRSRR--SQLEKQLTrcEAEMDSLQKRLRKAERdykQEREQVvqaKAGWCAVLRLArdndvERRlHRRELA 1139

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365344 1730 AQArAEQLR---DEARGLLQAAQDKLQRLQELEGTYEEN---ERELEVKAAQLDGLEARMR 1784
Cdd:COG3096  1140 YLS-ADELRsmsDKALGALRLAVADNEHLRDALRLSEDPrrpERKVQFYIAVYQHLRERIR 1199
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1458-1791 9.20e-13

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 73.26  E-value: 9.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1458 RARHTQAELQRALVEGG-GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVkdflsQEGADPDSI 1536
Cdd:COG4717   171 ELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1537 EMVATRVLDISIPASpeqIQRLASEIAERVRSLADVDTI---LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvQAA 1613
Cdd:COG4717   246 KEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLvlgLLALLFLLLAREKASLGKEAEELQALPALEELE--EEE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1614 LEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsaseRARQLHALLEALkLKRAGnslaaSTAEETAGS 1693
Cdd:COG4717   321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAAL-LAEAG-----VEDEEELRA 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1694 AQSRAREAEK------QLREQVGDQYQTVRALAERKAEGVLAAQ-ARAEQLRDEARGLLQAAQDKL----QRLQELE--G 1760
Cdd:COG4717   390 ALEQAEEYQElkeeleELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELaeleAELEQLEedG 469

                         330       340       350
                  ....*....|....*....|....*....|....
gi 564365344 1761 TYEENERELEVKAAQLDGLE---ARMRSVLQAIN 1791
Cdd:COG4717   470 ELAELLQELEELKAELRELAeewAALKLALELLE 503
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1455-1789 1.12e-12

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: 73.83  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1455 ALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA--------------QAALDKANASRGQVEQANQELREliq 1520
Cdd:COG3096   348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAeeevdslksqladyQQALDVQQTRAIQYQQAVQALEK--- 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1521 nvkdflSQE--GADPDSIEMVATRVldisipaspEQIQRLASEIAERVRSLadvdtilahtmgdvrraEQLLQDAQRARS 1598
Cdd:COG3096   425 ------ARAlcGLPDLTPENAEDYL---------AAFRAKEQQATEEVLEL-----------------EQKLSVADAARR 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1599 R------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:COG3096   473 QfekayelvckiaGEVERSQAwQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1664 RQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGDQYQTVRAlaerKAEGVLAAQARAEQLRDEARG 1743
Cdd:COG3096   553 EELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQL-EQLRARIKELAA----RAPAWLAAQDALERLREQSGE 620

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344 1744 LLQAAQDKLQRLQELegtyEENERELEVK----AAQLDGLEARMRSVLQA 1789
Cdd:COG3096   621 ALADSQEVTAAMQQL----LEREREATVErdelAARKQALESQIERLSQP 666
growth_prot_Scy NF041483
polarized growth protein Scy;
1446-1790 1.39e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 73.32  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1446 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1524
Cdd:NF041483  909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1525 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1591
Cdd:NF041483  984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1592 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1654
Cdd:NF041483 1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1655 SLNsasERARQLHAllEALKlkRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AA 1730
Cdd:NF041483 1136 ELH---ERARRESA--EQMK--SAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAE 1204

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344 1731 QARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1790
Cdd:NF041483 1205 QKKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1576-1790 1.49e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1576 LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtKNTEQTLQQVQERMAGTEQS 1655
Cdd:COG1196   181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKL------RELEAELEELEAELEELEAE 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1656 LNSASERARQLHALLEALKLKRagnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAE 1735
Cdd:COG1196   255 LEELEAELAELEAELEELRLEL-----------EELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLE 319

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1736 QLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
mukB PRK04863
chromosome partition protein MukB;
1449-1778 2.19e-12

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 72.68  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1449 AATADLALGR-ARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFls 1527
Cdd:PRK04863  332 AASDHLNLVQtALRQQEKIERYQAD-------LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADY-- 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 QEGadpdsIEMVATRVLdisipaspeQIQRlASEIAERVRSLADVDTILAHTMGD---------------VRRAEQLLQD 1592
Cdd:PRK04863  403 QQA-----LDVQQTRAI---------QYQQ-AVQALERAKQLCGLPDLTADNAEDwleefqakeqeateeLLSLEQKLSV 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1593 AQRARSR------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLN 1657
Cdd:PRK04863  468 AQAAHSQfeqayqlvrkiaGEVSRSEAwDVARELLRRLreQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1658 SASERARQLHALLEALKLKRAGNSLAASTAEETagsaqsraREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQL 1737
Cdd:PRK04863  548 KNLDDEDELEQLQEELEARLESLSESVSEARER--------RMALRQQLEQLQARIQRLAARAPA----WLAAQDALARL 615

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 564365344 1738 RD-------EARGLLQAAQDKLQRLQELEgtyeENERELEVKAAQLDG 1778
Cdd:PRK04863  616 REqsgeefeDSQDVTEYMQQLLERERELT----VERDELAARKQALDE 659
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1553-1758 3.75e-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: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1553 EQIQRLASEIAERVRSLADVDTILAhtMGDVRRAEQLLQDAQRARSRAEGERQKAEtvqAALEEAQRAQGAAQGAIRGAV 1632
Cdd:COG4913   255 EPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLE---AELERLEARLDALREELDELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1633 VD-TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGN--SLAA--STAEETAGSAQSRAREAEKQLRE 1707
Cdd:COG4913   330 AQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeEFAAlrAEAAALLEALEEELEALEEALAE 409

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344 1708 QVGDQYQTVRALAERKAE-GVLAAQ-----ARAEQLRDEARGLLQAAQDKLQRLQEL 1758
Cdd:COG4913   410 AEAALRDLRRELRELEAEiASLERRksnipARLLALRDALAEALGLDEAELPFVGEL 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1450-1779 3.88e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 71.63  E-value: 3.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1450 ATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALdkaNASRGQVEQANQELRELIQNVKDflsqe 1529
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLAN----- 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1530 gadpdsiemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLqdaqrarSRAEGERQKAET 1609
Cdd:TIGR02168  314 --------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1610 VQAALEEAQRAQgaaqgaiRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAGNSLAAstaee 1689
Cdd:TIGR02168  373 RLEELEEQLETL-------RSKVAQLELQIASLNNEIERL---EARLERLEDRRERLQQEIEELLKKLEEAELKE----- 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1690 tagsAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARglLQAAQDKLQRLQELEGTYEENEREL 1769
Cdd:TIGR02168  438 ----LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ--LQARLDSLERLQENLEGFSEGVKAL 511

                          330
                   ....*....|
gi 564365344  1770 EVKAAQLDGL 1779
Cdd:TIGR02168  512 LKNQSGLSGI 521
mukB PRK04863
chromosome partition protein MukB;
1463-1758 7.32e-12

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 71.14  E-value: 7.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1463 QAELQRALVEGGGilSRVSETRRQAEEAQQRA----------QAALDKANASRGQVEQANQELRE----------LIQNV 1522
Cdd:PRK04863  363 RLEEQNEVVEEAD--EQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNA 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1523 KDFLSQEGADPDSiemVATRVLDIsipaspEQIQRLASEIAER-------VRSLAD-VDTILAHtmgdvRRAEQLLQDA- 1593
Cdd:PRK04863  441 EDWLEEFQAKEQE---ATEELLSL------EQKLSVAQAAHSQfeqayqlVRKIAGeVSRSEAW-----DVARELLRRLr 506

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1594 -QRARS-RAEGERQKAETVQAALEEAQRAQGAAQGAIR--GAVVDTKNTEQTLQQVQE-RMAGTEQSLNSASERARQLHA 1668
Cdd:PRK04863  507 eQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlGKNLDDEDELEQLQEELEaRLESLSESVSEARERRMALRQ 586

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1669 LLEALKLKRAGNslaasTAEETAGSAqsrAREAEKQLREQVGDQY---QTVRALAERKAEGVLAAQ-------ARAEQLR 1738
Cdd:PRK04863  587 QLEQLQARIQRL-----AARAPAWLA---AQDALARLREQSGEEFedsQDVTEYMQQLLERERELTverdelaARKQALD 658

                         330       340
                  ....*....|....*....|
gi 564365344 1739 DEARGLLQAAQDKLQRLQEL 1758
Cdd:PRK04863  659 EEIERLSQPGGSEDPRLNAL 678
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1584-1798 1.32e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 70.09  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1584 RRAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG-------- 1651
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerqleel 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1652 ------TEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAE 1725
Cdd:TIGR02168  322 eaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344  1726 GVLA------AQARAEQLRDEARGLLQAAQDklQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1798
Cdd:TIGR02168  402 IERLearlerLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
growth_prot_Scy NF041483
polarized growth protein Scy;
1458-1776 1.37e-11

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 69.85  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1458 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1529
Cdd:NF041483  158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1530 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1607
Cdd:NF041483  234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 ETVQAALEEAQRAQGAAQGAIRGAvvdtknTEQTLQQVQERMAGTEqSLNSASERARQlHALLEALKL-KRAGNSLAAST 1686
Cdd:NF041483  287 EAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTVA 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1687 AEETAGSAQSRAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDE----ARGLLQAAQD--KLQRLQELE 1759
Cdd:NF041483  359 AEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE-EAERIRReAEAEADRLRGEaadqAEQLKGAAKDdtKEYRAKTVE 437

                         330
                  ....*....|....*..
gi 564365344 1760 gtYEENERELEVKAAQL 1776
Cdd:NF041483  438 --LQEEARRLRGEAEQL 452
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1146-1193 1.73e-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: 1.73e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 564365344  1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1193
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1456-1798 1.93e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 68.00  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1456 LGRARhtqAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELreliQNVKDFLSQegadpds 1535
Cdd:COG4372     8 VGKAR---LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL----EQLEEELEQ------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1536 iemvatrvldisipaSPEQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKaetVQAALE 1615
Cdd:COG4372    71 ---------------ARSELEQLEEELEELNEQLQAAQAELA-------QAQEELESLQEEAEELQEELEE---LQKERQ 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1616 EAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsasERARQLHALLEALKLKRAGNSLaASTAEETAGSAQ 1695
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL----AALEQELQALSEAEAEQALDEL-LKEANRNAEKEE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1696 SRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1775
Cdd:COG4372   201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280

                         330       340
                  ....*....|....*....|...
gi 564365344 1776 LDGLEARMRSVLQAINLQVQIYN 1798
Cdd:COG4372   281 AALELEALEEAALELKLLALLLN 303
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 524-565 2.04e-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: 2.04e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 564365344  524 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 565
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1549-1782 2.17e-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: 69.33  E-value: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1549 PASPEQIQRLASEIAERVRSLADVdtilahtMGDVRRAEQLLQDAQRARSRAEgerQKAETVQAALEEAQRAQGAAQGAI 1628
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSL-------QSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1629 RGAVVDTKNTEQTLQQVQERMAGTEQSLnsaSERARQLHALLEALklkragNSLAASTAEETAGSAQSRAREAEKQLREQ 1708
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARI---EELEEDLHKLEEAL------NDLEARLSHSRIPEIQAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344  1709 VGdqyqTVRALaERKAEGVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELEGTYEENERELEVKAAQLDGLEAR 1782
Cdd:TIGR02169  811 EA----RLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESR 883
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
525-564 2.84e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.02  E-value: 2.84e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 564365344    525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 1463-1784 4.06e-11

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 68.24  E-value: 4.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1463 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1521
Cdd:pfam07111  354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1522 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1592
Cdd:pfam07111  434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1593 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1672
Cdd:pfam07111  508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1673 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1736
Cdd:pfam07111  562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1737 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1784
Cdd:pfam07111  634 rLQDEARK--EEGQRLARRVQEL-----ERDKNLMLATLQQEGLLSRYK 675
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1464-1788 5.93e-11

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: 67.89  E-value: 5.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1464 AELQRALVEgggILSRVSETRRQ---AEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGAD-------- 1532
Cdd:pfam01576  218 TDLQEQIAE---LQAQIAELRAQlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqr 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1533 ---PDSIEMVATRVLDI--SIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRR---------AEQLLQdAQRARS 1598
Cdd:pfam01576  295 rdlGEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelTEQLEQ-AKRNKA 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1599 RAEGERQKAETVQAAL-EEAQRAQGAAQGAIRGavvdTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL---- 1673
Cdd:pfam01576  374 NLEKAKQALESENAELqAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssll 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1674 -----KLKRAGNSLAASTA----------EET----AGSAQSRAREAEKQ-LREQVGDQYQTVRALaERKAEGVLAAQAR 1733
Cdd:pfam01576  450 neaegKNIKLSKDVSSLESqlqdtqellqEETrqklNLSTRLRQLEDERNsLQEQLEEEEEAKRNV-ERQLSTLQAQLSD 528

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1734 AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyeenERELEVKAAQLDGLEaRMRSVLQ 1788
Cdd:pfam01576  529 MKKKLEEDAGTLEALEEGKKRLQrELEAL----TQQLEEKAAAYDKLE-KTKNRLQ 579
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
1448-1797 6.92e-11

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 66.21  E-value: 6.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQR----ALVEGGGIlsrvsetRRQAEEAQQRAQAAldkanasrgqVEQANQELRELIQNV- 1522
Cdd:COG1538    17 RAARARVEAARAQLRQARAGLlpsqELDLGGKR-------RARIEAAKAQAEAA----------EADLRAARLDLAAEVa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1523 KDFLSQEGADpdsiemvatRVLDISipaspEQIQRLASEIAERVRSLADVDTIlahTMGDVRRAEQLLQDAQRARSRAEG 1602
Cdd:COG1538    80 QAYFDLLAAQ---------EQLALA-----EENLALAEELLELARARYEAGLA---SRLDVLQAEAQLAQARAQLAQAEA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1603 ERQKAEtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAserARQLHALLEALKLKRAGN-- 1680
Cdd:COG1538   143 QLAQAR---NALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAA---EAQLEAAEAEIGVARAAFlp 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1681 --SLAASTAEE------------------------TAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARA 1734
Cdd:COG1538   217 slSLSASYGYSssddlfsggsdtwsvglslslplfDGGRNRARVRAAKAQLEQAE-AQYEQTVLQALQEVEDALAALRAA 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344 1735 EQLRDEARGLLQAAQDKLQRLQELegtYEENERE-LEVKAAQLDGLEARMRSV---LQAINLQVQIY 1797
Cdd:COG1538   296 REQLEALEEALEAAEEALELARAR---YRAGLASlLDVLDAQRELLQAQLNLIqarYDYLLALVQLY 359
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 413-470 8.45e-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: 58.52  E-value: 8.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344   413 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 470
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
PTZ00121 PTZ00121
MAEBL; Provisional
 1458-1775 1.07e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1458 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE 1537
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1538 mVATRVLDisipASPEQIQRLASEI--AERVRSLADVDTI-LAHTMGDVRRAEQlLQDAQRARsRAEgERQKAETVQAAL 1614
Cdd:PTZ00121 1168 -EARKAED----AKKAEAARKAEEVrkAEELRKAEDARKAeAARKAEEERKAEE-ARKAEDAK-KAE-AVKKAEEAKKDA 1239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1615 EEAQRAQgaaqgAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSA 1694
Cdd:PTZ00121 1240 EEAKKAE-----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA 1314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1695 QsRAREAEKQlREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQ-DKLQRLQELEGTYEENERELEVKA 1773
Cdd:PTZ00121 1315 K-KADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKKAEEKKK 1392


                  ..
gi 564365344 1774 AQ 1775
Cdd:PTZ00121 1393 AD 1394
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1098-1146 1.11e-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: 58.13  E-value: 1.11e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1146
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
PTZ00121 PTZ00121
MAEBL; Provisional
 1477-1776 1.16e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1477 LSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisiPASPEQIQ 1556
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEE-----------AKKADEAK 1450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1557 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLLQDAQRARsRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVD 1634
Cdd:PTZ00121 1451 KKAEEAkkAEEAKKKAE----------EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA---REAEKQLREQVGD 1711
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeeaKKAEEARIEEVMK 1599

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344 1712 QYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYE--ENERELEVKAAQL 1776
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEE 1666
growth_prot_Scy NF041483
polarized growth protein Scy;
1446-1770 1.56e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 66.39  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1446 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1521
Cdd:NF041483  720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1522 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1600
Cdd:NF041483  787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1601 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1670
Cdd:NF041483  843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1671 --EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1748
Cdd:NF041483  923 tsEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002

                         330       340
                  ....*....|....*....|..
gi 564365344 1749 QDKLQRLQelEGTYEENERELE 1770
Cdd:NF041483 1003 AAEAERLR--TEAREEADRTLD 1022
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1145-1194 2.15e-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: 2.15e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344 1145 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1194
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1478-1784 2.55e-10

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: 65.74  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1478 SRVSETRRQAEE-AQQRAQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-I 1555
Cdd:COG3096   785 KRLEELRAERDElAEQYAKASFDV------------QKLQRLHQAFSQFVGGH--------------LAVAFAPDPEAeL 838

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1556 QRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRAQG--AAQGAi 1628
Cdd:COG3096   839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQEAQAfiQQHGK- 917

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1629 RGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK--LKR--------AGNSLAASTAE--------ET 1690
Cdd:COG3096   918 ALAQLEPL--VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevVQRrphfsyedAVGLLGENSDLneklrarlEQ 995

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1691 AGSAQSRAREAEKQLREQVgDQY---------------QTVRALAERKAE-GVLA---AQARAEQLRDEARGLLQAAQdk 1751
Cdd:COG3096   996 AEEARREAREQLRQAQAQY-SQYnqvlaslkssrdakqQTLQELEQELEElGVQAdaeAEERARIRRDELHEELSQNR-- 1072

                         330       340       350
                  ....*....|....*....|....*....|...
gi 564365344 1752 lQRLQELEGTYEENERElevkaaqLDGLEARMR 1784
Cdd:COG3096  1073 -SRRSQLEKQLTRCEAE-------MDSLQKRLR 1097
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1434-1782 2.59e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.45  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1434 EDGQPRCGGLGCSGAAATADLALGRARHTQAELQRALVEgggilSRVSETRRQAEEAQQRAQAALDKANASRG---QVEQ 1510
Cdd:PRK02224  282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE-----DRDEELRDRLEECRVAAQAHNEEAESLREdadDLEE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1511 ANQELREL-------IQN----VKDFLSQEGADPDSIEMVATRVLDIsiPASPEQIQRLASEIAE---RVRS-LADVDTI 1575
Cdd:PRK02224  357 RAEELREEaaeleseLEEareaVEDRREEIEELEEEIEELRERFGDA--PVDLGNAEDFLEELREerdELRErEAELEAT 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1576 LAHTMGDVRRAEQLLQ---------------------DAQRARSRAEGERQKAETVQAALEEA-QRAQGAAQGAIRgavV 1633
Cdd:PRK02224  435 LRTARERVEEAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERlERAEDLVEAEDR---I 511

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1634 DTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQL-------- 1705
Cdd:PRK02224  512 ERL--EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkerie 589

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1706 -----------REQVGDQYQTVR----ALAE--------------RKAE--------GVLAAQA---RAEQLRDEARGLL 1745
Cdd:PRK02224  590 slerirtllaaIADAEDEIERLRekreALAElnderrerlaekreRKREleaefdeaRIEEAREdkeRAEEYLEQVEEKL 669

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 564365344 1746 QAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEAR 1782
Cdd:PRK02224  670 DELREERDDLQAEIGAVENELEELEELRERREALENR 706
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1448-1789 2.62e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 65.71  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEgggiLSRVSETRRQAEEAQQRAQAALDKANASR-----GQVEQANQELRELIQNV 1522
Cdd:COG4913   286 AQRRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRleqleREIERLERELEERERRR 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1523 KDFlsqegadpdsieMVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEG 1602
Cdd:COG4913   362 ARL------------EALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEA 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1603 ER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRGA------------------- 1631
Cdd:COG4913   427 EIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGFaltllvppehyaaalrwvn 506

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1632 --------------------------------VVDTKN---------------------TEQTLQQV------------- 1645
Cdd:COG4913   507 rlhlrgrlvyervrtglpdperprldpdslagKLDFKPhpfrawleaelgrrfdyvcvdSPEELRRHpraitragqvkgn 586

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1646 -----------------------------QERMAGTEQSLNSASERARQLHALLEAL-KLKRAGNSLAASTAEET-AGSA 1694
Cdd:COG4913   587 gtrhekddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEALEAELDALqERREALQRLAEYSWDEIdVASA 666

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1695 QSRAREAEKQLR---------EQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTY 1762
Cdd:COG4913   667 EREIAELEAELErldassddlAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                         490       500
                  ....*....|....*....|....*..
gi 564365344 1763 EENERELEVKAAQLDGLEARMRSVLQA 1789
Cdd:COG4913   747 LRALLEERFAAALGDAVERELRENLEE 773
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1041-1095 2.90e-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: 56.98  E-value: 2.90e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344  1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 1095
Cdd:pfam00053    1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1448-1749 2.98e-10

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 65.04  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLAlGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDfls 1527
Cdd:COG0840   273 AASAEELA-AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE--- 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 qegadpdsiemVATRVLDISipASPEQIqrlaSEIaervrsladVDTIlahtmGDVrrAEQ--LLqdaqrarsraegerq 1605
Cdd:COG0840   349 -----------TAETIEELG--ESSQEI----GEI---------VDVI-----DDI--AEQtnLL--------------- 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1606 kaetvqaALE---EAQRA--QGaaqgaiRG-AVV-D------------TKNTEQTLQQVQERMAGTEQSLNSASERARQL 1666
Cdd:COG0840   381 -------ALNaaiEAARAgeAG------RGfAVVaDevrklaersaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEG 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1667 HALLEalklkRAGNSLA--ASTAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEAR 1742
Cdd:COG0840   448 VELVE-----EAGEALEeiVEAVEEVSDLIQEIAAASEEQSAgtEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAE 522


                  ....*..
gi 564365344 1743 GLLQAAQ 1749
Cdd:COG0840   523 ELQELVS 529
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1443-1699 3.00e-10

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.40  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1443 LGCSGAAATADlalgRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV 1522
Cdd:COG4942    10 LLALAAAAQAD----AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1523 KDFLSQEGADPDSIE----MVATRVLDISIPASPEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRA 1596
Cdd:COG4942    86 AELEKEIAELRAELEaqkeELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1597 RSRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLK 1676
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

                         250       260
                  ....*....|....*....|...
gi 564365344 1677 ragnslAASTAEETAGSAQSRAR 1699
Cdd:COG4942   236 ------AAAAAERTPAAGFAALK 252
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 834-882 3.04e-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: 56.98  E-value: 3.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344   834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 882
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1590-1785 3.39e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 65.17  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1590 LQDAQRARSRAEGerQKAETVQAALEEAQRAQGAAQGAIRgavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHAL 1669
Cdd:COG4717    51 LEKEADELFKPQG--RKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1670 LEALKLKRAGNSLAASTAEEtagsaQSRAREAEKQLRE--QVGDQYQTVRA-LAERKAEGVLAAQARAEQLRDEARGLLQ 1746
Cdd:COG4717   125 LQLLPLYQELEALEAELAEL-----PERLEELEERLEElrELEEELEELEAeLAELQEELEELLEQLSLATEEELQDLAE 199

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564365344 1747 AAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:COG4717   200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1449-1795 4.13e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 64.94  E-value: 4.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1449 AATADLALGRARHTQAELQRALVEgggilsrvsETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdfLSQ 1528
Cdd:COG4913   271 LAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAELERL---EARLDALREELDELEAQI---RGN 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1529 EGADPDSIE--------------------MVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQ 1588
Cdd:COG4913   336 GGDRLEQLEreierlereleererrrarlEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEA 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1589 LLQDAQRARSRAEGER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRG------ 1630
Cdd:COG4913   413 ALRDLRRELRELEAEIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltll 492

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1631 ----------AVVDTKNTEQTLQ--------QVQERMAGTEQSL--------NSASERARQL------HALLEALK-LKR 1677
Cdd:COG4913   493 vppehyaaalRWVNRLHLRGRLVyervrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAElgrrfdYVCVDSPEeLRR 572

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1678 AGNSLAAS---------------------------------TAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAER 1722
Cdd:COG4913   573 HPRAITRAgqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEalEAELDALQERREALQR 652

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344 1723 KAE------GVLAAQARAEQLRDEaRGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG4913   653 LAEyswdeiDVASAEREIAELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 1462-1781 4.24e-10

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


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 63.93  E-value: 4.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1462 TQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGADPDSIEMVAT 1541
Cdd:pfam19220   39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE--AEAAKEELRIELRDK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1542 RvldisipASPEQIQRLASEIAERVRSLADvdtilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQ 1621
Cdd:pfam19220  117 T-------AQAEALERQLAAETEQNRALEE----------ENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1622 gaaqgairgavvdTKNTEQTLQQVQE---RMAGTEQSLNSASERARQLHAllealklkragnSLAASTAEetagsaqsRA 1698
Cdd:pfam19220  180 -------------QALSEEQAAELAEltrRLAELETQLDATRARLRALEG------------QLAAEQAE--------RE 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1699 ReAEKQLREQVGdQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLqaaQDKLQRLQELEGTYEENERELEVKAAQLDG 1778
Cdd:pfam19220  227 R-AEAQLEEAVE-AHRAERASLRMKLEALTARAAATEQLLAEARNQL---RDRDEAIRAAERRLKEASIERDTLERRLAG 301


                   ...
gi 564365344  1779 LEA 1781
Cdd:pfam19220  302 LEA 304
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1199-1795 4.62e-10

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: 64.99  E-value: 4.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1199 DWDRVVQDLAARTRRLeqwAQELQQTGVLGAFESSFLNLQGKLGMVQAiVAARNTSAASTAKLVEATEGLRHEIgktTER 1278
Cdd:TIGR00618  308 QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTL---TQH 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1279 LTQLEAELTDVQDENFNANHALSGLERD-GLALNLTLRQLDQHLDILkhsnflgaydsirHAHSQSTEAERRANASTFAI 1357
Cdd:TIGR00618  381 IHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLA-------------HAKKQQELQQRYAELCAAAI 447

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1358 pSPVSNSADTRRRAEVLMgAQRENFNRQHLANQQALGRLSTHTHTLSLTGVNELvcgapgdapcATSPCggagcrdedgq 1437
Cdd:TIGR00618  448 -TCTAQCEKLEKIHLQES-AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL----------QEEPC----------- 504

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1438 PRCGGLGCSGAAATADLALG-------RARHTQAELQRALV----EGGGILSRVSETRRQAEEAQQRAQAALDKANASRG 1506
Cdd:TIGR00618  505 PLCGSCIHPNPARQDIDNPGpltrrmqRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1507 QVEQanqeLRELIQNVKDFLSQEGADPDSIEMVATRVLdisIPASPEQ-IQRLASEIAERVRSLADVDTILAhtmgdvRR 1585
Cdd:TIGR00618  585 DIPN----LQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQdLQDVRLHLQQCSQELALKLTALH------AL 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1586 AEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQGAAQGairgavvdtknTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:TIGR00618  652 QLTLTQERVREHALSirVLPKELLASRQLALQKMQSEKEQLTY-----------WKEMLAQCQTLLRELETHIEEYDREF 720

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1664 RQLHALLEALKLKRAGNSlaaSTAEETAGSAQsraREAEKQLREQVGDQyqtvralaERKAEGVLAAQARaeqlrdearg 1743
Cdd:TIGR00618  721 NEIENASSSLGSDLAARE---DALNQSLKELM---HQARTVLKARTEAH--------FNNNEEVTAALQT---------- 776

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1744 llqaaqdkLQRLQELEGTYEENERELEVKAAQLDGLEARMR----SVLQAINLQVQ 1795
Cdd:TIGR00618  777 --------GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCE 824
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1458-1792 4.65e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 65.09  E-value: 4.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1458 RARHTQAELQRALvegGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFLSQegadpd 1534
Cdd:TIGR02169  678 RLRERLEGLKREL---SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSS------ 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1535 siemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAhtmgDVRR--AEQLLQDAQRARSRAEGERQKAEtvqA 1612
Cdd:TIGR02169  749 ---------LEQEIENVKSELKELEARIEELEEDLHKLEEALN----DLEArlSHSRIPEIQAELSKLEEEVSRIE---A 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1613 ALEEAQRAQGAAQgairgavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG 1692
Cdd:TIGR02169  813 RLREIEQKLNRLT-------LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1693 SAQSRAREAEKQLREQvGDQYQTVRALAERKAEGVLAAQARAEQLRDEarglLQAAQDKLQRLQElegtYEENERELEVK 1772
Cdd:TIGR02169  886 DLKKERDELEAQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEE----IPEEELSLEDV 956

                          330       340
                   ....*....|....*....|
gi 564365344  1773 AAQLDGLEARMRSvLQAINL 1792
Cdd:TIGR02169  957 QAELQRVEEEIRA-LEPVNM 975
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1584-1795 4.81e-10

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 64.29  E-value: 4.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1584 RRAEQLLQdaQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAvvdtkntEQtlQQVQERMAGTEQSLNSASERA 1663
Cdd:COG3064     8 KAAEAAAQ--ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQA-------EE--EAREAKAEAEQRAAELAAEAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1664 RQLhalleaLKLKRAGNSLAASTAEETAgsaqSRAREAEKQLREQVGDQYQTVRALAE--RKAEGvlAAQARAEQLRDEA 1741
Cdd:COG3064    77 KKL------AEAEKAAAEAEKKAAAEKA----KAAKEAEAAAAAEKAAAAAEKEKAEEakRKAEE--EAKRKAEEERKAA 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564365344 1742 RGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG3064   145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1582-1779 5.21e-10

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: 61.55  E-value: 5.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1582 DVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT-------------KNTEQTLQQVQER 1648
Cdd:pfam12795   21 DLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleqrlLQTSAQLQELQNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1649 MAGTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETA-GSAQSRAREAEKQLREQVGDQYQ------TVR-A 1718
Cdd:pfam12795  101 LAQLNSQLIELQTRPERAQQQLSEARqrLQQIRNRLNGPAPPGEPlSEAQRWALQAELAALKAQIDMLEqellsnNNRqD 180

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365344  1719 LAERKAEgvlAAQARAEQLRDEARgLLQAAQDKlQRLQELEGTYEENERELEVKAAQLDGL 1779
Cdd:pfam12795  181 LLKARRD---LLTLRIQRLEQQLQ-ALQELLNE-KRLQEAEQAVAQTEQLAEEAAGDHPLV 236
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1146-1190 7.37e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.78  E-value: 7.37e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344   1146 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1190
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 472-523 8.37e-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: 55.82  E-value: 8.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365344  472 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 523
Cdd:cd00055     1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PTZ00121 PTZ00121
MAEBL; Provisional
 1477-1788 8.47e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFL--SQEGADPDSIEMVATRvldisipAS 1551
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEAeaAEEKAEAAEKKKEEAK-------KK 1379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1552 PEQIQRLASEI--AERVRSLADVDTILAHtmgDVRRAEQLLQDAQRARSRAEgERQKAETVQAALEEAQRAQGAAQGAir 1629
Cdd:PTZ00121 1380 ADAAKKKAEEKkkADEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKA-- 1453

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1630 gavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSL-----AASTAEETAGSAQSR----ARE 1700
Cdd:PTZ00121 1454 ----EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaaeAKKKADEAKKAEEAKkadeAKK 1529

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1701 AEKQLREQVGDQYQTVRALAE-RKAEGVLAAQA--------RAEQLRDEA-RGLLQAAQDKLQRLQELEGTYEEN----- 1765
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADElKKAEELKKAEEkkkaeeakKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEEkkmka 1609

                         330       340
                  ....*....|....*....|....*...
gi 564365344 1766 -----ERELEVKAAQLDGLEARMRSVLQ 1788
Cdd:PTZ00121 1610 eeakkAEEAKIKAEELKKAEEEKKKVEQ 1637
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1040-1096 8.87e-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: 55.82  E-value: 8.87e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1040 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 1096
Cdd:cd00055     1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 473-527 1.20e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.44  E-value: 1.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 527
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
PTZ00121 PTZ00121
MAEBL; Provisional
 1479-1772 1.22e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisipaspeqiQRL 1558
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE------------------ARK 1279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1559 ASEI--AERVRSLADvdtilAHTMGDVRRAEQLLQDAQRARS------RAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1630
Cdd:PTZ00121 1280 ADELkkAEEKKKADE-----AKKAEEKKKADEAKKKAEEAKKadeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1631 AVVDTKNTEQTLQQVQERmagTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE-ETAGSAQSRAREAEKQLREQV 1709
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKK 1431

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344 1710 GDQYQTVRALAERKAEgvlAAQARAEQLRdEARGLLQAAQDKlQRLQELEGTYEENERELEVK 1772
Cdd:PTZ00121 1432 KADEAKKKAEEAKKAD---EAKKKAEEAK-KAEEAKKKAEEA-KKADEAKKKAEEAKKADEAK 1489
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1454-1775 1.22e-09

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 62.99  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1454 LALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEQANQELRELIQNVKDFLSQEGADP 1533
Cdd:pfam07888   24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD-------REQWERQRRELESRVAELKEELRQSREKH 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1534 DSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARsRAEGERQKAET---- 1609
Cdd:pfam07888   97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK-KAGAQRKEEEAerkq 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRagNSLAAS--TA 1687
Cdd:pfam07888  176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ--ERLNASerKV 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1688 E------ETAGSAQSRAREAEKQLREQVGDqyqtvraLAERKAEGVLAAQARAEQLRDEARGLLQAAQ---DKLQRL--- 1755
Cdd:pfam07888  254 EglgeelSSMAAQRDRTQAELHQARLQAAQ-------LTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLsae 326

                          330       340
                   ....*....|....*....|....
gi 564365344  1756 -QELEGTYEEN--ERE-LEVKAAQ 1775
Cdd:pfam07888  327 lQRLEERLQEErmEREkLEVELGR 350
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1553-1791 1.35e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.14  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1553 EQIQRLASEIAERVRS------------LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEaqra 1620
Cdd:PRK02224  187 GSLDQLKAQIEEKEEKdlherlngleseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1621 qgaaqgairgavvdtknteqtlqqVQERMAGTEQSLNSASERARQLHALLEALKLKRAGnSLAASTAEETAGSAQSRARE 1700
Cdd:PRK02224  263 ------------------------LRETIAETEREREELAEEVRDLRERLEELEEERDD-LLAEAGLDDADAEAVEARRE 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1701 AEKQLREQVGDQYQTVRALAERKAEgvlaaqaRAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLE 1780
Cdd:PRK02224  318 ELEDRDEELRDRLEECRVAAQAHNE-------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390

                         250
                  ....*....|.
gi 564365344 1781 ARMRSVLQAIN 1791
Cdd:PRK02224  391 EEIEELRERFG 401
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
1447-1796 1.38e-09

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


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 63.00  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1447 GAAATADLALGRARHTQAELQRALVegggILSRVSETRRQAEEAQ--QRA------QAALDKANASRGQVEQANQELREL 1518
Cdd:COG5278    23 VLGVLSYLSLNRLREASEWVEHTYE----VLRALEELLSALLDAEtgQRGylltgdESFLEPYEEARAEIDELLAELRSL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1519 IQNvkdflsqegadpdsiemvatrvldisipaSPEQIQRLAS--EIAERVRSLADvDTILAHTMGDVRRAEQLLQ----- 1591
Cdd:COG5278    99 TAD-----------------------------NPEQQARLDEleALIDQWLAELE-QVIALRRAGGLEAALALVRsgegk 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1592 ---DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1668
Cdd:COG5278   149 almDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1669 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1748
Cdd:COG5278   229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 564365344 1749 QDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG5278   309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1455-1789 1.70e-09

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: 62.89  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1455 ALGRARHTQA-ELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQV--------------EQANQELRELI 1519
Cdd:pfam01576  629 AEAREKETRAlSLARALEE-------ALEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskralEQQVEEMKTQL 701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1520 QNVKDFLsQEGADpdsiemvATRVLDISIPASPEQIQRLAS---EIAE-RVRSLADvdtilahtmgDVRRAEQLLQDAQR 1595
Cdd:pfam01576  702 EELEDEL-QATED-------AKLRLEVNMQALKAQFERDLQardEQGEeKRRQLVK----------QVRELEAELEDERK 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1596 ARSRAEGERQKAET-------------------------VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQ------- 1643
Cdd:pfam01576  764 QRAQAVAAKKKLELdlkeleaqidaankgreeavkqlkkLQAQMKDLQRELEEARASRDEILAQSKESEKKLKnleaell 843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1644 QVQERMAgteqslnsASERARQlHALLEALKLKragNSLAASTAEETAGSAQSRAREAE-KQLREQVGDQYQTVRALAER 1722
Cdd:pfam01576  844 QLQEDLA--------ASERARR-QAQQERDELA---DEIASGASGKSALQDEKRRLEARiAQLEEELEEEQSNTELLNDR 911

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1723 KAEGV---------LAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGT----YEENERELEVKAAQL-DGLEARMRSVL 1787
Cdd:pfam01576  912 LRKSTlqveqltteLAAERSTSQKSESARQQLERQNKELKaKLQEMEGTvkskFKSSIAALEAKIAQLeEQLEQESRERQ 991


                   ..
gi 564365344  1788 QA 1789
Cdd:pfam01576  992 AA 993
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1584-1792 2.01e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 61.70  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1584 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERA 1663
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1664 RQLHALLEAL--KLKRAGNS------LAASTAEETAGSAQ-----SRAREAE-KQLREQVGDQYQTVRALAERKAE---- 1725
Cdd:COG4942   100 EAQKEELAELlrALYRLGRQpplallLSPEDFLDAVRRLQylkylAPARREQaEELRADLAELAALRAELEAERAEleal 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344 1726 --GVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELegtyEENERELEVKAAQLDGLEARMRSVLQAINL 1792
Cdd:COG4942   180 laELEEERAALEALKAERQKLLARLEKELaelaAELAEL----QQEAEELEALIARLEAEAAAAAERTPAAGF 248
growth_prot_Scy NF041483
polarized growth protein Scy;
1556-1778 2.10e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 62.92  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1556 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1618
Cdd:NF041483  130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1619 RAQGAAQGAIRGAVVDTknteqtlqqvqERMagteqsLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSR 1697
Cdd:NF041483  204 SARAEAEAILRRARKDA-----------ERL------LNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQR 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1698 AREAEKQLREqvgdqyqtvralaerkaegvlaAQARAEQLRDEARgllQAAQdklQRLQELEGTYEENERELEVKAAQLD 1777
Cdd:NF041483  267 MQEAEEALRE----------------------ARAEAEKVVAEAK---EAAA---KQLASAESANEQRTRTAKEEIARLV 318


                  .
gi 564365344 1778 G 1778
Cdd:NF041483  319 G 319
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 412-471 2.23e-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: 54.67  E-value: 2.23e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  412 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 471
Cdd:cd00055     1 PCDCNGHGSL-SGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1200-1755 2.39e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.09  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1200 WDRVVQDLAARTRRLEQWAQELQQTgvlgafESSFLNLQGKLGMVQAIVAARntsaastaKLVEATEGLRHEIGKTTERL 1279
Cdd:COG4717    83 AEEKEEEYAELQEELEELEEELEEL------EAELEELREELEKLEKLLQLL--------PLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1280 TQLEAELTDVQDenfnanhalsgLERDGLALNLTLRQLDQHLDILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAIps 1359
Cdd:COG4717   149 EELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1360 pvsnsADTRRRAEVLMgAQRENFNRQHLAnQQALGRLSTHTHTLSLTGVnelvcgapgdapcatspcggagcrdedgqpR 1439
Cdd:COG4717   216 -----EEAQEELEELE-EELEQLENELEA-AALEERLKEARLLLLIAAA------------------------------L 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1440 CGGLGCSGAAATADLALGRArhtqaelqrALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasrgqveqANQELREli 1519
Cdd:COG4717   259 LALLGLGGSLLSLILTIAGV---------LFLVLGLLALLFLLLAREKASLGKEAEELQALP---------ALEELEE-- 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1520 QNVKDFLSQEGADPD-SIEMVATRVLDIsipaspEQIQRLASEIAERVRSL------ADVDTILAHtmGDVRRAEQLLQD 1592
Cdd:COG4717   319 EELEELLAALGLPPDlSPEELLELLDRI------EELQELLREAEELEEELqleeleQEIAALLAE--AGVEDEEELRAA 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1593 AQRARSRAEgERQKAETVQAALEEAQRAQGAAQgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEA 1672
Cdd:COG4717   391 LEQAEEYQE-LKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1673 LklkragnslaastaeETAGSAqSRAREAEKQLREQvgdqyqtVRALAERKAEGVLAAQArAEQLRDEAR-----GLLQA 1747
Cdd:COG4717   465 L---------------EEDGEL-AELLQELEELKAE-------LRELAEEWAALKLALEL-LEEAREEYReerlpPVLER 520


                  ....*...
gi 564365344 1748 AQDKLQRL 1755
Cdd:COG4717   521 ASEYFSRL 528
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
 1732-1801 2.80e-09

C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.


Pssm-ID: 411974 [Multi-domain]  Cd Length: 71  Bit Score: 55.14  E-value: 2.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1732 ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1801
Cdd:cd22303     2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 525-564 3.09e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.28  E-value: 3.09e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564365344   525 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 564
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1098-1143 3.67e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.85  E-value: 3.67e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365344   1098 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1143
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1553-1791 3.70e-09

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: 62.11  E-value: 3.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1553 EQIQRLASEIA---ERVRSLADVDTILAHTMGDV----RRAEQLLQDAQRARSRAEGE---------------------- 1603
Cdd:pfam01576  159 ERISEFTSNLAeeeEKAKSLSKLKNKHEAMISDLeerlKKEEKGRQELEKAKRKLEGEstdlqeqiaelqaqiaelraql 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1604 RQKAETVQAAL---EEAQRAQGAAQGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK--LKRA 1678
Cdd:pfam01576  239 AKKEEELQAALarlEEETAQKNNALKKIREL-------EAQISELQEDLESERAARNKAEKQRRDLGEELEALKteLEDT 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1679 GNSLAAS----TAEETAGSAQSRAREAEKQLRE-QVGD----QYQTVRALAE-----RKAEGVL--AAQA----RAEqLR 1738
Cdd:pfam01576  312 LDTTAAQqelrSKREQEVTELKKALEEETRSHEaQLQEmrqkHTQALEELTEqleqaKRNKANLekAKQAleseNAE-LQ 390

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1739 DEARGLLQAAQDKLQR-------LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:pfam01576  391 AELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1097-1144 4.21e-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: 53.90  E-value: 4.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564365344 1097 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1144
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1553-1769 5.92e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.47  E-value: 5.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1553 EQIQRLASEIAERVRSLADVDTILA------HTMGDVRRAEQLLQD----------AQRARSRAEGERQKAE-------T 1609
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEaleaelDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDassddlaA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ-LHALLEALKlkragnslaastae 1688
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERF-------------- 755

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1689 etagsAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARA-EQLRDEARGL---LQAAQDKLQRLQELEGT--- 1761
Cdd:COG4913   756 -----AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLdadLESLPEYLALLDRLEEDglp 830


                  ....*....
gi 564365344 1762 -YEENEREL 1769
Cdd:COG4913   831 eYEERFKEL 839
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1041-1095 8.26e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 8.26e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   1041 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 1095
Cdd:smart00180    1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 1592-1757 8.45e-09

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: 56.80  E-value: 8.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1592 DAQRARSRAEGERQKAETVQAALEeaqrAQGAAQGAIRG--AVVD-----TKNTEQTLQQVQERMAGTEQSLNSASERAR 1664
Cdd:pfam05335   22 DAQAAAAEAAARQVKNQLADKALQ----AAKAAEAALAGkqQIVEqleqeLREAEAVVQEESASLQQSQANANAAQRAAQ 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1665 QLHALLEALKlkragNSLAAstAEETAGSAQSRAREAEKQLREQvgdqyqtvRALAErkaegvlAAQARAEQLRDEargl 1744
Cdd:pfam05335   98 QAQQQLEALT-----AALKA--AQANLENAEQVAAGAQQELAEK--------TQLLE-------AAKKRVERLQRQ---- 151

                          170
                   ....*....|...
gi 564365344  1745 LQAAQDKLQRLQE 1757
Cdd:pfam05335  152 LAEARADLEKTKK 164
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 989-1031 1.21e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 52.36  E-value: 1.21e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564365344   989 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1550-1777 1.82e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 57.24  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1550 ASPEQIQRLaseiaervRSLADVDTILAHTMgdvRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgair 1629
Cdd:COG1579     1 AMPEDLRAL--------LDLQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1630 gavvdtKNTEQTLQQVQERMAGTEQSLNSASErARQLHAL---LEALKLKRAgnslaastaeetagsaqsrarEAEKQLR 1706
Cdd:COG1579    62 ------KRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRIS---------------------DLEDEIL 113

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1707 EqvgdqyqtvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLD 1777
Cdd:COG1579   114 E------------LMERIEELEEELAELEAELAELEAELEEKKAELDeELAELEAELEELEAEREELAAKIP 173
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1477-1797 2.59e-08

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 58.51  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1477 LSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELRELIQNVKdflsqegadpdsiemvatrvldisipasPEQIQ 1556
Cdd:COG3064    18 LEQAEAEKRAAAEAEQKAKE---EAEEERLAELEAKRQAEEEAREAK----------------------------AEAEQ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1557 RLASEIAERVRSLADvdtilahtmgdvrrAEQLLQDAQRarsRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdTK 1636
Cdd:COG3064    67 RAAELAAEAAKKLAE--------------AEKAAAEAEK---KAAAEKAKAAKEAEAAAAAEKAAAAAE---------KE 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1637 NTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG--SAQSRAREAEKQLREQVGDQYQ 1714
Cdd:COG3064   121 KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAgaAAALVAAAAAAVEAADTAAAAA 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1715 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQV 1794
Cdd:COG3064   201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280


                  ...
gi 564365344 1795 QIY 1797
Cdd:COG3064   281 VAA 283
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1555-1777 2.84e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1555 IQRLASEIAERVRSLADVDTILahtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG--AV 1632
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1633 VDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaasTAEETAGSAQSRAREAEKQLREQvgdQ 1712
Cdd:COG4717   125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-----------ELEAELAELQEELEELLEQLSLA---T 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1713 YQTVRALAERKAEgvlaAQARAEQLRDEarglLQAAQDKLQRLQElEGTYEENERELEVKAAQLD 1777
Cdd:COG4717   191 EEELQDLAEELEE----LQQRLAELEEE----LEEAQEELEELEE-ELEQLENELEAAALEERLK 246
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 833-875 3.35e-08

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: 51.20  E-value: 3.35e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564365344  833 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1485-1743 3.43e-08

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: 56.16  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1485 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNvkdfLSQEGADPDSiemvatrvldisipASPEQIQRLaseiae 1564
Cdd:pfam12795   23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAEA--------------APKEILASL------ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1565 rvrSLADVDTILAHTMGDVRRAEQLLQDAQrarSRAEGERQKAETVQAALEEAQRaqgaAQGAIRGAVVDTKNTEQTLQQ 1644
Cdd:pfam12795   79 ---SLEELEQRLLQTSAQLQELQNQLAQLN---SQLIELQTRPERAQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1645 VQERMAGTEQSLnsaserarqLHALLEALKLKRAGNS----LAASTAEETAgsAQSRAREAEKQ-LREQVGDQYQtvrAL 1719
Cdd:pfam12795  149 AQRWALQAELAA---------LKAQIDMLEQELLSNNnrqdLLKARRDLLT--LRIQRLEQQLQaLQELLNEKRL---QE 214

                          250       260
                   ....*....|....*....|....
gi 564365344  1720 AERkaegvlaAQARAEQLRDEARG 1743
Cdd:pfam12795  215 AEQ-------AVAQTEQLAEEAAG 231
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1591-1791 3.63e-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: 57.85  E-value: 3.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1591 QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALL 1670
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1671 EALKLKRAgnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQD 1750
Cdd:COG4942   100 EAQKEELA----------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAE 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 564365344 1751 KLQRLQELEGTYEENERELevkaAQLDGLEARMRSVLQAIN 1791
Cdd:COG4942   169 LEAERAELEALLAELEEER----AALEALKAERQKLLARLE 205
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1592-1790 3.77e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 57.53  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1592 DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLhalle 1671
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1672 ALKLKRAGNS-------LAASTAEETAGSAQSRAREAEKQlREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEargl 1744
Cdd:COG3883    92 ARALYRSGGSvsyldvlLGSESFSDFLDRLSALSKIADAD-ADLLEELKADKAELEAKKAE-LEAKLAELEALKAE---- 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 564365344 1745 LQAAQDKLQRLQElegtyeenereleVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3883   166 LEAAKAELEAQQA-------------EQEALLAQLSAEEAAAEAQL 198
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 1555-1756 3.81e-08

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 57.05  E-value: 3.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1555 IQRLASEIAERVR---SLADVDTILAHTMGDVRRAEqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGA 1631
Cdd:pfam00529   31 VTRVLVKEGDRVKagdVLFQLDPTDYQAALDSAEAQ--LAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1632 VVDTKNTEQTLQQVQERMAGTEqslNSASERARQLHALLEalklkrAGNSLAastaeetagSAQSRAREAEKQLREQVGD 1711
Cdd:pfam00529  109 QAAVKAAQAQLAQAQIDLARRR---VLAPIGGISRESLVT------AGALVA---------QAQANLLATVAQLDQIYVQ 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 564365344  1712 QYQTVRALAERKAEGVLAAQARAEQLRDEarglLQAAQDKLQRLQ 1756
Cdd:pfam00529  171 ITQSAAENQAEVRSELSGAQLQIAEAEAE----LKLAKLDLERTE 211
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1486-1758 3.84e-08

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 58.53  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1486 QAE--EAQQRAQAALDKANASRGQVEQANQ---ELRELIQNVKDFLSQEGADPDSIEmvatrvLDISIPASPEQIQRLAS 1560
Cdd:PRK10929   43 QAEivEALQSALNWLEERKGSLERAKQYQQvidNFPKLSAELRQQLNNERDEPRSVP------PNMSTDALEQEILQVSS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1561 EIAE----------RVRSLADVDTILAhtmgdvrraeQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1630
Cdd:PRK10929  117 QLLEksrqaqqeqdRAREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALK 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1631 AVVDtkntEQTLQQV-----QE--RMagteqSLNSASERARQLHALLEALKlkragNSLAASTAEETagsaqSRAREAEK 1703
Cdd:PRK10929  187 ALVD----ELELAQLsannrQElaRL-----RSELAKKRSQQLDAYLQALR-----NQLNSQRQREA-----ERALESTE 247

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344 1704 QLREQVGD-------QYQTVRALAErkaegVLAAQA-RAEQLRDEARgllQAAQDKLQRLQEL 1758
Cdd:PRK10929  248 LLAEQSGDlpksivaQFKINRELSQ-----ALNQQAqRMDLIASQQR---QAASQTLQVRQAL 302
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1627-1786 3.97e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1627 AIRGAVVDTKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnslaastaEETAGSAQSRAREAEKQLR 1706
Cdd:COG4913   239 RAHEALEDAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAELEELRAELA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1707 EqvgdqyqtvraLAERKAEgvlaAQARAEQLRDEARGLLQA-AQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:COG4913   306 R-----------LEAELER----LEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370


                  .
gi 564365344 1786 V 1786
Cdd:COG4913   371 L 371
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1455-1684 5.16e-08

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 55.22  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1455 ALGRARHTQAEL--QRALVEgggilSRVSETRRQAEEAQQRAQAALDKANasrgqveqanqelreliqnvkdflsqegad 1532
Cdd:COG1842    38 DLVEARQALAQViaNQKRLE-----RQLEELEAEAEKWEEKARLALEKGR------------------------------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1533 pdsiEMVATRVLdisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKAETVqA 1612
Cdd:COG1842    83 ----EDLAREAL--------ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEL----------KAKKDTL-K 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1613 ALEEAQRAQGAAQGAIRGavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRAGNS-LAA 1684
Cdd:COG1842   140 ARAKAAKAQEKVNEALSG--IDSDDATSALERMEEKIEEMEARAEAAAELAAGdsLDDELAELEADSEVEDeLAA 212
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1582-1788 5.34e-08

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: 56.78  E-value: 5.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1582 DVRRAEQLLQDAQRARSRAEGERQKAETV-QAALEEAQRAQGAAQGAirgavvdtknTEQTLQQVQERMAGTEQSLNSAS 1660
Cdd:TIGR02794   61 PAAKKEQERQKKLEQQAEEAEKQRAAEQArQKELEQRAAAEKAAKQA----------EQAAKQAEEKQKQAEEAKAKQAA 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1661 ERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQyqtvrALAERKAEGVlAAQARAEQLRDE 1740
Cdd:TIGR02794  131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK-----AEAEAKAKAE-EAKAKAEAAKAK 204

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 564365344  1741 ARgllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ 1788
Cdd:TIGR02794  205 AA---AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
834-875 5.42e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.77  E-value: 5.42e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 564365344    834 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 875
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
growth_prot_Scy NF041483
polarized growth protein Scy;
1554-1770 5.94e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.91  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1554 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1627
Cdd:NF041483   44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1628 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRArEAEK---Q 1704
Cdd:NF041483  121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARA-EAERlaeE 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1705 LREQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQEL 1758
Cdd:NF041483  194 ARQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEA 270

                         250
                  ....*....|..
gi 564365344 1759 EGTYEENERELE 1770
Cdd:NF041483  271 EEALREARAEAE 282
growth_prot_Scy NF041483
polarized growth protein Scy;
1459-1789 6.04e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.91  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1459 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1533
Cdd:NF041483  252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1534 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1598
Cdd:NF041483  326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1599 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1650
Cdd:NF041483  401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1651 GTEQSLNSA--------------SERARQlHALLEALKLKRagnslaasTAEETAgsaqSRAREAEKQLREQVGDQYQTV 1716
Cdd:NF041483  481 TAEELLTKAkadadelrstataeSERVRT-EAIERATTLRR--------QAEETL----ERTRAEAERLRAEAEEQAEEV 547

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1717 RALAERKA-----EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSv 1786
Cdd:NF041483  548 RAAAERAArelreETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT- 626


                  ...
gi 564365344 1787 LQA 1789
Cdd:NF041483  627 LQA 629
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1543-1775 6.76e-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: 56.70  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1543 VLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQG 1622
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1623 AAQGAIRGAVVDTKNTEQTLQQVQERMAGTE--------QSLNSASERARQLHALLEALKlkRAGNSLAASTAEETAgsA 1694
Cdd:COG4942    90 KEIAELRAELEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARR--EQAEELRADLAELAA--L 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1695 QSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAA 1774
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAE----RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241


                  .
gi 564365344 1775 Q 1775
Cdd:COG4942   242 R 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1488-1790 7.84e-08

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: 57.77  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1488 EEAQQRAQAALDKANASRGQVEQANQELRELIQNVkDFLSQEGADPDSIEMVATRVLDI-------SIPASPEQIQRLAS 1560
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYegyellkEKEALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1561 EIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQrARSRAEGERQKAEtVQAALEEAQRAQGAAQGAIRGAvvdtkntEQ 1640
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEK-------ER 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1641 TLQQVQERMAGTEQSLNSASERARQLhallealklkragnslaastaeetagsaqSRAREAEKQLREQVGDQY---QTVR 1717
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEEL-----------------------------EREIEEERKRRDKLTEEYaelKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1718 ALAERKAEGVLAAQARA-----------EQLRDEaRGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETrdelkdyreklEKLKRE-INELKRELDRLQeELQRLSEELADLNAAIAGIEAKINELEEEKED 445


                   ....*
gi 564365344  1786 VLQAI 1790
Cdd:TIGR02169  446 KALEI 450
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
413-470 8.67e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 8.67e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344    413 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 470
Cdd:smart00180    1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 989-1035 9.11e-08

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: 50.05  E-value: 9.11e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 564365344  989 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 1035
Cdd:cd00055     2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
473-516 9.95e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.00  E-value: 9.95e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 564365344    473 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 516
Cdd:smart00180    1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1446-1786 9.95e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 57.36  E-value: 9.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1446 SGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASrgqveqanqelrELIQNVKDF 1525
Cdd:PRK02224  397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP------------ECGQPVEGS 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1526 LSQEGADPD--SIEMVATRVLDISipaspEQIQRLASEIaERVRSLADVDTILAHTMGDVRRAEQLLQD----AQRARSR 1599
Cdd:PRK02224  465 PHVETIEEDreRVEELEAELEDLE-----EEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAErretIEEKRER 538

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1600 AEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERArQLHALLEALKLKRAG 1679
Cdd:PRK02224  539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA 617

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1680 -------------------NSLAASTAEETAGSAQSRAREAEKQLrEQVGDQyqtVRALAERKAE------GVLAAQARA 1734
Cdd:PRK02224  618 laelnderrerlaekrerkRELEAEFDEARIEEAREDKERAEEYL-EQVEEK---LDELREERDDlqaeigAVENELEEL 693

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1735 EQLRDEarglLQAAQDKLQRLQELegtYEENErELEVKAAQLDGlEARMRSV 1786
Cdd:PRK02224  694 EELRER----REALENRVEALEAL---YDEAE-ELESMYGDLRA-ELRQRNV 736
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1585-1785 1.51e-07

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: 54.26  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1585 RAEQLLQDAQRARSRAEGERQKAETVQAAL--------EEAQRAQG--------------AAQGAIRGavvdTKNTEQTL 1642
Cdd:pfam00261   12 EAEERLKEAMKKLEEAEKRAEKAEAEVAALnrriqlleEELERTEErlaealekleeaekAADESERG----RKVLENRA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1643 QQVQERMAGTEQSLNSASERARQLHALLE--ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLReQVGDQYQTVRALA 1720
Cdd:pfam00261   88 LKDEEKMEILEAQLKEAKEIAEEADRKYEevARKLVVVEGDL--ERAEERAELAESKIVELEEELK-VVGNNLKSLEASE 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344  1721 ErkaegvlAAQARAEQLRDEARgLLQAaqdklqRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:pfam00261  165 E-------KASEREDKYEEQIR-FLTE------KLKEAETRAEFAERSVQKLEKEVDRLEDELEA 215
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1452-1781 2.83e-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: 55.95  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1452 ADLALGRARHTQAELQRALVEG--GGILSRVSETRRQAEEAQQR---AQAALDKANASRGQVEQAN-------------- 1512
Cdd:pfam01576  391 AELRTLQQAKQDSEHKRKKLEGqlQELQARLSESERQRAELAEKlskLQSELESVSSLLNEAEGKNiklskdvsslesql 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1513 QELRELIQ-------NVKDFLSQEGADPDSI------EMVATRVLDisipaspEQIQRLASEIAERVRSLADVDTILaht 1579
Cdd:pfam01576  471 QDTQELLQeetrqklNLSTRLRQLEDERNSLqeqleeEEEAKRNVE-------RQLSTLQAQLSDMKKKLEEDAGTL--- 540

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1580 mgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQ---TLQQVQ---ERMAGTE 1653
Cdd:pfam01576  541 -------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsNLEKKQkkfDQMLAEE 613

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1654 QSLNS--ASERARQlhallEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQY-------QTVRAL--AER 1722
Cdd:pfam01576  614 KAISAryAEERDRA-----EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHELerSKR 688

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365344  1723 KAEGVLAA-QARAEQLRDEarglLQAAQDKLQRLQ------------ELEGTYEENE--RELEVKaaQLDGLEA 1781
Cdd:pfam01576  689 ALEQQVEEmKTQLEELEDE----LQATEDAKLRLEvnmqalkaqferDLQARDEQGEekRRQLVK--QVRELEA 756
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1514-1796 3.46e-07

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: 55.61  E-value: 3.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1514 ELRELIQNVKDFLSQEGADpdsIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGD---------VR 1584
Cdd:pfam12128  143 EYRSIIQNDRTLLGRERVE---LRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDdgvvppksrLN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1585 RAE--------QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSL 1656
Cdd:pfam12128  220 RQQvehwirdiQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1657 NSASERARQ-LHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARAE 1735
Cdd:pfam12128  300 KEKRDELNGeLSAADAAVAKDRS----ELEALEDQHGAFLDADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVT 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344  1736 QLRDEARGLL-QAAQDKLQRL-QELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:pfam12128  375 AKYNRRRSKIkEQNNRDIAGIkDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNE 437
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1464-1776 3.52e-07

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: 55.61  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1464 AELQRALVEGGGILSRVSETRRQaeEAQQRAQAALDKANAS-RGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATR 1542
Cdd:pfam12128  256 AELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGA 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1543 VLDISIP---ASPEQIQRLASEIAERVRSLAdvdtILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETvqaaleEAQR 1619
Cdd:pfam12128  334 FLDADIEtaaADQEQLPSWQSELENLEERLK----ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL------AKIR 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1620 aqgaaQGAIRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKragnsLAASTAEETAGSAQSRAR 1699
Cdd:pfam12128  404 -----EARDRQLAVAEDDLQALESELREQL---EAGKLEFNEEEYRLKSRLGELKLR-----LNQATATPELLLQLENFD 470

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344  1700 EAEKQLREQVGDQYQTVRALAErkaegvlaAQARAEQLRDEArglLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1776
Cdd:pfam12128  471 ERIERAREEQEAANAEVERLQS--------ELRQARKRRDQA---SEALRQASRRLEERQSALDELELQLFPQAGTL 536
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 880-927 3.87e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 3.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564365344   880 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 927
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1534-1791 3.94e-07

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 55.36  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1534 DSIEMVATRVLDIS------IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDA-------------- 1593
Cdd:TIGR00618  176 DQYTQLALMEFAKKkslhgkAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShayltqkreaqeeq 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1594 ---QRARSRAEGERQKAETVQAALEEAQRA-----QGAAQGAIRGAVVDT-KNTEQTLQQVQERMA-------------- 1650
Cdd:TIGR00618  256 lkkQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIeQQAQRIHTELQSKMRsrakllmkraahvk 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1651 ---------GTEQSLNSASERAR--------------QLHALLEALK--------LKRAGNSLAASTAEETAGSAQSRAR 1699
Cdd:TIGR00618  336 qqssieeqrRLLQTLHSQEIHIRdahevatsireiscQQHTLTQHIHtlqqqkttLTQKLQSLCKELDILQREQATIDTR 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1700 --------------EAEKQLREQVGDQYQ-----TVRALAERKAEGVLAAQA---RAEQLRDEARGLLQAAQDK------ 1751
Cdd:TIGR00618  416 tsafrdlqgqlahaKKQQELQQRYAELCAaaitcTAQCEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKavvlar 495

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 564365344  1752 LQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:TIGR00618  496 LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1484-1735 3.99e-07

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 54.60  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1484 RRQAEEAQQRAQAALdkanASRGQVEQANQELreliQNVKDFLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIA 1563
Cdd:PRK07735   12 KEAARRAKEEARKRL----VAKHGAEISKLEE----ENREKEKALPKNDDMTIE---------------EAKRRAAAAAK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1564 ERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-EGERQKAETVQAALEE--AQRAQGAAQGAIRGAVVDTKNTEQ 1640
Cdd:PRK07735   69 AKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAaALAKQKREGTEEVTEEekAAAKAKAAAAAKAKAAALAKQKRE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1641 TLQQVQERMAGTEQSL--NSASERARQLHALLEALKLKRAGNSLAASTAEE-------TAGSAQSRAREAEKQLREQV-- 1709
Cdd:PRK07735  149 GTEEVTEEEEETDKEKakAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEkakakakAAAAAKAKAAALAKQKASQGng 228

                         250       260
                  ....*....|....*....|....*...
gi 564365344 1710 --GDQYQTVRALAERKAEGVLAAQARAE 1735
Cdd:PRK07735  229 dsGDEDAKAKAIAAAKAKAAAAARAKTK 256
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1590-1750 4.09e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.43  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1590 LQDAQRARSRAEGERQKAETVQAalEEAQRAQGAAQgairgavvdtknteQTLQQV-QERMAGTEQslNSASERARQLHA 1668
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQA--EELQQKQAAEQ--------------ERLKQLeKERLAAQEQ--KKQAEEAAKQAA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1669 L----LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARAE-QLRDEARG 1743
Cdd:PRK09510  129 LkqkqAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA-EAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEA 207


                  ....*..
gi 564365344 1744 LLQAAQD 1750
Cdd:PRK09510  208 KKKAAAE 214
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1636-1796 4.44e-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: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAA-----STAEETAGSAQSRAREAEKQLREQ 1708
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerRIAALARRIRAleqelAALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1709 VGDQYQTVRALAER----------KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDG 1778
Cdd:COG4942   103 KEELAELLRALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                         170
                  ....*....|....*...
gi 564365344 1779 LEARMRSVLQAINLQVQI 1796
Cdd:COG4942   183 LEEERAALEALKAERQKL 200
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1534-1721 4.88e-07

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: 51.50  E-value: 4.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1534 DSIEMVATRVLDISipaspEQIQRLASEIAERV-RSLADVDTILAHTMGDVR-RAEQLLQDAQrarsraegerqkaETVQ 1611
Cdd:pfam01442    4 DSLDELSTYAEELQ-----EQLGPVAQELVDRLeKETEALRERLQKDLEEVRaKLEPYLEELQ-------------AKLG 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1612 AALEEAQRAQGAAQGAIRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASERAR-QLHALLEALKLK-----RAGNSLAAS 1685
Cdd:pfam01442   66 QNVEELRQRLEPYTEELRKRL--NADAEELQEKLAPYGEELRERLEQNVDALRaRLAPYAEELRQKlaerlEELKESLAP 143

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 564365344  1686 TAEEtagsAQSRAREAEKQLREQVGDQYQTVRALAE 1721
Cdd:pfam01442  144 YAEE----VQAQLSQRLQELREKLEPQAEDLREKLD 175
PTZ00121 PTZ00121
MAEBL; Provisional
 1479-1775 5.11e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1479 RVSETRRQAEEA---QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVAtrvldisipaspEQI 1555
Cdd:PTZ00121 1558 KKAEEKKKAEEAkkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------------EEL 1625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1556 QRlaseiAERVRSlaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGaaqgairgavvDT 1635
Cdd:PTZ00121 1626 KK-----AEEEKK--KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-----------DE 1687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSA-QSRAREAEKQLREQVGDQYQ 1714
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeEAKKDEEEKKKIAHLKKEEE 1767

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344 1715 TVRALAERKAEGVLAAQARAE--QLRDEARGLLQAAQDKLQRLQE--LEGT-YEENERELEVKAAQ 1775
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIEggKEGNlVINDSKEMEDSAIK 1833
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 879-924 5.64e-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: 47.73  E-value: 5.64e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 564365344  879 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 924
Cdd:cd00055     1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
 1733-1800 7.45e-07

C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 48.12  E-value: 7.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1733 RAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1800
Cdd:cd22301     3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1477-1790 1.19e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.59  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1477 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQ-ANQELRELiqnvkDFLSQEGADPDSiemvatrvldisipaspEQI 1555
Cdd:pfam17380  308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERmAMEREREL-----ERIRQEERKREL-----------------ERI 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1556 --QRLASEIaERVRSLADVDtilahtMGDVRRAEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQgaaQGAIRGa 1631
Cdd:pfam17380  366 rqEEIAMEI-SRMRELERLQ------MERQQKNERVRQELEAARKVKilEEERQRKIQQQKVEMEQIRAE---QEEARQ- 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1632 vVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETagsaQSRAREAEKQLREQVGD 1711
Cdd:pfam17380  435 -REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQAMI 509

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1712 QYQTVRALAERKAEGVLAAQARAEQLR--DEARGLLQAAQDKLQRLQELEGTYEENERelevkaaqLDGLEaRMRSVLQA 1789
Cdd:pfam17380  510 EEERKRKLLEKEMEERQKAIYEEERRReaEEERRKQQEMEERRRIQEQMRKATEERSR--------LEAME-REREMMRQ 580


                   .
gi 564365344  1790 I 1790
Cdd:pfam17380  581 I 581
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1453-1665 1.20e-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: 51.46  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1453 DLALGRARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegad 1532
Cdd:COG1579    16 DSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1533 pdsiemvatrvldISipaSPEQIQRLASEIAervrSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEGERQKAETVQA 1612
Cdd:COG1579    85 -------------VR---NNKEYEALQKEIE----SLK-------------RRISDLEDEILELMERIEELEEELAELEA 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564365344 1613 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGT-EQSLNSASERARQ 1665
Cdd:COG1579   132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYERIRK 185
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1545-1775 1.58e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.52  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1545 DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE--AQRA-- 1620
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelGERAra 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1621 ---QGAAQGAIrGAVVDTKNTEQTLQQVQermagteqSLNSASERARQLhalLEALKLKRAGNSLAASTAEETAGSAQSR 1697
Cdd:COG3883    95 lyrSGGSVSYL-DVLLGSESFSDFLDRLS--------ALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1698 AREAEKQLRE---QVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAA 1774
Cdd:COG3883   163 KAELEAAKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242


                  .
gi 564365344 1775 Q 1775
Cdd:COG3883   243 A 243
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1586-1790 1.61e-06

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: 53.42  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1586 AEQLLQDAQRARsrAEgERQKAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERARQ 1665
Cdd:COG3096   290 LRRELFGARRQL--AE-EQYRLVEMARELEELSARESDLEQDYQAAS-DHLNLVQTALRQQEKIERYQEDLEELTERLEE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1666 LHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQL--REQVGDQYQTvRALAERKAegvLAAQARAEQLRDEARG 1743
Cdd:COG3096   366 QEEVVEEAAEQLA-------EAEARLEAAEEEVDSLKSQLadYQQALDVQQT-RAIQYQQA---VQALEKARALCGLPDL 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564365344 1744 LLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3096   435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV 481
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1452-1683 1.67e-06

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: 50.83  E-value: 1.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1452 ADLALGRARHTQAEL---QRALVEgggilsRVSETRRQAEEAQQRAQAALDKanasrgqveqANQEL-RELIQnvkdfls 1527
Cdd:pfam04012   34 MQSELVKARQALAQTiarQKQLER------RLEQQTEQAKKLEEKAQAALTK----------GNEELaREALA------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1528 qegadpdsiemvatrvldisipaspeQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKA 1607
Cdd:pfam04012   91 --------------------------EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL----------KAKK 134

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344  1608 ETVQAAlEEAQRAQGAAQGAIRGAvvDTKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALLEALKLKRAGNSLA 1683
Cdd:pfam04012  135 NLLKAR-LKAAKAQEAVQTSLGSL--STSSATDSFERIEEKIEEREARADAAAELAsaVDLDAKLEQAGIQMEVSEDV 209
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1566-1781 2.00e-06

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: 51.26  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1566 VRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAAL----EEAQRAQGAAQGAIRGAvvdtknteqt 1641
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELsslaQETEELQKKATQTLAKA---------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1642 lQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLaasTAEETAGSAQSRA-REAEKQLREQVGDQYQTVRALA 1720
Cdd:pfam06008   71 -QQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMlAEAQRMLGEIRSRDFGTQLQNA 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1721 E---RKAEGVLAA------------QARAEQLRD----------EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1775
Cdd:pfam06008  147 EaelKAAQDLLSRiqtwfqspqeenKALANALRDslaeyeaklsDLRELLREAAAKTRDANRLNLANQANLREFQRKKEE 226


                   ....*.
gi 564365344  1776 LDGLEA 1781
Cdd:pfam06008  227 VSEQKN 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1514-1791 2.19e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1514 ELRELIQNVKDFLSQEgadpdsiemvatrvldisipaspEQIQRLASEIAERvrsladvdtiLAHTMGDVRRAEQLLQDA 1593
Cdd:PRK03918  173 EIKRRIERLEKFIKRT-----------------------ENIEELIKEKEKE----------LEEVLREINEISSELPEL 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1594 QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ------SLNSASERARQLH 1667
Cdd:PRK03918  220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLS 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1668 ALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEK---QLREQVGDQYQTVRALAE-----RKAEGVLAAQARAEQLRD 1739
Cdd:PRK03918  300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEEleerhELYEEAKAKKEELERLKK 379

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564365344 1740 EARGLlqaAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:PRK03918  380 RLTGL---TPEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
GAF COG2203
GAF domain [Signal transduction mechanisms];
1449-1796 2.31e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 52.50  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1449 AATADLALGRARHTQAELQRALvegggilsrvsETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1528
Cdd:COG2203   337 ADQAAIAIERARLYEALEAALA-----------ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1529 EGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAE 1608
Cdd:COG2203   406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1609 TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE 1688
Cdd:COG2203   486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1689 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERE 1768
Cdd:COG2203   566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645

                         330       340
                  ....*....|....*....|....*...
gi 564365344 1769 LEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG2203   646 LALALASLVLLRALLATELDLILDSSLL 673
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 1485-1795 2.32e-06

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 52.38  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1485 RQAEEAQQRAQ--AALDKANASRGQVEQANQELRELiqnvKDFLSQEG--ADPDSIEMvatRVLDISIPASPEQIQRLAS 1560
Cdd:pfam05622  160 RNAEYMQRTLQleEELKKANALRGQLETYKRQVQEL----HGKLSEESkkADKLEFEY---KKLEEKLEALQKEKERLII 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1561 E---------------IAERVRSLADVDTILAHTMGDVRRAE-----------QLLQDAQRARSRAEG-ERQKAETVQAA 1613
Cdd:pfam05622  233 ErdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEimpaeirekliRLQHENKMLRLGQEGsYRERLTELQQL 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1614 LEEAQRAQGAAQGAIRgavvdtKNTEQ--TLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAASTA-- 1687
Cdd:pfam05622  313 LEDANRRKNELETQNR------LANQRilELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHleKLHEAQSELQKKKEqi 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1688 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAA-QARAEQLR-DEARGLLQAAQDKLQRLQELE 1759
Cdd:pfam05622  387 EELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERykkyveKAKSVIKTlDPKQNPASpPEIQALKNQLLEKDKKIEHLE 466

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1760 GTYEEN--ERELEVK-----------AAQLDGLEARmrsvLQAINLQVQ 1795
Cdd:pfam05622  467 RDFEKSklQREQEEKlivtawynmgmALHRKAIEER----LAGLSSPGQ 511
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1448-1796 2.52e-06

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 52.33  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1527
Cdd:COG0840    16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 QEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1607
Cdd:COG0840    96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1608 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ-------SLNSASER---ARQLHALLEALK--- 1674
Cdd:COG0840   176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgdltvriDVDSKDEIgqlADAFNRMIENLRelv 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1675 --LKRAGNSLAAStAEETAGSAQSRAREAEKQlREQVgdqyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKL 1752
Cdd:COG0840   256 gqVRESAEQVASA-SEELAASAEELAAGAEEQ-AASL----EETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 564365344 1753 QRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG0840   330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDI 373
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1479-1796 2.53e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 52.35  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKdfLSQEGADPDSIEMVATRVLDISipASPEQIQRL 1558
Cdd:COG3064    17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK--AEAEQRAAELAAEAAKKLAEAE--KAAAEAEKK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1559 ASEIAERVRSLADVDTIL--AHTMGDVRRAEQLLQDAQR-ARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:COG3064    93 AAAEKAKAAKEAEAAAAAekAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHAllEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQT 1715
Cdd:COG3064   173 RAAAGAAAALVAAAAAAVEAADTAAAAAAALAA--AAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1716 VRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG3064   251 AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVR 330


                  .
gi 564365344 1796 I 1796
Cdd:COG3064   331 G 331
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 929-987 2.93e-06

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: 45.81  E-value: 2.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344  929 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 987
Cdd:cd00055     1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
989-1031 2.99e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 45.77  E-value: 2.99e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 564365344    989 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 1031
Cdd:smart00180    1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1464-1767 3.19e-06

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: 51.95  E-value: 3.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1464 AELQrALVEGggILSRVSETRRQAEEAQQRAQAALDKANAS----RGQVEQANQE---LRELIQNVKDFLSQEGADPDSI 1536
Cdd:pfam05701  264 AELA-AYMES--KLKEEADGEGNEKKTSTSIQAALASAKKEleevKANIEKAKDEvncLRVAAASLRSELEKEKAELASL 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1537 ---EMVATrvldISIPASPEQIQRLASEIA---ERVRSLADVDTILAHTMGDVRR-AEQLLQDAQRAR-----SRAEGER 1604
Cdd:pfam05701  341 rqrEGMAS----IAVSSLEAELNRTKSEIAlvqAKEKEAREKMVELPKQLQQAAQeAEEAKSLAQAAReelrkAKEEAEQ 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1605 QKAE--TVQAALEEAQRAQGAAQGAIRGAVVdtknteqTLQQVQERMAGTEQSLNSASERARQLhALLEALKL-KRagns 1681
Cdd:pfam05701  417 AKAAasTVESRLEAVLKEIEAAKASEKLALA-------AIKALQESESSAESTNQEDSPRGVTL-SLEEYYELsKR---- 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1682 laASTAEETAG----SAQSR---AREAEKQLREQVGDQYqtvRALAERKaEGVLAAQARAEQLRDEargllqaaqdKLQR 1754
Cdd:pfam05701  485 --AHEAEELANkrvaEAVSQieeAKESELRSLEKLEEVN---REMEERK-EALKIALEKAEKAKEG----------KLAA 548

                          330
                   ....*....|...
gi 564365344  1755 LQELEGTYEENER 1767
Cdd:pfam05701  549 EQELRKWRAEHEQ 561
mukB PRK04863
chromosome partition protein MukB;
1612-1785 3.80e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1612 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAS--------ERARQLHALLEALK-----LKRA 1678
Cdd:PRK04863  837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetlaDRVEEIREQLDEAEeakrfVQQH 916

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1679 GNSL------AASTAEETAGSAQSRAR--EAEKQLReqvgDQYQTVRALAE----------RKAEGVLAA---------- 1730
Cdd:PRK04863  917 GNALaqlepiVSVLQSDPEQFEQLKQDyqQAQQTQR----DAKQQAFALTEvvqrrahfsyEDAAEMLAKnsdlneklrq 992

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1731 -QARAEQLRDEARGLLQAAQDKL----QRLQELEGTYE-------ENERELEVKAAQLD-GLEARMRS 1785
Cdd:PRK04863  993 rLEQAEQERTRAREQLRQAQAQLaqynQVLASLKSSYDakrqmlqELKQELQDLGVPADsGAEERARA 1060
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
1504-1706 3.98e-06

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


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 51.00  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1504 SRGQVEQANQELreliqNVKDFLSQEGADP-------DSIE--------MVATR------VLDISIPA-SPEQIQRLA-- 1559
Cdd:COG3524    84 SRDAVERLDAEL-----DLRAHYSRPGIDPlsrldpdASIEdlykyyrrRVKVEydstsgIITLEVRAfDPEDAQAIAea 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1560 ----SE-----IAERVRSladvDTIlAHTMGDVRRAEQLLQDAQRA----RSR---------AEG--------ERQKAET 1609
Cdd:COG3524   159 llaeSEelvnqLSERARE----DAV-RFAEEEVERAEERLRDAREAllafRNRngildpeatAEAllqliatlEGQLAEL 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1610 vQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG--TEQSLNSASERarqlhalLEALKLKRAgnslaasTA 1687
Cdd:COG3524   234 -EAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGasGGDSLASLLAE-------YERLELERE-------FA 298

                         250       260
                  ....*....|....*....|...
gi 564365344 1688 EETAGSAQS---RAR-EAEKQLR 1706
Cdd:COG3524   299 EKAYTSALAaleQARiEAARQQR 321
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1455-1755 4.08e-06

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.43  E-value: 4.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1455 ALGRARHTQAELQRALVEGGGILSRVSETR----RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEG 1530
Cdd:pfam07888   88 ELRQSREKHEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1531 ADPDSiemvaTRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQR--------------A 1596
Cdd:pfam07888  168 EEEAE-----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleelrsL 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1597 RSRAEGERQKAETVQAALEE--AQRAQGAA---QGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERAR-QLHALL 1670
Cdd:pfam07888  243 QERLNASERKVEGLGEELSSmaAQRDRTQAelhQARLQAA-------QLTLQLADASLALREGRARWAQERETlQQSAEA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1671 EALKLKRAgnSLAASTAEETAGSAQSRAREAEKQL-REQVGDQYQ---TVRALAERKAeGVLAAQARAEQLRDEARGLLQ 1746
Cdd:pfam07888  316 DKDRIEKL--SAELQRLEERLQEERMEREKLEVELgREKDCNRVQlseSRRELQELKA-SLRVAQKEKEQLQAEKQELLE 392


                   ....*....
gi 564365344  1747 AAQDKLQRL 1755
Cdd:pfam07888  393 YIRQLEQRL 401
PTZ00121 PTZ00121
MAEBL; Provisional
 1477-1772 4.44e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1477 LSRVSETRRQAEEAQQRAQAAlDKANASRGQVEQAnQELRELIQNVKDFLSQEGADPDSIEmvATRVLDISIPAspEQIQ 1556
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKKKA--EEAK 1496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1557 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLlQDAQRARsRAEgERQKAETVQAAlEEAQRAQGAAQGAIRGAVVD 1634
Cdd:PTZ00121 1497 KKADEAkkAAEAKKKAD----------EAKKAEEA-KKADEAK-KAE-EAKKADEAKKA-EEKKKADELKKAEELKKAEE 1562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1635 TKNTEQTLQQVQER-MAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQY 1713
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKnMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344 1714 QTVRALAE--RKAE---GVLAAQ--ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVK 1772
Cdd:PTZ00121 1643 AEEKKKAEelKKAEeenKIKAAEeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
mukB PRK04863
chromosome partition protein MukB;
1479-1789 4.49e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.88  E-value: 4.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1479 RVSETRRQAEEAQQR-AQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-IQ 1556
Cdd:PRK04863  787 RIEQLRAEREELAERyATLSFDV------------QKLQRLHQAFSRFIGSH--------------LAVAFEADPEAeLR 840

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1557 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRA------QGAAQ 1625
Cdd:PRK04863  841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladETLADRVEEIREQLDEAEEAkrfvqqHGNAL 920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1626 GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLE---ALKLKRAGNSLAASTA--------EETAGSA 1694
Cdd:PRK04863  921 AQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrraHFSYEDAAEMLAKNSDlneklrqrLEQAEQE 1000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1695 QSRAREAEKQLREQVgDQYQTVRA------------LAERKAE----GVLA---AQARAEQLRDEARGLLQAAQdklQRL 1755
Cdd:PRK04863 1001 RTRAREQLRQAQAQL-AQYNQVLAslkssydakrqmLQELKQElqdlGVPAdsgAEERARARRDELHARLSANR---SRR 1076

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 564365344 1756 QELEGTYEENERELE-----VKAAQLDGLEARmRSVLQA 1789
Cdd:PRK04863 1077 NQLEKQLTFCEAEMDnltkkLRKLERDYHEMR-EQVVNA 1114
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1585-1797 4.71e-06

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: 50.69  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1585 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgAIRGAVV-----DTKNTEQTLQQVQERMAGTEQSlNSA 1659
Cdd:pfam13868   61 EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQERE-QMDEIVEriqeeDQAEAEEKLEKQRQLREEIDEF-NEE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1660 SERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQ-----LREQvgdQYQTVRALAERkaEGVLAAQARA 1734
Cdd:pfam13868  139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEreiarLRAQ---QEKAQDEKAER--DELRAKLYQE 213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1735 EQLRDEARGLLQAAQDKLQRLQELEGTYEE---NERELEVKAAQLDglEARMRSVLQAINLQVQIY 1797
Cdd:pfam13868  214 EQERKERQKEREEAEKKARQRQELQQAREEqieLKERRLAEEAERE--EEEFERMLRKQAEDEEIE 277
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 1491-1785 6.75e-06

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.98  E-value: 6.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1491 QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE----M--VATR---VLDISIPASPEQIQ---RL 1558
Cdd:pfam10174  337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRdlkdMldVKERkinVLQKKIENLQEQLRdkdKQ 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1559 ASEIAERVRSL----ADVDTILAhTMgdvrraEQLLQDAQRARSRAEGERQKAEtvQAALEEAQRAQGaaqgairgavvD 1634
Cdd:pfam10174  417 LAGLKERVKSLqtdsSNTDTALT-TL------EEALSEKERIIERLKEQRERED--RERLEELESLKK-----------E 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1635 TKNTEQTLQQVQERMAGTEQSLNSASERARQL--HALLEALKLKRAGNSLAASTAEETAGSAQS-RAREAEKQLR--EQV 1709
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLkKAHNAEEAVRtnPEI 556

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1710 GDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:pfam10174  557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
DUF4175 pfam13779
Domain of unknown function (DUF4175);
1432-1758 9.34e-06

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 50.76  E-value: 9.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1432 RDEDGQprcgglgcSGAAATADLALGRARHTQaELQRALVEgggilsrvsetrrqaeeaqQRAQAALDKANASRgqveqA 1511
Cdd:pfam13779  379 TDGAGQ--------EGRSEPLEIRLPERRFSD-PLARALIE-------------------QRRRLALDRENRPR-----V 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1512 NQELRELIqnvkdfLSQEGADPDSIEMVATRVL--DISIPASPEQIQRLAS---EIAERVRSladvdtilahtmGDVRRA 1586
Cdd:pfam13779  426 ARALDALT------LAPEEFGPDAGVYLGLRSAlaRLELARSDEALDEVADllwELALRIED------------GDLSDA 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1587 EQLLQDAQRARSRA------EGERQK-AETVQAALEE-----AQRAQGAAQGAIRGAVVDTK-NTEQTLQQVQERMAgtE 1653
Cdd:pfam13779  488 ERRLRAAQERLSEAlergasDEEIAKlMQELREALDDymqalAEQAQQNPQDLQQPDDPNAQeMTQQDLQRMLDRIE--E 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1654 QSLNSASERARQlhaLLEAlkLKRAGNSLAASTAEETAGSAQSRAREAEKQLRE-------------------------Q 1708
Cdd:pfam13779  566 LARSGRRAEAQQ---MLSQ--LQQMLENLQAGQPQQQQQQGQSEMQQAMDELGDllreqqqlldetfrqlqqqggqqqgQ 640

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 564365344  1709 VGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQEL 1758
Cdd:pfam13779  641 PGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEEL 690
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1550-1794 9.98e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1550 ASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtVQAALEEAQRaqgaAQGAIR 1629
Cdd:COG4717    85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE-LPERLEELEE----RLEELR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1630 GAVVDTKNTEQTLQQVQERMA--------GTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETAGSAQSRAR 1699
Cdd:COG4717   160 ELEEELEELEAELAELQEELEelleqlslATEEELQDLAEELEELQQRLAELEeeLEEAQEELEELEEELEQLENELEAA 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1700 EAEKQLREQ----------------VGDQYQTVRALAE----------------RKAEGVLAAQARAEQLRDEARGLLQA 1747
Cdd:COG4717   240 ALEERLKEArlllliaaallallglGGSLLSLILTIAGvlflvlgllallflllAREKASLGKEAEELQALPALEELEEE 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 564365344 1748 AQDKLQRLQELEGTYEENE-RELEVKAAQLDGLEARMRSVLQAINLQV 1794
Cdd:COG4717   320 ELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEE 367
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1584-1784 1.02e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.92  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1584 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgAIRGAvvdtknteQTL-QQVQERmagteqslnsasER 1662
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE-----RKRYR--------QELeEQIEER------------EQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1663 ARQL---HALLEALKLKRAgnsLAASTAEETAgsAQSRAREAEKQLREQVgDQYQtvRALAERKaegvlaaQARAEQLRD 1739
Cdd:pfam13868   88 KRQEeyeEKLQEREQMDEI---VERIQEEDQA--EAEEKLEKQRQLREEI-DEFN--EEQAEWK-------ELEKEEERE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 564365344  1740 EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:pfam13868  153 EDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1482-1796 1.03e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 50.28  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1482 ETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvKDFLSQEGADPDSIEMVATRvldisipaspEQIQRLASE 1561
Cdd:pfam07888   10 EEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQ--AQEAANRQREKEKERYKRDR----------EQWERQRRE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1562 IAERVrslADVDTILAHTMGDVRRAEQLLQDAQRARsraegerqkaetvqAALEEAQRAQGAAQGAirgAVVDTKNTEQT 1641
Cdd:pfam07888   78 LESRV---AELKEELRQSREKHEELEEKYKELSASS--------------EELSEEKDALLAQRAA---HEARIRELEED 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1642 LQQVQERMAGTEQSLNSASERARQLHALL-------EALKLKragnsLAASTAEETAGSAQ---SRAREAEK-----QLR 1706
Cdd:pfam07888  138 IKTLTQRVLERETELERMKERAKKAGAQRkeeeaerKQLQAK-----LQQTEEELRSLSKEfqeLRNSLAQRdtqvlQLQ 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1707 EQVGDQYQTVRALAERKAEgvlaaqarAEQLRDEARGLlqaaQDklqRLQELEGTYEENERELEVKAAQLDGLEARM-RS 1785
Cdd:pfam07888  213 DTITTLTQKLTTAHRKEAE--------NEALLEELRSL----QE---RLNASERKVEGLGEELSSMAAQRDRTQAELhQA 277

                          330
                   ....*....|.
gi 564365344  1786 VLQAINLQVQI 1796
Cdd:pfam07888  278 RLQAAQLTLQL 288
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1480-1684 1.05e-05

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: 48.95  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1480 VSETRRQAEEAQQ-RAQAALDKANASR--GQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDisipASPEQIQ 1556
Cdd:pfam06008   53 AQETEELQKKATQtLAKAQQVNAESERtlGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLS----RMLAEAQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1557 RLASEIAERvrslaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQK-AETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:pfam06008  129 RMLGEIRSR-----DFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAlANALRDSLAEYEAKLSDLRELLREAAAKT 203

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 564365344  1636 KNTEQTLQQVQERMagteQSLNSASERARQLHALLEALkLKRAGNSLAA 1684
Cdd:pfam06008  204 RDANRLNLANQANL----REFQRKKEEVSEQKNQLEET-LKTARDSLDA 247
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1639-1791 1.14e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1639 EQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGD--QYQtv 1716
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEEQL-GNVRNnkEYE-- 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1717 rALaERKAEgvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:COG1579    93 -AL-QKEIE---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1484-1784 1.14e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1484 RRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNVKDFLSQegadpdsiemvatrvldisipaspeQIQRLASEI 1562
Cdd:pfam13868  118 AEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDERILEYLKE-------------------------KAEREEERE 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1563 AERVRSLADVDtilahtmgdvRRAEQLLQDAQRARS-RAEGERQKAETVQAALEEAQRAqgaaqgairgavvdtknteqt 1641
Cdd:pfam13868  173 AEREEIEEEKE----------REIARLRAQQEKAQDeKAERDELRAKLYQEEQERKERQ--------------------- 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1642 lqqvQERMAgteqslnsASERARQLHALLEALKLKRAGNSLaastaeetagsAQSRAREAEKQLREQVgdqyqtVRALAE 1721
Cdd:pfam13868  222 ----KEREE--------AEKKARQRQELQQAREEQIELKER-----------RLAEEAEREEEEFERM------LRKQAE 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344  1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDK-LQRLQELEGTYEENERELEVKAAQLDGL-EARMR 1784
Cdd:pfam13868  273 DEEIEQEEAEKRRMKRLEHRRELEKQIEEReEQRAAEREEELEEGERLREEEAERRERIeEERQK 337
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 350-402 1.54e-05

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: 43.88  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  350 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 402
Cdd:cd00055     2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1476-1747 1.67e-05

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: 48.44  E-value: 1.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1476 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1553
Cdd:smart00283    2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1554 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRArsraeGERQK-----AETVQaAL 1614
Cdd:smart00283   75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARA-----GEAGRgfavvADEVR-KL 138

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1615 eeAQRAQGAAqgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTaEETAGSA 1694
Cdd:smart00283  139 --AERSAESA-----------KEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE--ETGDALEEIVDSV-EEIADLV 202

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   1695 QSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1747
Cdd:smart00283  203 QEIAAATDEQAAgsEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 350-401 1.67e-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: 43.50  E-value: 1.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344   350 CECNGH---SHSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 401
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
PRK15374 PRK15374
type III secretion system needle tip complex protein SipB;
1589-1782 1.82e-05

type III secretion system needle tip complex protein SipB;


Pssm-ID: 185272 [Multi-domain]  Cd Length: 593  Bit Score: 49.58  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1589 LLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEqSLNSASerarQLHA 1668
Cdd:PRK15374   13 YTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDAARE-KLSSEG----QLTL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1669 LLEALKLKRAGNSLAASTAEETAGSAQsraREAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRDEARGLL 1745
Cdd:PRK15374   88 LLGKLMTLLGDVSLSQLESRLAVWQAM---IESQKEMGIQVSKEFQTALGEAQeatDLYEASIKKTDTAKSVYDAAEKKL 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564365344 1746 QAAQDKLQRLQELEGTYEENERELEVKAAqlDGLEAR 1782
Cdd:PRK15374  165 TQAQNKLQSLDPADPGYAQAEAAVEQAGK--EATEAK 199
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1452-1673 1.83e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1452 ADLALGRARHTQAELQ---RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1528
Cdd:COG4913   659 DEIDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1529 --EGADPDSIEMVATRVLDISIPASPEQIQRlasEIAERVRSLAdvdtilahtmGDVRRAEQLLQDAQRA-RSRAEGERQ 1605
Cdd:COG4913   739 aeDLARLELRALLEERFAAALGDAVERELRE---NLEERIDALR----------ARLNRAEEELERAMRAfNREWPAETA 805

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344 1606 KAETVQAALEEAQR------AQG--AAQGAIRGAVvdTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEAL 1673
Cdd:COG4913   806 DLDADLESLPEYLAlldrleEDGlpEYEERFKELL--NENSIEFVADLLSKL---RRAIREIKERIDPLNDSLKRI 876
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 956-986 1.90e-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: 43.50  E-value: 1.90e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 564365344   956 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 986
Cdd:pfam00053   19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 286-338 1.97e-05

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: 43.50  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  286 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 338
Cdd:cd00055     2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1479-1795 2.13e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.27  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1479 RVSETRRQAEE-AQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQR 1557
Cdd:COG3064   121 KAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1558 LASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKN 1637
Cdd:COG3064   201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1638 TEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAG-------NSLAASTAEETAGSAQSRAREAEK------Q 1704
Cdd:COG3064   281 VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAaagalvvRGGGAASLEAALSLLAAGAAAAAAgagalaT 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1705 LREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:COG3064   361 GALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKL 440

                         330
                  ....*....|.
gi 564365344 1785 SVLQAINLQVQ 1795
Cdd:COG3064   441 VADLAGGLVGI 451
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1477-1795 2.21e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.57  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1477 LSRVSETRRQA-------EEAQQRAQAA-LDKANASRGQVEQANQELRELIQNVKDFLSQEgadpdsiemvatrvldisi 1548
Cdd:COG3096   245 LEAIRVTQSDRdlfkhliTEATNYVAADyMRHANERRELSERALELRRELFGARRQLAEEQ------------------- 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1549 paspEQIQRLASEIAERVRSLADVDTilahtmgDVRRAE---QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQ 1625
Cdd:COG3096   306 ----YRLVEMARELEELSARESDLEQ-------DYQAASdhlNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAA 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1626 GAIRGAVVDTKNTEQT----------LQQ---VQERMAGTEQSLNSASERARQLHAlLEALKLKRAGNSLAASTAEE--- 1689
Cdd:COG3096   375 EQLAEAEARLEAAEEEvdslksqladYQQaldVQQTRAIQYQQAVQALEKARALCG-LPDLTPENAEDYLAAFRAKEqqa 453

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1690 -----------------------------------TAGSAQSRAREAEKQLREQ--VGDQYQTVRA-LAErkAEGVLAAQ 1731
Cdd:COG3096   454 teevleleqklsvadaarrqfekayelvckiagevERSQAWQTARELLRRYRSQqaLAQRLQQLRAqLAE--LEQRLRQQ 531

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344 1732 ARAEQLRDEargLLQAAQDKLQRLQELEGTYEENERELEVKAAQL-DGLEARM--RSVLQAINLQVQ 1795
Cdd:COG3096   532 QNAERLLEE---FCQRIGQQLDAAEELEELLAELEAQLEELEEQAaEAVEQRSelRQQLEQLRARIK 595
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1475-1765 2.35e-05

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: 47.79  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1475 GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegadpdsiemvATRVLdisipASPEQ 1554
Cdd:pfam06008    9 GALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK-----------ATQTL-----AKAQQ 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1555 IQRLASEIAERVRSLADvdtilahtmgdvrRAEQLLQDAQRARSRAEGERQKAE-----TVQAALEEAQRAQGAaqgaIR 1629
Cdd:pfam06008   73 VNAESERTLGHAKELAE-------------AIKNLIDNIKEINEKVATLGENDFalpssDLSRMLAEAQRMLGE----IR 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1630 GavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEETAgsAQSRAREAEKQLREqv 1709
Cdd:pfam06008  136 S-----RDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA-NALRDSLAEYEAKLSD--LRELLREAAAKTRD-- 205

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1710 gdqyqtvralaerkAEGVLAAQARAeqlrdearglLQAAQDKLQRLQELEGTYEEN 1765
Cdd:pfam06008  206 --------------ANRLNLANQAN----------LREFQRKKEEVSEQKNQLEET 237
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 1477-1647 2.50e-05

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 46.24  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1477 LSRVSETR-RQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvatrvldisipaSPEQI 1555
Cdd:pfam07321    4 LLRVKHLReDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAW--------------------------------RPQEE 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1556 QRLASEIAERVRSLADVDTILaHTMGDVRRAEQLL-QDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAIRGAVVD 1634
Cdd:pfam07321   52 QRLYAEIQGKLVLLKELEKVK-QQVALLRENEADLeKQVAEARQQLEAEREALRQARQALAEARRAV--EKFAELVRLVQ 128

                          170
                   ....*....|...
gi 564365344  1635 TKntEQTLQQVQE 1647
Cdd:pfam07321  129 AE--ELRQQERQE 139
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1607-1791 2.66e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1607 AETVQAALEEAQRAQGAAQGAIRGavvdtKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnSLAAST 1686
Cdd:COG4717    40 LAFIRAMLLERLEKEADELFKPQG-----RKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEE--ELEELE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1687 AEETAgsAQSRAREAEKQLreQVGDQYQTVRALAERKAEGvlaaQARAEQLRDEarglLQAAQDKLQRLQELEGTYEENE 1766
Cdd:COG4717   109 AELEE--LREELEKLEKLL--QLLPLYQELEALEAELAEL----PERLEELEER----LEELRELEEELEELEAELAELQ 176

                         170       180
                  ....*....|....*....|....*.
gi 564365344 1767 RELEVKAAQLD-GLEARMRSVLQAIN 1791
Cdd:COG4717   177 EELEELLEQLSlATEEELQDLAEELE 202
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1554-1796 2.77e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1554 QIQRLAS-EIAERVRSLADVDTILAHTMGDVRRAEQLLQDA----QRARSR-----AEGE-RQKA-ETVQAALEEAQRAQ 1621
Cdd:COG3206    86 QIEILKSrPVLERVVDKLNLDEDPLGEEASREAAIERLRKNltvePVKGSNvieisYTSPdPELAaAVANALAEAYLEQN 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1622 GAAQgairgavvdTKNTEQTLQQVQERMAGTEQSLNSAsERArqlhalLEALKLKRAGNSLaastaEETAGSAQSRAREA 1701
Cdd:COG3206   166 LELR---------REEARKALEFLEEQLPELRKELEEA-EAA------LEEFRQKNGLVDL-----SEEAKLLLQQLSEL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1702 EKQLREqvgdqyqtvrALAERKAegvlaAQARAEQLRDEARGLLQAA---------QDKLQRLQELEGTYEENEREL--- 1769
Cdd:COG3206   225 ESQLAE----------ARAELAE-----AEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYtpn 289

                         250       260       270
                  ....*....|....*....|....*....|.
gi 564365344 1770 --EVKA--AQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG3206   290 hpDVIAlrAQIAALRAQLQQEAQRILASLEA 320
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1587-1776 2.78e-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: 47.37  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1587 EQLLQDAQRARSRAEGERQKAETVQAALEeaQRAqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSASER-ARq 1665
Cdd:pfam04012   28 EQAIRDMQSELVKARQALAQTIARQKQLE--RRL------------------EQQTEQAKKLEEKAQAALTKGNEElAR- 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1666 lhallEAL-KLKRAGNSLAASTAEetagsaQSRAREAEKQLREQVGDQYQTVRALaERKAEGVLA--AQARAEQLRDEAR 1742
Cdd:pfam04012   87 -----EALaEKKSLEKQAEALETQ------LAQQRSAVEQLRKQLAALETKIQQL-KAKKNLLKArlKAAKAQEAVQTSL 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 564365344  1743 GLLQA--AQDKLQRLQ----ELEGTYE-----ENERELEVKAAQL 1776
Cdd:pfam04012  155 GSLSTssATDSFERIEekieEREARADaaaelASAVDLDAKLEQA 199
HBM pfam16591
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ...
 1564-1785 3.21e-05

Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 435446 [Multi-domain]  Cd Length: 246  Bit Score: 47.39  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1564 ERVRSLADVDTILaHTMGDVRRAEqlLQDAQrarsrAEGERQKAETVQAALEE--AQRAQGAAQ----------GAIRGA 1631
Cdd:pfam16591    3 ERSDRMTDISQLN-DTLTDLRIAR--LQYML-----SNGDATAAQAVQKKLDElkQQLQQLKTTftspenvrllQEQLQL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1632 VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRAREAEKQLREQV-G 1710
Cdd:pfam16591   75 IQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEA----EVLQTPEADSRRAAQYQAISELKRQVQMARYQVrG 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344  1711 DQYQTVRALAERKAEGVLAAQARAEQLRDeargllQAAQDKLQRLQELE---GTYEENERELEVKAAQLDGLEARMRS 1785
Cdd:pfam16591  151 YTFTPNEDSEQAAYQQLDAALASLDQLRQ------ALAGDPGAALQQLTsalQGYRDALDTFKAAVAAIEQARQEMTS 222
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1554-1718 3.41e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.23  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1554 QIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGErqkAETVQAALEEAQRAQG---------AA 1624
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGnvrnnkeyeAL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1625 QGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgNSLAASTAEETAgsAQSRAREAEKQ 1704
Cdd:COG1579    95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEE--LEAEREELAAK 171

                         170
                  ....*....|....
gi 564365344 1705 LREQVGDQYQTVRA 1718
Cdd:COG1579   172 IPPELLALYERIRK 185
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
930-979 3.44e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 42.68  E-value: 3.44e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 564365344    930 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 979
Cdd:smart00180    1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1484-1790 3.56e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1484 RRQAEEAQQRA-QAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEI 1562
Cdd:COG3064   119 KEKAEEAKRKAeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1563 AERVRSLADVDTILAHTMGDVRRAEqllQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL 1642
Cdd:COG3064   199 AAAALAAAAAAAAADAALLALAVAA---RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1643 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER 1722
Cdd:COG3064   276 SGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGA 355

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1723 KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG3064   356 GALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 1684-1795 3.72e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 46.09  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1684 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:PRK14475   36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564365344 1760 GTYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1795
Cdd:PRK14475  115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1613-1751 4.13e-05

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: 47.92  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1613 ALEEAQRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMAGT----EQSLNSASERARQLHA--LLEALKLK----RAGNS 1681
Cdd:TIGR02794   22 SLYHSVKPEPGGGAEIIQAVlVDPGAVAQQANRIQQQKKPAakkeQERQKKLEQQAEEAEKqrAAEQARQKeleqRAAAE 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1682 LAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEArgllQAAQDK 1751
Cdd:TIGR02794  102 KAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA----AEAKKK 167
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1489-1774 4.93e-05

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: 48.03  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1489 EAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRS 1568
Cdd:COG5185   272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1569 LADVDTILahtmgdVRRAEQLLQDAQRARSRAEGERQKA--ETVQAALEEAQRAQGAAQGAIRGAVVDT-KNTEQTLQQV 1645
Cdd:COG5185   352 LTENLEAI------KEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEEL 425

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1646 QERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALaerkae 1725
Cdd:COG5185   426 QRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL------ 497

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 564365344 1726 gvlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTyEENERELEVKAA 1774
Cdd:COG5185   498 -----KATLEKLRAKLERQLEGVRSKLDQVAESLKD-FMRARGYAHILA 540
PRK09039 PRK09039
peptidoglycan -binding protein;
1647-1776 5.36e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1647 ERMAGTEQSLNsasERARQLHALLEALKLKRAGN-SLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAERKAE 1725
Cdd:PRK09039   46 REISGKDSALD---RLNSQIAELADLLSLERQGNqDLQDSVANLRASLSAA---EAERSRLQALLAELAGAGAAAEGRAG 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1726 GVLAAQARAEQLRDEARG---LLQ----AAQDKLQRLQELEGTYEENERELEVKAAQL 1776
Cdd:PRK09039  120 ELAQELDSEKQVSARALAqveLLNqqiaALRRQLAALEAALDASEKRDRESQAKIADL 177
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1637-1784 5.63e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 46.36  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1637 NTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLREQVGdqyqtv 1716
Cdd:COG1842    23 DPEKMLDQAIRDM---EEDLVEARQALAQVIANQKRLERQLE-------ELEAEAEKWEEKARLALEKGREDLA------ 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344 1717 RALAERKAEgvlaAQARAEQLRdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:COG1842    87 REALERKAE----LEAQAEALE-AQLAQLEEQVEKLKEaLRQLESKLEELKAKKDTLKARAKAAKAQEK 150
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
1478-1757 6.42e-05

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 46.58  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1478 SRVSETRRQAEEAQQRAqAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvATRVLDISIPASPEQIQR 1557
Cdd:COG4223     7 AAVAELPAQLTALEQRL-AALEAAPAAAAATAALEARLAAL---------------------RAALAAAREAVAAAAAAA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1558 LASEIAErvrsladvdtilahtmgdvrraeqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQG------AIRGA 1631
Cdd:COG4223    65 LEARLAA-------------------------LEAKAAAPEAEAAAAARAAALALAAAALRAAVERGQPfaaelaALEAL 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1632 VVDtknteqtlQQVQERMAGTEQS-LNSASERARQLHALLEALklkragnsLAASTAEETAGSAQSRAREAekqLREQVg 1710
Cdd:COG4223   120 APD--------APALAALAAFAATgVPTLAALRAEFPAAARAA--------LAAARAPEADASWLDRLLAF---ARSLV- 179

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 564365344 1711 dqyqTVRALAERKAEGVLAAQARAEQ-LRdeaRGLLQAAQDKLQRLQE 1757
Cdd:COG4223   180 ----TVRRVGPVEGDDPDAILARAEAaLA---AGDLAGALAELEALPE 220
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1532-1751 6.45e-05

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: 47.15  E-value: 6.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1532 DPDSIEMVATRV-LDISIPASPEQ-----IQRLASE-----IAERVRSLADVDTILAHTmgDVRRAEQLLQDAQRARSRA 1600
Cdd:TIGR02794   44 DPGAVAQQANRIqQQKKPAAKKEQerqkkLEQQAEEaekqrAAEQARQKELEQRAAAEK--AAKQAEQAAKQAEEKQKQA 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1601 EGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL--QQVQERMAGTEQSLNSASERARQlhALLEALKLKra 1678
Cdd:TIGR02794  122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEAEAK--AKAEEAKAK-- 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1679 gnslaASTAEETAGS-AQSRArEAEKQLREqvgdqyqtvRALAERKAE-------GVLAAQARAEQLRDEARGLLQAAQD 1750
Cdd:TIGR02794  198 -----AEAAKAKAAAeAAAKA-EAEAAAAA---------AAEAERKADeaelgdiFGLASGSNAEKQGGARGAAAGSEVD 262


                   .
gi 564365344  1751 K 1751
Cdd:TIGR02794  263 K 263
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1553-1791 6.58e-05

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: 46.51  E-value: 6.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1553 EQIQRLASEIAERVRSLADVDTILAHTMgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAqgAAQGAIRgav 1632
Cdd:smart00283    7 EEIAAGAEEQAEELEELAERMEELSASI------EEVAANADEIAATAQSAAEAAEEGREAVEDAITA--MDQIREV--- 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1633 vdTKNTEQTLQQVQERMAGTEQSLNSASERARQ-----LHALLEAlklKRAGNS------LAA---STAEETAGSA---Q 1695
Cdd:smart00283   76 --VEEAVSAVEELEESSDEIGEIVSVIDDIADQtnllaLNAAIEA---ARAGEAgrgfavVADevrKLAERSAESAkeiE 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344   1696 SRAREAEKQLREQVGDQYQTVR------ALAERK-------AEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTY 1762
Cdd:smart00283  151 SLIKEIQEETNEAVAAMEESSSeveegvELVEETgdaleeiVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVT 230

                           250       260
                    ....*....|....*....|....*....
gi 564365344   1763 EENERELEVKAAQLDGLEARMRSVLQAIN 1791
Cdd:smart00283  231 QETAAMSEEISAAAEELSGLAEELDELVE 259
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 1577-1760 6.73e-05

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 47.21  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1577 AHTMGDVRRAEQLLqdaQRARSRAEGERQKAETVQAaleEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSL 1656
Cdd:COG3071    60 AQALGDYERRDEYL---AQALELAPEAELAVLLTRA---ELLLDQGQAEQAL-----------ATLEALRAGAPRHPQVL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1657 NSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQTVRAL------AERKAEGVLAA 1730
Cdd:COG3071   123 RLLLQAYRQLGDWEELLELLPALRKHKALSAEE----AQALERRAYLGLLRQAARDAEALKALwkalprAERRDPELAAA 198

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564365344 1731 QARA-EQLRD--EARGLLQAAQDK------LQRLQELEG 1760
Cdd:COG3071   199 YARAlIALGDhdEAERLLREALKRqwdprlVRLYGRLQG 237
Alanine_zipper pfam11839
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ...
 1584-1625 7.45e-05

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: 42.37  E-value: 7.45e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564365344  1584 RRAEQLLQDAQRARSRAEGERQKA----ETVQAALEEAQRAQGAAQ 1625
Cdd:pfam11839    8 SKADQAEQDAAAAQSAADSAKAKAdeaaARANAAEAAAEEAQQAAE 53
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1479-1706 7.86e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.83  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1479 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQ------NVKDFLSQEGADPDSIE--------MVATRVL 1544
Cdd:COG1340    51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREeldelrKELAELNKAGGSIDKLRkeierlewRQQTEVL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1545 disipaSPEQIQRLASEIAErvrsladvdtiLAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE-AQRAQga 1623
Cdd:COG1340   131 ------SPEEEKELVEKIKE-----------LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQ-- 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1624 aqgAIRGAVVDTKnteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK---------LKRAGNSLAASTAEETAGSA 1694
Cdd:COG1340   192 ---ELHEEMIELY---KEADELRKEADELHKEIVEAQEKADELHEEIIELQkelrelrkeLKKLRKKQRALKREKEKEEL 265

                         250
                  ....*....|..
gi 564365344 1695 QSRAREAEKQLR 1706
Cdd:COG1340   266 EEKAEEIFEKLK 277
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1696-1791 8.37e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1696 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKL----QRLQELEGTYEENERELE 1770
Cdd:COG4913   238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312

                          90       100
                  ....*....|....*....|.
gi 564365344 1771 VKAAQLDGLEARMRSVLQAIN 1791
Cdd:COG4913   313 RLEARLDALREELDELEAQIR 333
FliJ pfam02050
Flagellar FliJ protein;
1605-1740 8.42e-05

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 43.81  E-value: 8.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1605 QKAETvqaALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRagNSL 1682
Cdd:pfam02050    1 DEAAR---ELAEAQRELQQAEEKLE-------ELQQYRAEYQQQLSGAGQGISAAELRNYQafISQLDEAIAQQQ--QEL 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365344  1683 AASTAEetagsaQSRAREA--EKQLReqvgdqYQTVRALAERKAEGVLAAQARAEQLR-DE 1740
Cdd:pfam02050   69 AQAEAQ------VEKAREEwqEARQE------RKSLEKLREREKKEERKEQNRREQKQlDE 117
PRK12472 PRK12472
hypothetical protein; Provisional
 1606-1750 9.56e-05

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 47.17  E-value: 9.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1606 KAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERArqlhallEAlKLKRAGNSLAAS 1685
Cdd:PRK12472  181 KAEALAAAPARAETLAREAEDAARAAD-EAKTAAAAAAREAAPLKASLRKLERAKARA-------DA-ELKRADKALAAA 251

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1686 TAEETAGSAQSRAREAEKQLREqVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQD 1750
Cdd:PRK12472  252 KTDEAKARAEERQQKAAQQAAE-AATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATD 315
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1587-1773 9.60e-05

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: 44.95  E-value: 9.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1587 EQLLQDAQRARSRAEGERQKA-ETVQAALEEAqraqgaaqgaiRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASER--- 1662
Cdd:pfam01442   18 EQLGPVAQELVDRLEKETEALrERLQKDLEEV-----------RAKL--EPYLEELQAKLGQNVEELRQRLEPYTEElrk 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1663 --ARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVgdqyqtvralaerkaegvlaaQARAEQLRDE 1740
Cdd:pfam01442   85 rlNADAEELQEKLAPYGEE---LRERLEQNVDALRARLAPYAEELRQKL---------------------AERLEELKES 140

                          170       180       190
                   ....*....|....*....|....*....|....
gi 564365344  1741 ARGLLQAAQDKL-QRLQELEGTYEENERELEVKA 1773
Cdd:pfam01442  141 LAPYAEEVQAQLsQRLQELREKLEPQAEDLREKL 174
T3SSipB pfam16535
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ...
 1663-1781 9.98e-05

Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.


Pssm-ID: 435406 [Multi-domain]  Cd Length: 155  Bit Score: 44.57  E-value: 9.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1663 ARQLHALLEALKLKRAGNSLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRD 1739
Cdd:pfam16535    1 AGQLTLLLGNLMSLLGEVSLSQLESRIAAWKAMQ---EAQQQKGLELSDEFQTALSEAEeatDAYEKAINKLKNAKSKAK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 564365344  1740 EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA 1781
Cdd:pfam16535   78 AAEKKIDQAQTRLQSLAPDSPGKAKLEAAEQQAGIKKDALQA 119
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1580-1775 1.06e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 46.90  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1580 MGDVRRAEQLLQDA-QRARSRAEGE---RQKAEtvQAALEEAQRAQGAAQgairgavvdTKNTEQTLQQVQERMAgtEQS 1655
Cdd:PRK07735    1 MDPEKDLEDLKKEAaRRAKEEARKRlvaKHGAE--ISKLEEENREKEKAL---------PKNDDMTIEEAKRRAA--AAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1656 LNSASERARQLHALLEALklkrAGNSLAASTAEeTAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGvlAAQARAE 1735
Cdd:PRK07735   68 KAKAAALAKQKREGTEEV----TEEEKAKAKAK-AAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAA--AAKAKAA 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 564365344 1736 QLRDEARGllqaaqdklqrlQELEGTYEENERELEVKAAQ 1775
Cdd:PRK07735  141 ALAKQKRE------------GTEEVTEEEEETDKEKAKAK 168
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1484-1784 1.08e-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: 46.45  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1484 RRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflsQEgadpdsiemvatRVLDisipaspEQIQRLASEIA 1563
Cdd:pfam13868  108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EE------------REED-------ERILEYLKEKA 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1564 ERVRSladvdtilahtmgdvRRAEQLLQDAQRARsraegERQKaetVQAALEEAQRAQgAAQGAIRgavvdtkntEQTLQ 1643
Cdd:pfam13868  166 EREEE---------------REAEREEIEEEKER-----EIAR---LRAQQEKAQDEK-AERDELR---------AKLYQ 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1644 QVQERMagteqslnsasERARQLHALLEALKLKRAgnslaastaeetagsaQSRAREAEKQLREQvgdQYQTVRALAERK 1723
Cdd:pfam13868  213 EEQERK-----------ERQKEREEAEKKARQRQE----------------LQQAREEQIELKER---RLAEEAEREEEE 262

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344  1724 AEGVLAAQA---RAEQLRDEARgllqaAQDKLQRLQELEGTYEENE--RELEVKAAQLDGLEARMR 1784
Cdd:pfam13868  263 FERMLRKQAedeEIEQEEAEKR-----RMKRLEHRRELEKQIEEREeqRAAEREEELEEGERLREE 323
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1445-1795 1.44e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.96  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1445 CSGAAATADLALGRARHTQAELQRALVEGGGIL-------------------SRVSETRRQAEEAQQRAQAAL----DKA 1501
Cdd:TIGR00606  632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLrlapDKL 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1502 NASRGQVEQANQELRELI------QNVKDFLSQEgadpdsiemvatrvldisIPASPEQIQRLASEIAERVRSLADVDTI 1575
Cdd:TIGR00606  712 KSTESELKKKEKRRDEMLglapgrQSIIDLKEKE------------------IPELRNKLQKVNRDIQRLKNDIEEQETL 773

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1576 LAHTMGDVRRAEQLLQDAqrarsraegerQKAETVQAALEEAQR--AQGAAQgairgavVDTKNTEQTLQQVQERMAGTE 1653
Cdd:TIGR00606  774 LGTIMPEEESAKVCLTDV-----------TIMERFQMELKDVERkiAQQAAK-------LQGSDLDRTVQQVNQEKQEKQ 835

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1654 QSLNSASERARQLHALLE-----ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVL 1728
Cdd:TIGR00606  836 HELDTVVSKIELNRKLIQdqqeqIQHLKSKTNEL--KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1729 AAQARaEQLRDEARGLL-------QAAQDKLQRLQE-----------LEGTYEE--------NERELEVKAAQLDGLEAR 1782
Cdd:TIGR00606  914 LETFL-EKDQQEKEELIssketsnKKAQDKVNDIKEkvknihgymkdIENKIQDgkddylkqKETELNTVNAQLEECEKH 992

                          410       420
                   ....*....|....*....|
gi 564365344  1783 -------MRSVLQAINLQVQ 1795
Cdd:TIGR00606  993 qekinedMRLMRQDIDTQKI 1012
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1452-1791 1.47e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 46.76  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1452 ADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA-----QAAL----DKANASRGQVEQANQELRELIQNV 1522
Cdd:pfam12128  651 ARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQldkkhQAWLeeqkEQKREARTEKQAYWQVVEGALDAQ 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1523 KDFLSQE--------GADPDSIEMVATRVLDiSIPASPEQIQRLASEIAERVRSLADVdtilAHTMGDVRRAEQLLQDA- 1593
Cdd:pfam12128  731 LALLKAAiaarrsgaKAELKALETWYKRDLA-SLGVDPDVIAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETw 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1594 ----QRARSRAEGERQKAETVQ---AALEEAQRAQGAA----QGAIRGAVVDTKNTEQTLQQVQERMA------GTEQSL 1656
Cdd:pfam12128  806 lqrrPRLATQLSNIERAISELQqqlARLIADTKLRRAKlemeRKASEKQQVRLSENLRGLRCEMSKLAtlkedaNSEQAQ 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1657 NSASERARQlhalLEALKLKRAGNSLAASTAEE---TAGSAQSRAREAEKQLREQVGDQYQT---VRALAERKAEGVLA- 1729
Cdd:pfam12128  886 GSIGERLAQ----LEDLKLKRDYLSESVKKYVEhfkNVIADHSGSGLAETWESLREEDHYQNdkgIRLLDYRKLVPYLEq 961

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365344  1730 -AQARAEQ----LRDEARGLLQAAQDKLQRLQELEGTYEENEREL--EVKA-AQLDGL---EARMRSVLQAIN 1791
Cdd:pfam12128  962 wFDVRVPQsimvLREQVSILGVDLTEFYDVLADFDRRIASFSRELqrEVGEeAFFEGVsesAVRIRSKVSELE 1034
Filament pfam00038
Intermediate filament protein;
1553-1798 1.96e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.68  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1553 EQIQ----RLASEIaERVRSLADVDTILAhtmgdvRRAEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQGAI 1628
Cdd:pfam00038    4 EQLQelndRLASYI-DKVRFLEQQNKLLE------TKISELRQKKGAEPSRLY------SLYEKEIEDLRRQLDTLTVER 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1629 RGAVVDTKNTEQTLQQVQERMAgTEQSLNSASERA-----RQLHAL-LEALKLKRAGNSLAastaEETAgsAQSRAREAE 1702
Cdd:pfam00038   71 ARLQLELDNLRLAAEDFRQKYE-DELNLRTSAENDlvglrKDLDEAtLARVDLEAKIESLK----EELA--FLKKNHEEE 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1703 -KQLREQVGDQYQTV-----------RALAERKAE-GVLAA----------QARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:pfam00038  144 vRELQAQVSDTQVNVemdaarkldltSALAEIRAQyEEIAAknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELR 223

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 564365344  1760 GTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1798
Cdd:pfam00038  224 RTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQ 262
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1699-1795 2.17e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.43  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1699 REAEKQL---REQVGDQyQTVRALAERKAEgvlAAQARAEQLRDEARGLLQAAQDKL-----QRLQELEGTYEENERELE 1770
Cdd:COG1842    33 RDMEEDLveaRQALAQV-IANQKRLERQLE---ELEAEAEKWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA 108

                          90       100
                  ....*....|....*....|....*
gi 564365344 1771 vkaaQLDGLEARMRSVLQAINLQVQ 1795
Cdd:COG1842   109 ----QLEEQVEKLKEALRQLESKLE 129
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1647-1754 2.23e-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: 43.24  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1647 ERMAGTEQSLNSASERARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEg 1726
Cdd:COG0711    31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAE---ARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE- 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 564365344 1727 vlAAQARA-EQLRDEARGL-LQAAQDKLQR 1754
Cdd:COG0711   107 --QERAKAlAELRAEVADLaVAIAEKILGK 134
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1448-1668 2.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1448 AAATADLALGRARHTQAELQRALVEGggILSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIqnvkdfls 1527
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEA--ELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLD-------- 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1528 qegadpdsiemvatrvldisipASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA 1607
Cdd:COG4913   682 ----------------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---QDRL 736

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365344 1608 ETVQAALEEAQRAQGAAQgaiRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1668
Cdd:COG4913   737 EAAEDLARLELRALLEER---FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1553-1737 2.31e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 45.74  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1553 EQIQRLASEIAERVRSLADVDTIlahtmgDVRRAEQLLQDAQRARSrAEGERQKAETVQAALEE--AQRAQGAAQGAIRG 1630
Cdd:PRK07735   32 AEISKLEEENREKEKALPKNDDM------TIEEAKRRAAAAAKAKA-AALAKQKREGTEEVTEEekAKAKAKAAAAAKAK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1631 AVVDTKNTEQTLQQVQE------RMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGS-AQSRAREAEK 1703
Cdd:PRK07735  105 AAALAKQKREGTEEVTEeekaaaKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAkAKAAALAKQK 184

                         170       180       190
                  ....*....|....*....|....*....|....
gi 564365344 1704 QLREQVGDQYQTVRALAERKAEGVLAAQARAEQL 1737
Cdd:PRK07735  185 AAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAL 218
PRK11281 PRK11281
mechanosensitive channel MscK;
1588-1791 2.59e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1588 QLLQDAQRARSRAEGERQKAETVQAALEEAQRaQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASErarqlh 1667
Cdd:PRK11281   70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA-ELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQN------ 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1668 ALLEAlklkragNSLAAS--TAEETAGSAQSRAREAEKQLREQvgdqyqtvraLAERKAEGvlaaqaraEQLRDEARGLL 1745
Cdd:PRK11281  143 DLAEY-------NSQLVSlqTQPERAQAALYANSQRLQQIRNL----------LKGGKVGG--------KALRPSQRVLL 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1746 QA------AQDKLQRlQELEG-----TYEENERELevKAAQLDGLEaRMRSVLQ-AIN 1791
Cdd:PRK11281  198 QAeqallnAQNDLQR-KSLEGntqlqDLLQKQRDY--LTARIQRLE-HQLQLLQeAIN 251
DUF4398 pfam14346
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. ...
 1446-1511 2.62e-04

Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 127 and 269 amino acids in length.


Pssm-ID: 464144 [Multi-domain]  Cd Length: 78  Bit Score: 41.09  E-value: 2.62e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344  1446 SGAAATADLALGRARHTQAELQRALVEGggilsRVSETRRQAEEAQQRAQAALDKANA--SRGQVEQA 1511
Cdd:pfam14346   16 DGAAQYAPLELKRARDALAKAEAAMAEK-----DYEKARHLAYLAEADAELAEAKARAakAEAAAAQA 78
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1694-1796 2.82e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.04  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1694 AQSRAREAEKQLrEQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQDKL---QRLQELEGTYEENERELE 1770
Cdd:COG1566    88 AEAQLAAAEAQL-ARLEAELGAEAEIAAAEAQ-LAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDAAQAQLE 165

                          90       100
                  ....*....|....*....|....*.
gi 564365344 1771 VKAAQLDGLEARMRSVLQAINLQVQI 1796
Cdd:COG1566   166 AAQAQLAQAQAGLREEEELAAAQAQV 191
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1455-1650 2.88e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.25  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1455 ALGRARHTQ----AELQRALVEGGGILsRVSETRRQAEEAQQRAQAALDKAnasrgQVEQANQELRELIQNVKdfLSQEG 1530
Cdd:COG2268   188 ALGRRKIAEiirdARIAEAEAERETEI-AIAQANREAEEAELEQEREIETA-----RIAEAEAELAKKKAEER--REAET 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1531 AdpdsiEMVATRVLDISIPASPEQIQRLAsEIAERVRSLAdvdtiLAHtmgdvRRAEQLLQDAQRA-RSRAEGERQKAET 1609
Cdd:COG2268   260 A-----RAEAEAAYEIAEANAEREVQRQL-EIAEREREIE-----LQE-----KEAEREEAELEADvRKPAEAEKQAAEA 323

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564365344 1610 VQAALEEAQRAQGAAQGAIRGAVVDTKNTE----------QTLQQVQERMA 1650
Cdd:COG2268   324 EAEAEAEAIRAKGLAEAEGKRALAEAWNKLgdaaillmliEKLPEIAEAAA 374
PRK12472 PRK12472
hypothetical protein; Provisional
 1548-1703 2.88e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 45.63  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1548 IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEgerqkaetvqAALEEAQRAQGAAQga 1627
Cdd:PRK12472  185 LAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARAD----------AELKRADKALAAAK-- 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365344 1628 irgavvdtknTEQTLQQVQERMAGTEQslnSASERARQLHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEK 1703
Cdd:PRK12472  253 ----------TDEAKARAEERQQKAAQ---QAAEAATQLDTAKADAEAKRA----AAAATKEAAKAAAAKKAETAK 311
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1638-1790 2.94e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1638 TEQTLQQVQERMA-----GTE-----QSLNSASERARQLHALLEALKLKRAgnSLAASTAEEtagsAQSRAREAEKQLRE 1707
Cdd:COG1196   177 AERKLEATEENLErlediLGElerqlEPLERQAEKAERYRELKEELKELEA--ELLLLKLRE----LEAELEELEAELEE 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1708 qvgdqyqtvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ----ELEGTYEENERELEVKAAQLDGLEARM 1783
Cdd:COG1196   251 ------------LEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERL 318


                  ....*..
gi 564365344 1784 RSVLQAI 1790
Cdd:COG1196   319 EELEEEL 325
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 1585-1620 3.03e-04

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: 41.52  E-value: 3.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564365344 1585 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1620
Cdd:NF040598   37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1454-1709 3.38e-04

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: 44.72  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1454 LALGRARHTQAELQRALvegggilsRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvkdflsqegADP 1533
Cdd:COG2956    46 LALGNLYRRRGEYDRAI--------RIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE----------LDP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1534 DSIEmVATRVLDISipaspEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1611
Cdd:COG2956   108 DDAE-ALRLLAEIY-----EQEGDWekAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1612 AALEEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEET 1690
Cdd:COG2956   182 LLLAELYLEQGDYEEAI-----------AALERALEQDPDYLPALPRLAELYEKLGDPEEALElLRKALELDPSDDLLLA 250

                         250       260
                  ....*....|....*....|..
gi 564365344 1691 AGS---AQSRAREAEKQLREQV 1709
Cdd:COG2956   251 LADlleRKEGLEAALALLERQL 272
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1636-1783 3.90e-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: 43.90  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1636 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaastaeETAGSAQSRAREAEKQLREQVgdqyqt 1715
Cdd:pfam04012   25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQT--------------EQAKKLEEKAQAALTKGNEEL------ 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344  1716 VRALAERKAEgvLAAQARAEQlrdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARM 1783
Cdd:pfam04012   85 AREALAEKKS--LEKQAEALE---TQLAQQRSAVEQLRKqLAALETKIQQLKAKKNLLKARLKAAKAQE 148
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 1447-1748 4.00e-04

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 44.52  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1447 GAAATAD--LALGRARHTQAE--LQRAlvegggilsrvsetrrqAEEAQQRAQAALDKANAS--RGQVEQANQELRELIQ 1520
Cdd:COG3071    16 LLAALLEglLALAEGRYARAEklLSKA-----------------AEHSEAPLLAYLLAARAAqaLGDYERRDEYLAQALE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1521 NvkdflsqegaDPDSIEMVAtrvldisipaspeqiqrlaseiaervrsladvdtilahtmgdVRRAEQLLQ--DAQRARS 1598
Cdd:COG3071    79 L----------APEAELAVL------------------------------------------LTRAELLLDqgQAEQALA 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1599 RAEGERQKA---ETVQAALEEAQRAQGAAQGAI--------RGAVvdtknTEQTLQQVQERMAgtEQSLNSASERARQLH 1667
Cdd:COG3071   107 TLEALRAGAprhPQVLRLLLQAYRQLGDWEELLellpalrkHKAL-----SAEEAQALERRAY--LGLLRQAARDAEALK 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1668 ALLEAL-KLKRAGNSLAASTAEetAGSAQSRAREAEKQLREQVGDQYQT--VRALAERKAEGVLAAQARAE--------- 1735
Cdd:COG3071   180 ALWKALpRAERRDPELAAAYAR--ALIALGDHDEAERLLREALKRQWDPrlVRLYGRLQGGDPAKQLKRAEkwlkkhpnd 257

                         330       340
                  ....*....|....*....|....*..
gi 564365344 1736 --------------QLRDEARGLLQAA 1748
Cdd:COG3071   258 pdlllalgrlclrnQLWGKAREYLEAA 284
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
1612-1789 4.01e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 44.27  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1612 AALEEAQRAQGA-AQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEET 1690
Cdd:COG4223    24 AALEAAPAAAAAtAALEARLAALRAALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAA-RAAALALAAAALRAA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1691 AGSAQSRAREAEkQLREQVGDQyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAqdklqrlqelegtyeeneRELE 1770
Cdd:COG4223   103 VERGQPFAAELA-ALEALAPDA-PALAALAAFAATGVPTLAALRAEFPAAARAALAAA------------------RAPE 162

                         170
                  ....*....|....*....
gi 564365344 1771 VKAAQLDGLEARMRSVLQA 1789
Cdd:COG4223   163 ADASWLDRLLAFARSLVTV 181
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
880-919 4.02e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 4.02e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 564365344    880 CVCNGR---ADECDAHTGACLgCRDYTGGEHCERCIAGFHGDP 919
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
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 ...
 1641-1737 4.28e-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: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1641 TLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQtvRALA 1720
Cdd:pfam00430   38 EIAEAEERRKDAAAALAEAEQQLKE--ARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKD--RALA 113

                           90
                   ....*....|....*..
gi 564365344  1721 ERKAEGVLAAQARAEQL 1737
Cdd:pfam00430  114 ELRQQVVALAVQIAEKL 130
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1469-1756 4.76e-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: 45.21  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1469 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1548
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1549 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1625
Cdd:NF012221 1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1626 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALL---EALKLKRAGNSLA----------ASTAEET 1690
Cdd:NF012221 1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1691 AGSAQSRAR-----EAEKQLREQV------GDQYqTVRALAER----KAEGVLAAQAR-AEQLRDEARGLLQAAQDKLQR 1754
Cdd:NF012221 1762 ANQAQADAKgakqdESDKPNRQGAagsglsGKAY-SVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNR 1840


                  ..
gi 564365344 1755 LQ 1756
Cdd:NF012221 1841 LQ 1842
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 1571-1770 4.79e-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: 43.50  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1571 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1650
Cdd:cd07596     1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1651 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKQlREQVGDQYQTV-------RALAE 1721
Cdd:cd07596    71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDD-RADALLTLQSLkkdlaskKAQLE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 564365344 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1770
Cdd:cd07596   135 KLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 1616-1763 4.82e-04

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 44.67  E-value: 4.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1616 EAQRAQGAAQGAIRGAVVDTKnTEQTLQQVQERMAGTEQSLNsaseRARQLHALLEALKLKRAgnslAASTAEETAGSAQ 1695
Cdd:pfam15070   10 QTERDQYAENLKEEGAVWQQK-MQQLSEQVRTLREEKERSVS----QVQELETSLAELKNQAA----VPPAEEEQPPAGP 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344  1696 SrarEAEKQLREQVGDQYQTVRALAerkaegvlaAQARAeQLRDEArGLLQAAQDKLQRLQELEGTYE 1763
Cdd:pfam15070   81 S---EEEQRLQEEAEQLQKELEALA---------GQLQA-QVQDNE-QLSRLNQEQEQRLLELERAAE 134
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1562-1759 5.39e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.48  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1562 IAErVRSLADVDTILAHTMGDVRRAEQ--------LLQDAQRAR---SRAEGERQKAEtvQAALEEAQRAQGAAQgairg 1630
Cdd:COG2268   194 IAE-IIRDARIAEAEAERETEIAIAQAnreaeeaeLEQEREIETariAEAEAELAKKK--AEERREAETARAEAE----- 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1631 avvdtknteqtlQQVQERMAGTEQSLNSASERARQLHALleALKLKRagnslaastaeetagsAQSRAREAEKQLREQVG 1710
Cdd:COG2268   266 ------------AAYEIAEANAEREVQRQLEIAEREREI--ELQEKE----------------AEREEAELEADVRKPAE 315

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1711 DQYQTVRALAERKAEGVLA---AQARAEQLRDEARGLLQAAQDKLQRLQELE 1759
Cdd:COG2268   316 AEKQAAEAEAEAEAEAIRAkglAEAEGKRALAEAWNKLGDAAILLMLIEKLP 367
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1585-1775 5.56e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1585 RAEQLLQDAQRA-----RSRAEGERqKAETVQAALEEAqraqgaaqgairgavVDTKNTEQT-LQQVQERMAGTEQSLNS 1658
Cdd:pfam05557   10 RLSQLQNEKKQMelehkRARIELEK-KASALKRQLDRE---------------SDRNQELQKrIRLLEKREAEAEEALRE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1659 ASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRARE-------AEKQLREQVGDQYQTVRALAERKAEgvlaaQ 1731
Cdd:pfam05557   74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSElrrqiqrAELELQSTNSELEELQERLDLLKAK-----A 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 564365344  1732 ARAEQLRDEarglLQAAQDKL----QRLQELEgtYE---ENERELEVKAAQ 1775
Cdd:pfam05557  149 SEAEQLRQN----LEKQQSSLaeaeQRIKELE--FEiqsQEQDSEIVKNSK 193
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1564-1784 6.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 6.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1564 ERVRSLADVDTILAHTMGDVRRaeQLLQDAQRARSRAEGERQKA-ETVQAALEEA-----QRAQGAAQG----------- 1626
Cdd:PHA03247 1552 ERVDQSPVKDTAYAEYVAFVAR--RDLAEAKDALVRAKQQRAEAtDRVTAALREAlaaheRRAQSEAESlanlktllrva 1629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1627 AIRGAVVDT----KNTEQTLQQVQERMAGTEQS--LNSAS----ERARQL---HALLEALK-----LKRAGNSLAASTAE 1688
Cdd:PHA03247 1630 AIPATAAKTldqaRSVAEIVDQIELLLEQTEKAaeLDVAAvdwlEHARRVfeaHPLTAARGggpdpLARLHARLDALGET 1709

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1689 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLL----QAAQDKL-QRLQELEGTyE 1763
Cdd:PHA03247 1710 RRRTEALRRSLEAAEAEWDEVWGRFGRVRGGAWKSPEALRAAREQLRALQTATNTVLglraDAHYERLpAKYQGALGA-K 1788

                         250       260
                  ....*....|....*....|....*.
gi 564365344 1764 ENER-----ELEVKAAQLDGLEARMR 1784
Cdd:PHA03247 1789 SAERagaveELGAAVARHDGLLARLR 1814
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 1556-1645 6.62e-04

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 40.88  E-value: 6.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1556 QRLASEIAERVRSLAD-VDTILAHTMGDVRRAEQ----LLQDAQ----------RARSRAEGERQKAETVQAALEEAQRA 1620
Cdd:pfam16999    4 SRLLSELAEREAALDQqIEAARKEAEREVEAAEAeaarILREAEakakalqaeyRQELAAETARIREEARARAEAEAQAV 83

                           90       100
                   ....*....|....*....|....*
gi 564365344  1621 QGAAQGAIRGAVvdtkntEQTLQQV 1645
Cdd:pfam16999   84 RTRAEGRLQQAV------ELILRAV 102
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 1485-1660 6.63e-04

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 43.67  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1485 RQAEEA-QQRAQAAL---------DKA-NASRGQVeqaNQELRELIQnvkdflsqEGADPDSIEMVATRVLDISIPaspE 1553
Cdd:COG0330   102 ENAEEAlRQLAESALrevigkmtlDEVlSTGRDEI---NAEIREELQ--------EALDPYGIEVVDVEIKDIDPP---E 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1554 QIQRlaseiaervrsladvdtilahTMGDVRRAEQllqDAQRARSRAEGERQKAETVqaALEEAQR----AQGAAQGAIR 1629
Cdd:COG0330   168 EVQD---------------------AMEDRMKAER---EREAAILEAEGYREAAIIR--AEGEAQRaiieAEAYREAQIL 221

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564365344 1630 GAVVDTKNTEQTLQQ-------VQERMAGT-EQSLNSAS 1660
Cdd:COG0330   222 RAEGEAEAFRIVAEAysaapfvLFYRSLEAlEEVLSPNS 260
DUF6781 pfam20572
Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. ...
 1620-1754 7.23e-04

Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 223 and 298 amino acids in length.


Pssm-ID: 466721  Cd Length: 213  Bit Score: 43.02  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1620 AQGAAQGAIRGAVVDTkntEQTLQQVqerMAGTEQSLNSASErARQLhALLEALK---------LKRAGNSLAA------ 1684
Cdd:pfam20572   56 TEGASQGANAARGGEV---EALLKQA---VAGLDDALLKAAE-ASRL-ALEEAVDqgaafseqdLKKALDDLEKledtff 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1685 ----STAEETAGSAQS------------------RAREAEKQLREQVGDqyqtvrALAERKAEGVLAAQARAEQLRDEAR 1742
Cdd:pfam20572  128 dtlrKAAKSAGGPLKGpwgdlldhlkrsgtdtgaQARAAVEQLAAQLQA------ALREGRAAGSRAARALADSYAALAS 201

                          170
                   ....*....|..
gi 564365344  1743 GLLQAAQDKLQR 1754
Cdd:pfam20572  202 GVLIGLSEALQP 213
PTZ00491 PTZ00491
major vault protein; Provisional
 1618-1790 7.53e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 44.62  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1618 QRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMagtEQSLNSASERAR---QLHALLEALKLKRAgnsLAASTAEETAGS 1693
Cdd:PTZ00491  643 ERTRDSLQKSVQLAIeITTKSQEAAARHQAELL---EQEARGRLERQKmhdKAKAEEQRTKLLEL---QAESAAVESSGQ 716

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1694 AQSRAR-EAEKqlreqvgdqyqtvrALAERKAEgVLAAQARAEQLRDEARGLLqaaqDKLQRLQELEGTYEENERELEV- 1771
Cdd:PTZ00491  717 SRAEALaEAEA--------------RLIEAEAE-VEQAELRAKALRIEAEAEL----EKLRKRQELELEYEQAQNELEIa 777

                         170       180
                  ....*....|....*....|
gi 564365344 1772 KAAQLDGLEA-RMRSVLQAI 1790
Cdd:PTZ00491  778 KAKELADIEAtKFERIVEAL 797
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
1470-1617 8.05e-04

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 43.87  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1470 LVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdflsqegadpdsiemvatRVLDISIP 1549
Cdd:COG1538   250 LFDGGRNRARVRAAKAQLEQAEAQYEQTVLQA---LQEVEDALAALRAAREQL-------------------EALEEALE 307

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365344 1550 ASpEQIQRLAseiaeRVRSLADVDTILahtmgDVRRAEQLLQDAQRARSRAEGERQKAetvQAALEEA 1617
Cdd:COG1538   308 AA-EEALELA-----RARYRAGLASLL-----DVLDAQRELLQAQLNLIQARYDYLLA---LVQLYRA 361
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 1640-1778 8.19e-04

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 44.28  E-value: 8.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1640 QTLQQVQERmagteqsLNSASERARQLHALLEALKLKRAGNSLAASTAEETA---------------------GSAQSRA 1698
Cdd:pfam15070  288 QELQETQER-------LEALTQQNQQLQAQLSLLANPGEGDGLESEEEEEEAprpslsipedfesreamvaffNSALAQA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1699 REAEKQLREQVGDQYQTVRALAERKAEG-------VLAAQARAEQLRDEARGLLQAAQDKLQ-RLQEL-EGTYEENER-- 1767
Cdd:pfam15070  361 EEERAELRRQLKEQKRRCRRLAQQAAPAqeepeheAHAPGTGGDSVPVEVHQALQVAMEKLQsRFTELmQEKADLKERve 440

                          170
                   ....*....|.
gi 564365344  1768 ELEVKAAQLDG 1778
Cdd:pfam15070  441 ELEHRCIQLSG 451
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 1469-1653 9.21e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 43.57  E-value: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1469 ALVEGGGILSRVSETRRQAEEAQqrAQAALDKAnasRGQVEQANQELRELiQNVKDFLSQEGADPDSIEmVATRVLDISI 1548
Cdd:pfam00529   40 DRVKAGDVLFQLDPTDYQAALDS--AEAQLAKA---QAQVARLQAELDRL-QALESELAISRQDYDGAT-AQLRAAQAAV 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1549 PASPEQIQrLASEIAERVRSLADVDTILAHTMGDVRRaeqLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAI 1628
Cdd:pfam00529  113 KAAQAQLA-QAQIDLARRRVLAPIGGISRESLVTAGA---LVAQAQANLLATVAQLDQIYVQITQSAAENQAE--VRSEL 186

                          170       180
                   ....*....|....*....|....*
gi 564365344  1629 RGAVVDTKNTEQTLQQVQERMAGTE 1653
Cdd:pfam00529  187 SGAQLQIAEAEAELKLAKLDLERTE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1583-1757 9.34e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.43  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1583 VRRAEQLLQDAQRARS--RAEGERQKAETVQAALEEAQRA----QGAAQGAIRGAVVDTKNTEQTLQQVQER-------M 1649
Cdd:cd00176    16 LSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERvealNELGEQLIEEGHPDAEEIQERLEELNQRweelrelA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1650 AGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEETAGSAQSRAREaEKQLREQVgDQYQTVRALAERKAEGVL 1728
Cdd:cd00176    96 EERRQRLEEALDLQQFFRDADDLEQwLEEKEAALASEDLGKDLESVEELLKK-HKELEEEL-EAHEPRLKSLNELAEELL 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 564365344 1729 AA---------QARAEQLRDEARGLLQAAQDKLQRLQE 1757
Cdd:cd00176   174 EEghpdadeeiEEKLEELNERWEELLELAEERQKKLEE 211
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
350-403 1.21e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.45  E-value: 1.21e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564365344    350 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 403
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1646-1796 1.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1646 QERMAGTEQSLNSASERARQLHALLEalKLKRAgnslaASTAEEtAGSAQSRAREAEKQLReqvGDQYQTVRALAERKAE 1725
Cdd:COG1196   178 ERKLEATEENLERLEDILGELERQLE--PLERQ-----AEKAER-YRELKEELKELEAELL---LLKLRELEAELEELEA 246

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1726 GVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ-AINLQVQI 1796
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErRRELEERL 318
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 1634-1760 1.22e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 41.48  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1634 DTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlKLKRAGNSLAASTAEETAGSAQSRARE--AEKQlreqvgd 1711
Cdd:PRK07352   58 ALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKA-RAEAIRAEIEKQAIEDMARLKQTAAADlsAEQE------- 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365344 1712 qyqtvRALAERKAEGVLAAQARAE-QLRDearGLLQAAQDKL--QRLQELEG 1760
Cdd:PRK07352  130 -----RVIAQLRREAAELAIAKAEsQLPG---RLDEDAQQRLidRSIANLGG 173
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1691-1790 1.42e-03

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: 43.21  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1691 AGSAQSRAREAEKQLREQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENER 1767
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKElaaLKKEEKALLKQLAALERRIAALARRIRALE---QELAALEAELAELEK 90

                          90       100
                  ....*....|....*....|...
gi 564365344 1768 ELEVKAAQLDGLEARMRSVLQAI 1790
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRAL 113
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1585-1776 1.66e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.25  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1585 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgaIRGAVV----DTKNTEQTLQQVQERMAGTEQSL---- 1656
Cdd:PRK10246  251 RLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQ--LRPHWEriqeQSAALAHTRQQIEEVNTRLQSTMalra 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1657 ---NSASERARQLHALLEALKLKRAGNSLAASTAEETAG-----SAQSRAREAEKQLREQVGDQYQTVRALAE------- 1721
Cdd:PRK10246  329 rirHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLRQWQQQLTHAEQKLNALPAitltlta 408

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564365344 1722 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1776
Cdd:PRK10246  409 DEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1636-1793 1.79e-03

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: 41.94  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1636 KNTEQTLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLaastaEETAGSAQSRAREAEKQLRE--QVGDQY 1713
Cdd:pfam00261    4 QQIKEELDEAEERLKEAMKKLEEAEKRAEK--AEAEVAALNRRIQLL-----EEELERTEERLAEALEKLEEaeKAADES 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1714 QTVR-ALAERKAEG-----VLAAQAR-AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyEENERELEVKAAQldgLEARMRS 1785
Cdd:pfam00261   77 ERGRkVLENRALKDeekmeILEAQLKeAKEIAEEADRKYEEVARKLVVVEgDLERA-EERAELAESKIVE---LEEELKV 152


                   ....*...
gi 564365344  1786 VLQaiNLQ 1793
Cdd:pfam00261  153 VGN--NLK 158
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 ...
 1720-1796 2.23e-03

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: 39.99  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1720 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1791
Cdd:pfam00430   42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121


                   ....*
gi 564365344  1792 LQVQI 1796
Cdd:pfam00430  122 LAVQI 126
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1553-1650 2.25e-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: 40.54  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1553 EQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQ------RARSRAEGERQKAETVQAALEEAQRAQGAAQG 1626
Cdd:COG0711    31 ERQEKIADGLAEAERAKEEAEAALA-------EYEEKLAEARaeaaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEA 103

                          90       100
                  ....*....|....*....|....
gi 564365344 1627 AIRGAVvdtkntEQTLQQVQERMA 1650
Cdd:COG0711   104 EIEQER------AKALAELRAEVA 121
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
1594-1775 2.38e-03

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 42.82  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1594 QRARSRAEGERQKAETVQAALEEAQRAQgaaqgairgavvdtkntEQTLQQVQERMagteqslnsasERARQLHALLEAL 1673
Cdd:COG1193   503 ERARELLGEESIDVEKLIEELERERREL-----------------EEEREEAERLR-----------EELEKLREELEEK 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1674 KLKragnslaastaeetagsaqsrAREAEKQLREQvgdqyqtvralAERKAEGVLA-AQARAEQLRDEAR---GLLQAAQ 1749
Cdd:COG1193   555 LEE---------------------LEEEKEEILEK-----------AREEAEEILReARKEAEELIRELReaqAEEEELK 602

                         170       180
                  ....*....|....*....|....*.
gi 564365344 1750 DKLQRLQELEGTYEENERELEVKAAQ 1775
Cdd:COG1193   603 EARKKLEELKQELEEKLEKPKKKAKP 628
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1692-1796 2.66e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1692 GSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLR---DEARGLLQAAQDKLQR----LQELEGTYEE 1764
Cdd:COG4372     5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQarseLEQLEEELEE 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564365344 1765 NERELEVKAAQLDGLEARMRSV-LQAINLQVQI 1796
Cdd:COG4372    85 LNEQLQAAQAELAQAQEELESLqEEAEELQEEL 117
PRK09039 PRK09039
peptidoglycan -binding protein;
1535-1750 2.89e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1535 SIEMVATRVLDISIPASPEQIQRLASEIAERVRSLA-------DVDTILAHTMGDVRRAEQL---LQ--DAQRARSRAEG 1602
Cdd:PRK09039   35 TVFVVAQFFLSREISGKDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQalLAELAGAGAAA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1603 ERQKAETVQA-ALEEAQRAQGAAQgairgavVDTKNteQTLQQVQERMAGTEQSLNSASERARQLHALLEALklkraGNS 1681
Cdd:PRK09039  115 EGRAGELAQElDSEKQVSARALAQ-------VELLN--QQIAALRRQLAALEAALDASEKRDRESQAKIADL-----GRR 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344 1682 LAASTAEETAGSAQSRArEAEKQLREQVGDQyQTVRALAER---KAEgVLAAQARAE-------QLRDEARGLLQAAQD 1750
Cdd:PRK09039  181 LNVALAQRVQELNRYRS-EFFGRLREILGDR-EGIRIVGDRfvfQSE-VLFPTGSAElnpegqaEIAKLAAALIELAKE 256
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 1456-1544 2.95e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 40.29  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1456 LGRA-RHTQAELQRALVEGGGILSRVSEtRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSqegadpD 1534
Cdd:PRK14473   58 LANAkRDYEAELAKARQEAAKIVAQAQE-RARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIA------D 130

                          90
                  ....*....|
gi 564365344 1535 SIEMVATRVL 1544
Cdd:PRK14473  131 LVTLTASRVL 140
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1478-1758 3.21e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.48  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1478 SRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ-EGADPDSIEMVATRVLDISIPASPEQIQ 1556
Cdd:PRK10246  304 AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEhDRFRQWNNELAGWRAQFSQQTSDREQLR 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1557 RLASEIAERVRSLADV-DTILAHTMGDVRRAEqllqdAQRARSRAegERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1635
Cdd:PRK10246  384 QWQQQLTHAEQKLNALpAITLTLTADEVAAAL-----AQHAEQRP--LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQ 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1636 KNTEQTLQQVQERMAGTEQSLNSAS---ERARQLHALLEALKLKRAGNS--LAASTAEETAGSAQSRAREAEKQLREQVg 1710
Cdd:PRK10246  457 TQRNAALNEMRQRYKEKTQQLADVKticEQEARIKDLEAQRAQLQAGQPcpLCGSTSHPAVEAYQALEPGVNQSRLDAL- 535

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564365344 1711 dqYQTVRALAERKAEGVLAAQARAEQLR---DEARGLLQAAQDKLQRLQEL 1758
Cdd:PRK10246  536 --EKEVKKLGEEGAALRGQLDALTKQLQrdeSEAQSLRQEEQALTQQWQAV 584
HrpE_YscL_not TIGR02499
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ...
 1563-1677 3.25e-03

type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274165 [Multi-domain]  Cd Length: 166  Bit Score: 40.36  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1563 AERVRSLADVDTILAHTmgdVRRAEQLLQDAQRarsraEGERQKAETVQAALEEAQRAQgAAQGAirGAVVDtknTEQTL 1642
Cdd:TIGR02499    6 AEDLAALAQAQAILAAA---RQRAEAILADAEE-----EAEASRQLGYEQGLEQFWQEA-AAQLA--EWQQE---AEQLE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 564365344  1643 QQVQERMAG-----TEQSLNSASERARQLHALLEALKLKR 1677
Cdd:TIGR02499   72 ASLEERLAElvlqaLEQILGEYDEPERLVRLLRQLLRAVA 111
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 1553-1674 3.33e-03

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


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 39.10  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1553 EQIQRL---ASEIAERVRSLADVDTilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgaiR 1629
Cdd:pfam18595    9 EELAELerkARELQAKIDALQVVEK-------DLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEIEL-------R 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 564365344  1630 GAVVDTKNTEQTLQQVQERMAGTEQslnSASERARQLHALLEALK 1674
Cdd:pfam18595   75 ELERREERLQRQLENAQEKLERLRE---QAEEKREAAQARLEELR 116
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1720-1788 3.51e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.41  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344 1720 AERKAEgvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKaaqldgLEARMRSVLQ 1788
Cdd:cd16269   196 KEKEIE---AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK------MEEERENLLK 255
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 309-341 3.64e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.95  E-value: 3.64e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 564365344   309 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 341
Cdd:pfam00053   16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1464-1616 4.17e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.98  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1464 AELQRALVEG-GGILSRVSETRRQAEEAQQ---RAQAALDKANASRGQVEQANQELRELIQNVkDFlsqegaDPDSIEMV 1539
Cdd:COG0497   229 QEALEALSGGeGGALDLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSL-EF------DPERLEEV 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1540 ATRVLDISIPA-----SPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA-----ET 1609
Cdd:COG0497   302 EERLALLRRLArkygvTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA---RKKAakkleKA 378


                  ....*..
gi 564365344 1610 VQAALEE 1616
Cdd:COG0497   379 VTAELAD 385
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
 1660-1792 4.31e-03

FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.


Pssm-ID: 428323 [Multi-domain]  Cd Length: 140  Bit Score: 39.27  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1660 SERARQLHALLEALKLKRA------GNSLAASTAEETAGSAQsrAREAEKQLReqvgdqyQTVRALAERKAEGVLAAQAR 1733
Cdd:pfam05130    8 EEELELLEELLELLEEEQEalkagdIEALEELTEEKQELLQK--LAQLEKERR-------ELLAELGLSPEEATLSELLA 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564365344  1734 AEQLRDEARGLLQAAQDKLQRLQELEgtyEENeRELevkaaqldgLEARMRSVLQAINL 1792
Cdd:pfam05130   79 KEEEDPELRELWQELLELLERLKELN---ELN-GEL---------IEQSLEFNNRSLNI 124
COG3899 COG3899
Predicted ATPase [General function prediction only];
1577-1784 4.98e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.77  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1577 AHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSL 1656
Cdd:COG3899   755 LYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALF 834

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1657 NSASERARQLHaLLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQ 1736
Cdd:COG3899   835 NLGFILHWLGP-LREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAAL 913

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 564365344 1737 LRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1784
Cdd:COG3899   914 AAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
 908-987 5.68e-03

Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.


Pssm-ID: 276911 [Multi-domain]  Cd Length: 142  Bit Score: 38.92  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  908 CERCIAGFHGDPRLPYGgqCRPC-PCPEGPGSQRHFATSCHRDgysqqIVCHCRAGYT-------GLRCEACAPGHFGDP 979
Cdd:cd13406    36 CSPCEPGFYNEAVNYEP--CKPCtQCNQRSGSEEKQKCTKTSD-----TVCRCRPGTQpldsykpGVDCVPCPPGHFSRG 108


                  ....*...
gi 564365344  980 SkpGGRCQ 987
Cdd:cd13406   109 D--NQACK 114
DUF1631 pfam07793
Protein of unknown function (DUF1631); The members of this family are sequences derived from a ...
 1476-1667 5.80e-03

Protein of unknown function (DUF1631); The members of this family are sequences derived from a group of hypothetical proteins expressed by certain bacterial species. The region concerned is approximately 440 amino acid residues in length.


Pssm-ID: 429661  Cd Length: 742  Bit Score: 41.54  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1476 ILSRVSETRRQAEEAQQRAQAAL---DKANASRGQVEqanQELRELIQN------VKDFLSQ------------EGAD-P 1533
Cdd:pfam07793  459 FEEFLERERRRAELAEQRTVDAAegrERLELARQQAA---DELEQRLAGrplpevVREFLRQawsdvlaltylrHGEDsE 535

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1534 DSIEMVAT------RVLDISIPASPEQIQRLASEIAERVRS-LADVdtilAHTMGDVRRAEQLLQDAQRARSRAEGERQK 1606
Cdd:pfam07793  536 EWQEALATaddlvwSVSPKPTAEERARLLALLPELLKRLRQgLASI----GYDPDESEAFFKELEALHAAAFRAKAAALA 611

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365344  1607 AETVQAALEEAQRAQGAaqgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSAS-ERARQLH 1667
Cdd:pfam07793  612 AALKAAAAKPAPAAAPA-------SPVEAEEEEALLGADAPPLAVVASPEDDAYlAQARALP 666
FUSC pfam04632
Fusaric acid resistance protein family; This family includes a conserved region found in two ...
 1531-1774 5.94e-03

Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.


Pssm-ID: 428044 [Multi-domain]  Cd Length: 655  Bit Score: 41.50  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1531 ADPDSIEMVA-TRVLDISI-------------PASPEQiqRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAQRA 1596
Cdd:pfam04632  118 ADPEAIFDIAvARVSEISLgilcaalvsalvfPRSVGP--ALRARLRARLRDAL-------------RLAAAALAGAPGA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1597 RSRAEGERQKAETVqAALEeAQRAQGAAQGA-IRGAVvdtknteQTLQQVQERMAgteqslnSASERARQLHALLEALkl 1675
Cdd:pfam04632  183 EAFEAARLRLAADI-LALE-ALRSHAAFESPrGRARA-------RALRRLLARML-------ALLPRLRSLARLLARL-- 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1676 kragnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQLRDEARGLLQAAQDKLQRL 1755
Cdd:pfam04632  245 -------RTEGAGTVPELAALLDELAAWEAALAAEALQAALAALRAR----LRALRPALPLDFDTAAELLARLADLLAEL 313

                          250
                   ....*....|....*....
gi 564365344  1756 QELEGTYEENERELEVKAA 1774
Cdd:pfam04632  314 AEALASCRALRHPIAQGAR 332
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1694-1774 7.26e-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: 39.00  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1694 AQSRAREAEKQLREqvgdqYQTVRALAERKAEGVLA-AQARAEQLRDEARgllQAAQDKLQRLQELegtyEENERELEVK 1772
Cdd:COG0711    43 AERAKEEAEAALAE-----YEEKLAEARAEAAEIIAeARKEAEAIAEEAK---AEAEAEAERIIAQ----AEAEIEQERA 110


                  ..
gi 564365344 1773 AA 1774
Cdd:COG0711   111 KA 112
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1634-1789 9.31e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.74  E-value: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1634 DTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALleALKLKRAGNSLAASTAEEtagsaqsrareaekqlREQVGDQY 1713
Cdd:cd00176    27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNEL--GEQLIEEGHPDAEEIQER----------------LEELNQRW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344 1714 QTVRALAERKAEGVLAAQARAEQLRD------------------EARGLLQAAQDKLQRLQELegtyeenERELEVKAAQ 1775
Cdd:cd00176    89 EELRELAEERRQRLEEALDLQQFFRDaddleqwleekeaalaseDLGKDLESVEELLKKHKEL-------EEELEAHEPR 161

                         170
                  ....*....|....
gi 564365344 1776 LDGLEARMRSVLQA 1789
Cdd:cd00176   162 LKSLNELAEELLEE 175
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 1620-1784 9.66e-03

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: 39.09  E-value: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1620 AQGAAQGAIrgAVVDTKNT--EQTLQQVQERMAgteqslnsasERARQlhallealklkragnslAASTAEET-AGSAQ- 1695
Cdd:pfam05335   10 AQKAAQEAK--AANDAQAAaaEAAARQVKNQLA----------DKALQ-----------------AAKAAEAAlAGKQQi 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365344  1696 -----SRAREAEKQLrEQVGDQYQTvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDklqRLQELEGTYEENERELE 1770
Cdd:pfam05335   61 veqleQELREAEAVV-QEESASLQQ----SQANANAAQRAAQQAQQQLEALTAALKAAQA---NLENAEQVAAGAQQELA 132

                          170
                   ....*....|....
gi 564365344  1771 VKAAQLDglEARMR 1784
Cdd:pfam05335  133 EKTQLLE--AAKKR 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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