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Conserved domains on  [gi|1958794731|ref|XP_038936810|]
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laminin subunit beta-2 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
2-150 8.81e-70

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 234.01  E-value: 8.81e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731    2 VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVVCESRYSEIE 79
Cdd:pfam00055   81 VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVICTSEYSDIS 159

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731   80 PSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVIRG 150
Cdd:pfam00055  160 PLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISVGG 230
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
 1596-1667 8.17e-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: 133.34  E-value: 8.17e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1596 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1667
Cdd:cd22299      1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1314-1659 1.09e-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: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1393
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1473
Cdd:COG1196    320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1553
Cdd:COG1196    378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1554 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1633
Cdd:COG1196    458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528

                          330       340
                   ....*....|....*....|....*.
gi 1958794731 1634 ELEVKAAQLDGLEARMRSVLQAINLQ 1659
Cdd:COG1196    529 LIGVEAAYEAALEAALAAALQNIVVE 554
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
652-697 3.64e-14

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.11  E-value: 3.64e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731   652 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 697
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1012-1059 2.15e-11

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.06  E-value: 2.15e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1012 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1059
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 390-431 2.55e-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: 60.06  E-value: 2.55e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958794731  390 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 431
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 279-336 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731  279 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 336
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.
 964-1012 1.38e-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: 1.38e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  964 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1012
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 700-748 3.59e-10

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 3.59e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  700 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 748
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 907-961 3.70e-10

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 3.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731  907 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 961
Cdd:pfam00053    1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 338-389 1.07e-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: 55.44  E-value: 1.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958794731  338 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 389
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.
 855-897 1.53e-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: 51.97  E-value: 1.53e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958794731  855 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 897
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.
 746-793 4.57e-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: 4.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731  746 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 793
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 795-853 3.61e-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: 45.42  E-value: 3.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731  795 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 853
Cdd:cd00055      1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 216-268 1.88e-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: 1.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731  216 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 268
Cdd:cd00055      2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 152-204 2.42e-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: 43.11  E-value: 2.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731  152 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 204
Cdd:cd00055      2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
2-150 8.81e-70

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 234.01  E-value: 8.81e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731    2 VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVVCESRYSEIE 79
Cdd:pfam00055   81 VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVICTSEYSDIS 159

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731   80 PSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVIRG 150
Cdd:pfam00055  160 PLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISVGG 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 2-150 1.04e-55

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: 194.12  E-value: 1.04e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731     2 VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR--WDDVVCESRYSEIE 79
Cdd:smart00136   88 VNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITKgnEDEVICTSEYSDIV 166

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731    80 PSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVIRG 150
Cdd:smart00136  167 PLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAVGG 238
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
 1596-1667 8.17e-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: 133.34  E-value: 8.17e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1596 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1667
Cdd:cd22299      1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1314-1659 1.09e-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: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1393
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1473
Cdd:COG1196    320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1553
Cdd:COG1196    378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1554 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1633
Cdd:COG1196    458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528

                          330       340
                   ....*....|....*....|....*.
gi 1958794731 1634 ELEVKAAQLDGLEARMRSVLQAINLQ 1659
Cdd:COG1196    529 LIGVEAAYEAALEAALAAALQNIVVE 554
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1331-1656 9.51e-17

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 86.63  E-value: 9.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1331 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1402
Cdd:PRK02224   210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1403 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1474
Cdd:PRK02224   290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1475 TVQAALEEAQRAQGAAQGAIR--------------GAVVDTKNTE-------QTLQQVQERMAGTEQSLNSASERARQLH 1533
Cdd:PRK02224   367 ELESELEEAREAVEDRREEIEeleeeieelrerfgDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1534 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1580
Cdd:PRK02224   447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1581 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEaRMRSVLQAI 1656
Cdd:PRK02224   527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1065-1662 3.84e-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: 3.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1065 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1142
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1143 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1220
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1221 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1280
Cdd:TIGR02168  518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1281 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1350
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1351 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1430
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1431 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK----NTEQ 1506
Cdd:TIGR02168  752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRE 824

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1507 TLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKQLreqvgdqyqtVRALA 1586
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--------------ELEELIEELESEL----------EALLN 880

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1587 ERKAegvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:TIGR02168  881 ERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
652-697 3.64e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.11  E-value: 3.64e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731   652 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 697
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 651-698 6.04e-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: 67.38  E-value: 6.04e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731  651 PCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGF--GPAGCQ 698
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 652-700 6.25e-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: 67.38  E-value: 6.25e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  652 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 700
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1314-1622 1.34e-13

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 76.40  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1380
Cdd:NF041483   478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1381 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDA- 1459
Cdd:NF041483   558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADAr 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 ---QRARSRA--EGERQKAE------TVQA-ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQvqERMAGTEQSLNSASE 1527
Cdd:NF041483   600 aeaERIRREAaeETERLRTEaaerirTLQAqAEQEAERLRTEAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQE 677

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1528 RARQLHALLEALKLK---RAGNSLAAST---------AEETAGSAQS-------RAREAEKQL----REQVGD-QYQTVR 1583
Cdd:NF041483   678 SADRVRAEAAAAAERvgtEAAEALAAAQeeaarrrreAEETLGSARAeadqereRAREQSEELlasaRKRVEEaQAEAQR 757

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1958794731 1584 ALAE---RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ 1622
Cdd:NF041483   758 LVEEadrRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
growth_prot_Scy NF041483
polarized growth protein Scy;
1312-1656 2.14e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 72.55  E-value: 2.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1312 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1390
Cdd:NF041483   909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1391 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1457
Cdd:NF041483   984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1458 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1520
Cdd:NF041483  1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1521 SLNsasERARQLHAllEALKlkRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AA 1596
Cdd:NF041483  1136 ELH---ERARRESA--EQMK--SAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAE 1204

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1597 QARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1656
Cdd:NF041483  1205 QKKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1012-1059 2.15e-11

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.06  E-value: 2.15e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1012 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1059
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
growth_prot_Scy NF041483
polarized growth protein Scy;
1324-1642 2.42e-11

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 69.08  E-value: 2.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1324 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1395
Cdd:NF041483   158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1396 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1473
Cdd:NF041483   234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 ETVQAALEEAQRAQGAAQGAIRGAvvdtknTEQTLQQVQERMAGTEqSLNSASERARQlHALLEALKL-KRAGNSLAAST 1552
Cdd:NF041483   287 EAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTVA 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1553 AEETAGSAQSRAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDE----ARGLLQAAQD--KLQRLQELE 1625
Cdd:NF041483   359 AEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE-EAERIRReAEAEADRLRGEaadqAEQLKGAAKDdtKEYRAKTVE 437

                          330
                   ....*....|....*..
gi 1958794731 1626 gtYEENERELEVKAAQL 1642
Cdd:NF041483   438 --LQEEARRLRGEAEQL 452
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 390-431 2.55e-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: 60.06  E-value: 2.55e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958794731  390 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 431
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
391-430 3.56e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.63  E-value: 3.56e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1958794731   391 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 430
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 1329-1650 4.62e-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: 67.85  E-value: 4.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1329 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1387
Cdd:pfam07111  354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1388 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1458
Cdd:pfam07111  434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1459 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1538
Cdd:pfam07111  508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1539 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1602
Cdd:pfam07111  562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1603 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1650
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.
 279-336 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731  279 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 336
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.
 964-1012 1.38e-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: 1.38e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  964 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1012
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1312-1636 2.23e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 66.00  E-value: 2.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1312 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1387
Cdd:NF041483   720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1388 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1466
Cdd:NF041483   787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1467 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1536
Cdd:NF041483   843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1537 --EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1614
Cdd:NF041483   923 tsEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002

                          330       340
                   ....*....|....*....|..
gi 1958794731 1615 QDKLQRLQelEGTYEENERELE 1636
Cdd:NF041483  1003 AAEAERLR--TEAREEADRTLD 1022
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1011-1060 2.56e-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: 2.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1011 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1060
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 700-748 3.59e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 3.59e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  700 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 748
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 907-961 3.70e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 3.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731  907 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 961
Cdd:pfam00053    1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1012-1056 9.24e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.40  E-value: 9.24e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731  1012 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1056
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 338-389 1.07e-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: 55.44  E-value: 1.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958794731  338 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 389
Cdd:cd00055      1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 906-962 1.15e-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: 55.44  E-value: 1.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731  906 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 962
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.
 339-393 1.50e-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: 55.05  E-value: 1.50e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731  339 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 393
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1422-1644 2.95e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 62.15  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1484
Cdd:NF041483   130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1485 RAQGAAQGAIRGAVVDTknteqtlqqvqERMagteqsLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSR 1563
Cdd:NF041483   204 SARAEAEAILRRARKDA-----------ERL------LNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQR 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1564 AREAEKQLREqvgdqyqtvralaerkaegvlaAQARAEQLRDEARgllqaaQDKLQRLQELEGTYEENERELEVKAAQLD 1643
Cdd:NF041483   267 MQEAEEALRE----------------------ARAEAEKVVAEAK------EAAAKQLASAESANEQRTRTAKEEIARLV 318


                   .
gi 1958794731 1644 G 1644
Cdd:NF041483   319 G 319
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 278-337 2.96e-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: 54.28  E-value: 2.96e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  278 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 337
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.
 391-430 3.48e-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: 53.90  E-value: 3.48e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958794731  391 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 430
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
964-1009 4.42e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 4.42e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731   964 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1009
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 963-1010 5.17e-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: 53.51  E-value: 5.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731  963 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1010
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
907-961 1.04e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.70  E-value: 1.04e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731   907 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 961
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.
 855-897 1.53e-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: 51.97  E-value: 1.53e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958794731  855 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 897
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 699-741 3.96e-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: 3.96e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958794731  699 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 741
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
700-741 6.34e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.39  E-value: 6.34e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958794731   700 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 741
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
growth_prot_Scy NF041483
polarized growth protein Scy;
1420-1636 8.64e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.53  E-value: 8.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1420 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1493
Cdd:NF041483    44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1494 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRArEAEK---Q 1570
Cdd:NF041483   121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARA-EAERlaeE 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1571 LREQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQEL 1624
Cdd:NF041483   194 ARQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEA 270

                          250
                   ....*....|..
gi 1958794731 1625 EGTYEENERELE 1636
Cdd:NF041483   271 EEALREARAEAE 282
growth_prot_Scy NF041483
polarized growth protein Scy;
1325-1655 9.40e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.14  E-value: 9.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1325 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1399
Cdd:NF041483   252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1464
Cdd:NF041483   326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1465 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1516
Cdd:NF041483   401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1517 GTEQSLNSASERARQLH--ALLEALKLkRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKA---- 1590
Cdd:NF041483   481 TAEELLTKAKADADELRstATAESERV-RTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArelr 559

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1591 -EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSvLQA 1655
Cdd:NF041483   560 eETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT-LQA 629
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 855-901 1.09e-07

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.66  E-value: 1.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958794731  855 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 901
Cdd:cd00055      2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
279-336 1.14e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.62  E-value: 1.14e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731   279 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 336
Cdd:smart00180    1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
339-382 1.20e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.62  E-value: 1.20e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958794731   339 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 382
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.
 746-793 4.57e-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: 4.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731  746 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 793
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 745-790 6.73e-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: 47.35  E-value: 6.73e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  745 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 790
Cdd:cd00055      1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
855-897 3.57e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 45.38  E-value: 3.57e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958794731   855 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 897
Cdd:smart00180    1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 795-853 3.61e-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: 45.42  E-value: 3.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731  795 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 853
Cdd:cd00055      1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1342-1613 1.54e-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: 1.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1342 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1419
Cdd:smart00283    2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1420 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRArsraeGERQK-----AETVQaAL 1480
Cdd:smart00283   75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARA-----GEAGRgfavvADEVR-KL 138

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1481 eeAQRAQGAAqgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTaEETAGSA 1560
Cdd:smart00283  139 --AERSAESA-----------KEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE--ETGDALEEIVDSV-EEIADLV 202

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731  1561 QSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1613
Cdd:smart00283  203 QEIAAATDEQAAgsEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 216-268 1.88e-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: 1.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731  216 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 268
Cdd:cd00055      2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 216-267 2.02e-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: 2.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731  216 CECNGH---SHSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 267
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.
 822-852 2.10e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.10e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958794731  822 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 852
Cdd:pfam00053   19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 152-204 2.42e-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: 43.11  E-value: 2.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731  152 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 204
Cdd:cd00055      2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 1550-1661 4.15e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 45.70  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1550 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELE 1625
Cdd:PRK14475    36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958794731 1626 GTYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1661
Cdd:PRK14475   115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
796-845 4.28e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 42.30  E-value: 4.28e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958794731   796 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 845
Cdd:smart00180    1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1562-1657 8.78e-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: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1562 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKL----QRLQELEGTYEENERELE 1636
Cdd:COG4913    238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312

                           90       100
                   ....*....|....*....|.
gi 1958794731 1637 VKAAQLDGLEARMRSVLQAIN 1657
Cdd:COG4913    313 RLEARLDALREELDELEAQIR 333
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 1451-1486 2.88e-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: 2.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1486
Cdd:NF040598    37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1335-1622 4.37e-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: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1335 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1414
Cdd:NF012221  1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1415 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1491
Cdd:NF012221  1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1492 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALL---EALKLKRAGNSLA----------ASTAEET 1556
Cdd:NF012221  1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1557 AGSAQSRAR-----EAEKQLREQV------GDQYqTVRALAER----KAEGVLAAQAR-AEQLRDEARGLLQAAQDKLQR 1620
Cdd:NF012221  1762 ANQAQADAKgakqdESDKPNRQGAagsglsGKAY-SVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNR 1840


                   ..
gi 1958794731 1621 LQ 1622
Cdd:NF012221  1841 LQ 1842
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 1437-1636 4.41e-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: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1437 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1516
Cdd:cd07596      1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1517 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKQlREQVGDQYQTV-------RALAE 1587
Cdd:cd07596     71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDD-RADALLTLQSLkkdlaskKAQLE 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1588 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1636
Cdd:cd07596    135 KLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
746-785 4.76e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 4.76e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958794731   746 CVCNGR---ADECDAHTGACLgCRDYTGGEHCERCIAGFHGDP 785
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
216-269 1.49e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 1.49e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731   216 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 269
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 ...
 1586-1662 2.05e-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: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1586 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1657
Cdd:pfam00430   42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121


                   ....*
gi 1958794731 1658 LQVQI 1662
Cdd:pfam00430  122 LAVQI 126
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 175-207 3.79e-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: 3.79e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958794731  175 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 207
Cdd:pfam00053   16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
2-150 8.81e-70

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 234.01  E-value: 8.81e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731    2 VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFpGIPLAPPRRW--DDVVCESRYSEIE 79
Cdd:pfam00055   81 VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIkdDEVICTSEYSDIS 159

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731   80 PSTEGEVIYRVL--DPAIPIPDpYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIReKYYYALYELVIRG 150
Cdd:pfam00055  160 PLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISVGG 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 2-150 1.04e-55

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: 194.12  E-value: 1.04e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731     2 VTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSaDFGRTWRVYRYFSYDCGADFPGIPLAPPRR--WDDVVCESRYSEIE 79
Cdd:smart00136   88 VNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITKgnEDEVICTSEYSDIV 166

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731    80 PSTEGEVIYRVLDPAIPIPD-PYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVIRG 150
Cdd:smart00136  167 PLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAVGG 238
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
 1596-1667 8.17e-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: 133.34  E-value: 8.17e-37
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1596 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1667
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 ...
 1597-1666 2.29e-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: 2.29e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1597 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1666
Cdd:cd22295      1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1314-1659 1.09e-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: 1.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEGGgiLSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1393
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 QEGadpdsiemvatrvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1473
Cdd:COG1196    320 ELE----------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1553
Cdd:COG1196    378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1554 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKaegvLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTyeeneR 1633
Cdd:COG1196    458 EEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-----V 528

                          330       340
                   ....*....|....*....|....*.
gi 1958794731 1634 ELEVKAAQLDGLEARMRSVLQAINLQ 1659
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 ...
 1596-1666 1.07e-21

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: 90.23  E-value: 1.07e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1596 AQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1666
Cdd:cd22300      2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1318-1648 2.22e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 101.55  E-value: 2.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1318 ADLALGRARHTQAELQRAlvegggilsrvSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLSQEga 1397
Cdd:COG1196    227 AELLLLKLRELEAELEEL-----------EAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEE-- 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1398 dpdsiemvatRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1477
Cdd:COG1196    291 ----------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1478 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETA 1557
Cdd:COG1196    361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1558 GSAQSRAREAEKQLREQvgdQYQTVRALAERKAEgvlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERelEV 1637
Cdd:COG1196    441 EEALEEAAEEEAELEEE---EEALLELLAELLEE-----AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE--GV 510

                          330
                   ....*....|.
gi 1958794731 1638 KAAQLDGLEAR 1648
Cdd:COG1196    511 KAALLLAGLRG 521
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1420-1656 7.62e-20

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 96.54  E-value: 7.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1420 QIQRLA--SEIAERVRSLADVDTILAHTM---------GDVRRAEQLLQDAQRARSRAEGERQKAET----VQAALEEAQ 1484
Cdd:COG1196    201 QLEPLErqAEKAERYRELKEELKELEAELlllklreleAELEELEAELEELEAELEELEAELAELEAeleeLRLELEELE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1485 RAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA 1564
Cdd:COG1196    281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1565 REAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDG 1644
Cdd:COG1196    361 AEAEEALLEAEAELAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                          250
                   ....*....|..
gi 1958794731 1645 LEARMRSVLQAI 1656
Cdd:COG1196    440 EEEALEEAAEEE 451
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1358-1660 1.26e-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: 1.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1358 QRAQAALDKANASRGQVEQANQELRELIQNVKdflsqegadpdsIEMVA-TRVLDISIPA-SPEQIQRLASEIAErvrsl 1435
Cdd:COG3206     97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLT------------VEPVKgSNVIEISYTSpDPELAAAVANALAE----- 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1436 ADVDTILAHTMGDVRRAEQLLQDaqrarsRAEGERQKAETVQAALEEAQRAQGAAqgairgavvdtkNTEQTLQQVQERM 1515
Cdd:COG3206    160 AYLEQNLELRREEARKALEFLEE------QLPELRKELEEAEAALEEFRQKNGLV------------DLSEEAKLLLQQL 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1516 AGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAE-----KQLREQVGDQYQTVRALAERKA 1590
Cdd:COG3206    222 SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEleaelAELSARYTPNHPDVIALRAQIA 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1591 E-----------GVLAAQARAEQLR---DEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1656
Cdd:COG3206    302 AlraqlqqeaqrILASLEAELEALQareASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381


                   ....
gi 1958794731 1657 NLQV 1660
Cdd:COG3206    382 ALTV 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1314-1621 3.85e-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: 3.85e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELRELIQNVKDFLS 1393
Cdd:COG1196    275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 QEGADPDSIEMVATRVLDISipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1473
Cdd:COG1196    352 ELEEAEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 EtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTA 1553
Cdd:COG1196    427 E---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1554 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRL 1621
Cdd:COG1196    504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1331-1656 9.51e-17

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 86.63  E-value: 9.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1331 ELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV------KDFLSQEGADPDSI-- 1402
Cdd:PRK02224   210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaetereREELAEEVRDLRERle 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1403 -------EMVATRVL-DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDvrrAEQLLQDAQRARSRAEGERQKAE 1474
Cdd:PRK02224   290 eleeerdDLLAEAGLdDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE---AESLREDADDLEERAEELREEAA 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1475 TVQAALEEAQRAQGAAQGAIR--------------GAVVDTKNTE-------QTLQQVQERMAGTEQSLNSASERARQLH 1533
Cdd:PRK02224   367 ELESELEEAREAVEDRREEIEeleeeieelrerfgDAPVDLGNAEdfleelrEERDELREREAELEATLRTARERVEEAE 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1534 ALLEALKLKRAGNSLAASTAEETAGSAQSR---------------------------AREAEKQL------REQVGDQYQ 1580
Cdd:PRK02224   447 ALLEAGKCPECGQPVEGSPHVETIEEDRERveeleaeledleeeveeveerleraedLVEAEDRIerleerREDLEELIA 526

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1581 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEaRMRSVLQAI 1656
Cdd:PRK02224   527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAI 601
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1111-1655 1.22e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.14  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1111 QAIVAARNTSAASTAKLVEAtEGLRHEIGKTTERLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDIL 1190
Cdd:COG1196    208 QAEKAERYRELKEELKELEA-ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1191 KHSNFLGAYDSIRHAHSQSTEAERRANAstfaipspvsnsADTRRRAEvlmgAQRENFNRQHLANQQALGRLSThthtls 1270
Cdd:COG1196    287 QAEEYELLAELARLEQDIARLEERRREL------------EERLEELE----EELAELEEELEELEEELEELEE------ 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1271 ltgvnelvcgapgdapcatspcggagcrdedgqprcgglgcsgAAATADLALGRARHTQAELQRALVEgggILSRVSETR 1350
Cdd:COG1196    345 -------------------------------------------ELEEAEEELEEAEAELAEAEEALLE---AEAELAEAE 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1351 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASpEQIQRLASEIAE 1430
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEE 457

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1431 RVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQG-AAQGAIRGAVVDTKNTEQTLQ 1509
Cdd:COG1196    458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYE 537

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1510 QVQE-RMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER 1588
Cdd:COG1196    538 AALEaALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1589 KAEGV------------LAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1655
Cdd:COG1196    616 YVLGDtllgrtlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1430-1648 1.84e-16

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 85.74  E-value: 1.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1430 ERVRSLADVDTILAHtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGA-IRGAVVDTKNTEQTL 1508
Cdd:COG4913    219 EEPDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAEL 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1509 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQT-VRAL-- 1585
Cdd:COG4913    298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----REIERLERELEERERRRARLEAlLAALgl 373

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794731 1586 -AERKAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENERELEVKAAQLDGLEAR 1648
Cdd:COG4913    374 pLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1065-1662 3.84e-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: 3.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1065 DWDRVVQDLAARTRRLEQwaQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAK--LVEATEGLRHEIGKTT 1142
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLEL--QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1143 ERLTQLEAELTDVQDENFNANHALSGLERDglalnltLRQLDQHLDILKH--SNFLGAYDSIRhahsqsteaERRANAST 1220
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERE-------LAQLQARLDSLERlqENLEGFSEGVK---------ALLKNQSG 517

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1221 FA-IPSPVSN--SADTRRRA--EVLMGAQR-----ENFNR-----QHLAnQQALGR-----LSTHTHTLSLTGVNELVCG 1280
Cdd:TIGR02168  518 LSgILGVLSEliSVDEGYEAaiEAALGGRLqavvvENLNAakkaiAFLK-QNELGRvtflpLDSIKGTEIQGNDREILKN 596

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1281 APGDAPCATSPCGGAGCRDEDGQPRCGGLGC--SGAAATADLALGRARHTQAELQRALVEGGGILSRVS--------ETR 1350
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssilERR 676

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1351 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEgaDPDSIEMVATRvldISIPASPEQIQRLASEIAE 1430
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALR---KDLARLEAEVEQLEERIAQ 751

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1431 RVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTK----NTEQ 1506
Cdd:TIGR02168  752 LSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaaNLRE 824

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1507 TLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaastaeetagSAQSRAREAEKQLreqvgdqyqtVRALA 1586
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--------------ELEELIEELESEL----------EALLN 880

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1587 ERKAegvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:TIGR02168  881 ERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1065-1657 4.05e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.14  E-value: 4.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1065 DWDRVVQDLAARTRRLEQWAQELQQT-GVLGAFESSFLNLQgklgmvQAIVAARNTSAASTAKLVEATEGLRHEigktTE 1143
Cdd:COG1196    240 ELEELEAELEELEAELEELEAELAELeAELEELRLELEELE------LELEEAQAEEYELLAELARLEQDIARL----EE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1144 RLTQLEAELTDVQDENFNANHALSGLERDGLALNLTLRQLDQHLDILKH--SNFLGAYDSIRHAHSQSTEAERRANASTF 1221
Cdd:COG1196    310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELAEAEEELEELAEELL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1222 AIpspVSNSADTRRRAEVLMGAQRENFNRQHLANQQALGRLSTHTHTLSLtgvnelvcgapgdapcatspcggagcRDED 1301
Cdd:COG1196    390 EA---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------------------------EEEE 440

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1302 GQprcgglgcsgAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQEL 1381
Cdd:COG1196    441 EE----------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1382 RELIQNVKDF-LSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVD-----TILAHTMGDVRRAEQL 1455
Cdd:COG1196    511 KAALLLAGLRgLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagraTFLPLDKIRARAALAA 590

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1456 LQDA---QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMA----------GTEQSL 1522
Cdd:COG1196    591 ALARgaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltgGSRREL 670

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1523 NSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAA 1596
Cdd:COG1196    671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREElleellEEEELLEE 750

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1597 QARAEQLRDEARGLLQAAQDKLQR------------LQELEgtyEENER--ELEvkaAQLDGLEARMRSVLQAIN 1657
Cdd:COG1196    751 EALEELPEPPDLEELERELERLEReiealgpvnllaIEEYE---ELEERydFLS---EQREDLEEARETLEEAIE 819
cc_DmLAMB1-like_C cd22302
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ...
 1597-1666 7.58e-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: 7.58e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1597 QARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1666
Cdd:cd22302      1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
652-697 3.64e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.11  E-value: 3.64e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731   652 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGC 697
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1070-1657 4.35e-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: 4.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1070 VQDLAARTRRLEQWAQELQQTGVLGAFESSFLNLQGKLGMVQAIVAARNTSAASTAKLVEATEGLRHEIGKTTERLTQLE 1149
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1150 AELTDVQD-------------ENFNANHALSGL-----------ERDGLALNLTLRQLDQHL------------DILKHS 1193
Cdd:TIGR02168  489 ARLDSLERlqenlegfsegvkALLKNQSGLSGIlgvlselisvdEGYEAAIEAALGGRLQAVvvenlnaakkaiAFLKQN 568

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1194 N-----FLgAYDSIRHAHSQSTEAERRANASTFAipSPVSNSADTRRRAEVLMGAQrenFNR----QHLANQQALGRLST 1264
Cdd:TIGR02168  569 ElgrvtFL-PLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKFDPKLRKALSYL---LGGvlvvDDLDNALELAKKLR 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1265 HTHTL-SLTGvnELV--CG--APGDAPCATspcgGAGCRD---EDGQPRCGGLGcsGAAATADLALGRARHTQAELQ--- 1333
Cdd:TIGR02168  643 PGYRIvTLDG--DLVrpGGviTGGSAKTNS----SILERRreiEELEEKIEELE--EKIAELEKALAELRKELEELEeel 714

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1334 -----------RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASR----GQVEQANQELRELIQNVKDFlsQEGAD 1398
Cdd:TIGR02168  715 eqlrkeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEEL--EAQIE 792

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1399 PDSIEMVATRvldisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvqA 1478
Cdd:TIGR02168  793 QLKEELKALR----------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---A 859

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1479 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAG 1558
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-------QLELRLE 932

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1559 SAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRdeargllqaaqDKLQRL--------QELEgtyEE 1630
Cdd:TIGR02168  933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE-----------NKIKELgpvnlaaiEEYE---EL 998

                          650       660
                   ....*....|....*....|....*..
gi 1958794731 1631 NEReLEVKAAQLDGLEARMRSVLQAIN 1657
Cdd:TIGR02168  999 KER-YDFLTAQKEDLTEAKETLEEAIE 1024
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 651-698 6.04e-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: 67.38  E-value: 6.04e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731  651 PCQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGF--GPAGCQ 698
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 652-700 6.25e-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: 67.38  E-value: 6.25e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  652 CQCDPQGSLSSECNPHGGQCRCKPGVVGRRCDACATGYYGFGPAGCQAC 700
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1314-1622 1.34e-13

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 76.40  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQR-ALVEGGGI----LSRVSETRRQAEEAQQRAQA--------ALDKANASRGQVEQANQE 1380
Cdd:NF041483   478 AARTAEELLTKAKADADELRStATAESERVrteaIERATTLRRQAEETLERTRAeaerlraeAEEQAEEVRAAAERAARE 557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1381 LREliqnvkdflsqegadpDSIEMVATRVLDisipaSPEQIQRLASEIAERVRSladvdtilahtmgdvrrAEQLLQDA- 1459
Cdd:NF041483   558 LRE----------------ETERAIAARQAE-----AAEELTRLHTEAEERLTA-----------------AEEALADAr 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 ---QRARSRA--EGERQKAE------TVQA-ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQvqERMAGTEQSLNSASE 1527
Cdd:NF041483   600 aeaERIRREAaeETERLRTEaaerirTLQAqAEQEAERLRTEAAADASAARAEGENVAVRLRS--EAAAEAERLKSEAQE 677

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1528 RARQLHALLEALKLK---RAGNSLAAST---------AEETAGSAQS-------RAREAEKQL----REQVGD-QYQTVR 1583
Cdd:NF041483   678 SADRVRAEAAAAAERvgtEAAEALAAAQeeaarrrreAEETLGSARAeadqereRAREQSEELlasaRKRVEEaQAEAQR 757

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1958794731 1584 ALAE---RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ 1622
Cdd:NF041483   758 LVEEadrRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1343-1658 1.39e-13

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 75.96  E-value: 1.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQ 1422
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLL-----QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgA 1497
Cdd:COG4717    153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-Q 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1498 VVDTKNTEQTLQQVQERM------------AGTEQSLNSASERARQLHALLEAL------KLKRAGNSLAASTAEETAGS 1559
Cdd:COG4717    232 LENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALP 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1560 AQSRAREAE-KQLREQVG--------------DQYQTVRALAERKAEgvLAAQARAEQLRDEARGLLQAAQ----DKLQR 1620
Cdd:COG4717    312 ALEELEEEElEELLAALGlppdlspeellellDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAGvedeEELRA 389

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1958794731 1621 LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINL 1658
Cdd:COG4717    390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1306-1602 1.54e-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: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1306 CGGLGCSGAAATADLALGRARHTQAELQRALVEgggILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELI 1385
Cdd:COG3883      2 LALALAAPTPAFADPQIQAKQKELSELQAELEA---AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1386 QNVKD----------FLSQEGADPDSIEMVATrvldisipaspeqiqrlASEIAERVRSLADVDTILAHTMGDVRRAEQL 1455
Cdd:COG3883     79 AEIEErreelgerarALYRSGGSVSYLDVLLG-----------------SESFSDFLDRLSALSKIADADADLLEELKAD 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1456 LQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlhal 1535
Cdd:COG3883    142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA---- 217

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731 1536 lEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQ 1602
Cdd:COG3883    218 -AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1322-1655 1.58e-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: 1.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1322 LGRARHTQAELQRALVEGGGILSRVSETRRQAE-------EAQQRAQ----AALDKANASRGQVEQANQELRELIQNVKD 1390
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkEKREYEGyellKEKEALERQKEAIERQLASLEEELEKLTE 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1391 FLSQEGADPDSIEmvatRVLDisipASPEQIQRLASEIAERVRS-LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGE 1469
Cdd:TIGR02169  259 EISELEKRLEEIE----QLLE----ELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1470 RQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL----QQVQERMAGTEQSLNSASERarqlhalLEALKLKRag 1545
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraelEEVDKEFAETRDELKDYREK-------LEKLKREI-- 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1546 NSLAAStaeetagsaQSRAREAEKQLREQVGDqyqtVRALAERKAEGVLAAQARAEQLRDE---ARGLLQAAQDKL---- 1618
Cdd:TIGR02169  402 NELKRE---------LDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEikkQEWKLEQLAADLskye 468

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1958794731 1619 QRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQA 1655
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
mukB PRK04863
chromosome partition protein MukB;
1315-1662 2.42e-13

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 75.76  E-value: 2.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1315 AATADLALGRARHtQAELQRALVEGGGILSRVSETRRQAEEAQQRA---QAALDKANASRGQVEQANQELRELIQNVKDF 1391
Cdd:PRK04863   265 ESTNYVAADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAASDHLNLVQTA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1392 LSQEGAdpdsIEMVATRVLDISIPA-SPEQIQRLASEIAERVRSLA-----DVDTiLAHTMGDVRRAEQLLQdaqrarSR 1465
Cdd:PRK04863   344 LRQQEK----IERYQADLEELEERLeEQNEVVEEADEQQEENEARAeaaeeEVDE-LKSQLADYQQALDVQQ------TR 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1466 AeGERQKAetvQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQlHAllEALKLKRag 1545
Cdd:PRK04863   413 A-IQYQQA---VQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ-FE--QAYQLVR-- 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1546 nSLAASTAEETAgsaQSRAREAEKQLREQ--VGDQYQTVRA-LAErkAEGVLAAQARAEQLRDEArglLQAAQDKLQRLQ 1622
Cdd:PRK04863   484 -KIAGEVSRSEA---WDVARELLRRLREQrhLAEQLQQLRMrLSE--LEQRLRQQQRAERLLAEF---CKRLGKNLDDED 554

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1958794731 1623 ELEGTYEENERELEVKAAQLDGLEARmRSVLQAINLQVQI 1662
Cdd:PRK04863   555 ELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQA 593
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1318-1650 8.23e-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: 73.83  E-value: 8.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1318 ADLALGRARhtQAELQRALVEGGGILSRVSETRRQAEEAQQ-----RAQAAL-------DKANASRGQVEQANQELRELI 1385
Cdd:COG3096    836 AELAALRQR--RSELERELAQHRAQEQQLRQQLDQLKEQLQllnklLPQANLladetlaDRLEELREELDAAQEAQAFIQ 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1386 QN------VKDFLSQEGADPDSIEMVATRVLDISipASPEQIQRLA---SEIAERVRSLA--DVDTILAHTMGDVRRAEQ 1454
Cdd:COG3096    914 QHgkalaqLEPLVAVLQSDPEQFEQLQADYLQAK--EQQRRLKQQIfalSEVVQRRPHFSyeDAVGLLGENSDLNEKLRA 991

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1455 LLQDAQRARSRAegeRQKAETVQAALEEAQRAQGAAQGAIrgavvDTKNteQTLQQVQERMAGTEQSLNS-ASERAR--- 1530
Cdd:COG3096    992 RLEQAEEARREA---REQLRQAQAQYSQYNQVLASLKSSR-----DAKQ--QTLQELEQELEELGVQADAeAEERARirr 1061

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1531 -QLHALLEALKLKRagNSLAASTA--EETAGSAQSRAREAEK---QLREQV---GDQYQTVRALA-ERKAEGVLA----A 1596
Cdd:COG3096   1062 dELHEELSQNRSRR--SQLEKQLTrcEAEMDSLQKRLRKAERdykQEREQVvqaKAGWCAVLRLArDNDVERRLHrrelA 1139

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1597 QARAEQLR---DEARGLLQAAQDKLQRLQELEGTYEEN---ERELEVKAAQLDGLEARMR 1650
Cdd:COG3096   1140 YLSADELRsmsDKALGALRLAVADNEHLRDALRLSEDPrrpERKVQFYIAVYQHLRERIR 1199
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1324-1657 8.38e-13

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 73.26  E-value: 8.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1324 RARHTQAELQRALVEGG-GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVkdflsQEGADPDSI 1402
Cdd:COG4717    171 ELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1403 EMVATRVLDISIPASpeqIQRLASEIAERVRSLADVDTI---LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtvQAA 1479
Cdd:COG4717    246 KEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLvlgLLALLFLLLAREKASLGKEAEELQALPALEELE--EEE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1480 LEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsaseRARQLHALLEALkLKRAGnslaaSTAEETAGS 1559
Cdd:COG4717    321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAAL-LAEAG-----VEDEEELRA 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1560 AQSRAREAEK------QLREQVGDQYQTVRALAERKAEGVLAAQ-ARAEQLRDEARGLLQAAQDKL----QRLQELE--G 1626
Cdd:COG4717    390 ALEQAEEYQElkeeleELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELaeleAELEQLEedG 469

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1958794731 1627 TYEENERELEVKAAQLDGLE---ARMRSVLQAIN 1657
Cdd:COG4717    470 ELAELLQELEELKAELRELAeewAALKLALELLE 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1442-1656 1.37e-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: 1.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1442 LAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtKNTEQTLQQVQERMAGTEQS 1521
Cdd:COG1196    181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKL------RELEAELEELEAELEELEAE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1522 LNSASERARQLHALLEALKLKRagnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAE 1601
Cdd:COG1196    255 LEELEAELAELEAELEELRLEL-----------EELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLE 319

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1602 QLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1656
Cdd:COG1196    320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1321-1655 1.50e-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: 73.06  E-value: 1.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1321 ALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA--------------QAALDKANASRGQVEQANQELREliq 1386
Cdd:COG3096    348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAeeevdslksqladyQQALDVQQTRAIQYQQAVQALEK--- 424

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1387 nvkdflSQE--GADPDSIEMVATRVldisipaspEQIQRLASEIAERVRSLadvdtilahtmgdvrraEQLLQDAQRARS 1464
Cdd:COG3096    425 ------ARAlcGLPDLTPENAEDYL---------AAFRAKEQQATEEVLEL-----------------EQKLSVADAARR 472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1465 R------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERA 1529
Cdd:COG3096    473 QfekayelvckiaGEVERSQAwQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1530 RQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGDQYQTVRAlaerKAEGVLAAQARAEQLRDEARG 1609
Cdd:COG3096    553 EELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQL-EQLRARIKELAA----RAPAWLAAQDALERLREQSGE 620

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1610 LLQAAQDKLQRLQELegtyEENERELEVK----AAQLDGLEARMRSVLQA 1655
Cdd:COG3096    621 ALADSQEVTAAMQQL----LEREREATVErdelAARKQALESQIERLSQP 666
growth_prot_Scy NF041483
polarized growth protein Scy;
1312-1656 2.14e-12

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 72.55  E-value: 2.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1312 SGAAATADLALGRARHTQAELQRALVEGGGILsrVSETRRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNvkd 1390
Cdd:NF041483   909 SDAAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAAAQAEQLIAeATGEAERLRAEAAETVGS--- 983

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1391 flSQEGADPDSIEmvATRVLDiSIPASPEQIQRLASEIAERV-----------RSLA--DVDTILAHTMGDvrrAEQLLQ 1457
Cdd:NF041483   984 --AQQHAERIRTE--AERVKA-EAAAEAERLRTEAREEADRTldearkdankrRSEAaeQADTLITEAAAE---ADQLTA 1055

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1458 DAQRA--RSRAEGERQKAETVQAALEEAQR--AQGAAQGAIR-------------GAVVDTKNTEQTLQQVQERMAGTEQ 1520
Cdd:NF041483  1056 KAQEEalRTTTEAEAQADTMVGAARKEAERivAEATVEGNSLvekartdadellvGARRDATAIRERAEELRDRITGEIE 1135

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1521 SLNsasERARQLHAllEALKlkRAGNSLAA--STAEETAGSAQSRAreaeKQLREQVGDQYQTVRALAERKAEGVL--AA 1596
Cdd:NF041483  1136 ELH---ERARRESA--EQMK--SAGERCDAlvKAAEEQLAEAEAKA----KELVSDANSEASKVRIAAVKKAEGLLkeAE 1204

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1597 QARAEQLRdeargllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA---RMRSVLQAI 1656
Cdd:NF041483  1205 QKKAELVR-------EAEKIKAEAEAEAKRTVEEGKRELDVLVRRREDINAeisRVQDVLEAL 1260
mukB PRK04863
chromosome partition protein MukB;
1315-1644 2.80e-12

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 72.30  E-value: 2.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1315 AATADLALGR-ARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFls 1393
Cdd:PRK04863   332 AASDHLNLVQtALRQQEKIERYQAD-------LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADY-- 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 QEGadpdsIEMVATRVLdisipaspeQIQRlASEIAERVRSLADVDTILAHTMGD---------------VRRAEQLLQD 1458
Cdd:PRK04863   403 QQA-----LDVQQTRAI---------QYQQ-AVQALERAKQLCGLPDLTADNAEDwleefqakeqeateeLLSLEQKLSV 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1459 AQRARSR------------AEGERQKA-ETVQAALEEA--QRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLN 1523
Cdd:PRK04863   468 AQAAHSQfeqayqlvrkiaGEVSRSEAwDVARELLRRLreQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLG 547

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1524 SASERARQLHALLEALKLKRAGNSLAASTAEETagsaqsraREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQL 1603
Cdd:PRK04863   548 KNLDDEDELEQLQEELEARLESLSESVSEARER--------RMALRQQLEQLQARIQRLAARAPA----WLAAQDALARL 615

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1604 RD-------EARGLLQAAQDKLQRLQELEgtyeENERELEVKAAQLDG 1644
Cdd:PRK04863   616 REqsgeefeDSQDVTEYMQQLLERERELT----VERDELAARKQALDE 659
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1316-1645 3.53e-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: 3.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1316 ATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALdkaNASRGQVEQANQELRELIQNVKDflsqe 1395
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLAN----- 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1396 gadpdsiemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLqdaqrarSRAEGERQKAET 1475
Cdd:TIGR02168  314 --------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1476 VQAALEEAQRAQgaaqgaiRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAGNSLAAstaee 1555
Cdd:TIGR02168  373 RLEELEEQLETL-------RSKVAQLELQIASLNNEIERL---EARLERLEDRRERLQQEIEELLKKLEEAELKE----- 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1556 tagsAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARglLQAAQDKLQRLQELEGTYEENEREL 1635
Cdd:TIGR02168  438 ----LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ--LQARLDSLERLQENLEGFSEGVKAL 511

                          330
                   ....*....|
gi 1958794731 1636 EVKAAQLDGL 1645
Cdd:TIGR02168  512 LKNQSGLSGI 521
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1419-1624 4.60e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 71.48  E-value: 4.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRLASEIAERVRSLADVDTILAhtMGDVRRAEQLLQDAQRARSRAEGERQKAEtvqAALEEAQRAQGAAQGAIRGAV 1498
Cdd:COG4913    255 EPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLE---AELERLEARLDALREELDELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1499 VD-TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGN--SLAA--STAEETAGSAQSRAREAEKQLRE 1573
Cdd:COG4913    330 AQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeEFAAlrAEAAALLEALEEELEALEEALAE 409

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731 1574 QVGDQYQTVRALAERKAE-GVLAAQ-----ARAEQLRDEARGLLQAAQDKLQRLQEL 1624
Cdd:COG4913    410 AEAALRDLRRELRELEAEiASLERRksnipARLLALRDALAEALGLDEAELPFVGEL 466
mukB PRK04863
chromosome partition protein MukB;
1329-1624 1.03e-11

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 70.37  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1329 QAELQRALVEGGGilSRVSETRRQAEEAQQRA----------QAALDKANASRGQVEQANQELRE----------LIQNV 1388
Cdd:PRK04863   363 RLEEQNEVVEEAD--EQQEENEARAEAAEEEVdelksqladyQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNA 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1389 KDFLSQEGADPDSiemVATRVLDIsipaspEQIQRLASEIAER-------VRSLAD-VDTILAHtmgdvRRAEQLLQDA- 1459
Cdd:PRK04863   441 EDWLEEFQAKEQE---ATEELLSL------EQKLSVAQAAHSQfeqayqlVRKIAGeVSRSEAW-----DVARELLRRLr 506

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 -QRARS-RAEGERQKAETVQAALEEAQRAQGAAQGAIR--GAVVDTKNTEQTLQQVQE-RMAGTEQSLNSASERARQLHA 1534
Cdd:PRK04863   507 eQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlGKNLDDEDELEQLQEELEaRLESLSESVSEARERRMALRQ 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1535 LLEALKLKRAGNslaasTAEETAGSAqsrAREAEKQLREQVGDQY---QTVRALAERKAEGVLAAQ-------ARAEQLR 1604
Cdd:PRK04863   587 QLEQLQARIQRL-----AARAPAWLA---AQDALARLREQSGEEFedsQDVTEYMQQLLERERELTverdelaARKQALD 658

                          330       340
                   ....*....|....*....|
gi 1958794731 1605 DEARGLLQAAQDKLQRLQEL 1624
Cdd:PRK04863   659 EEIERLSQPGGSEDPRLNAL 678
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1450-1664 1.20e-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: 1.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1450 RRAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG-------- 1517
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerqleel 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1518 ------TEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAE 1591
Cdd:TIGR02168  322 eaqleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1592 GVLA------AQARAEQLRDEARGLLQAAQDklQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1664
Cdd:TIGR02168  402 IERLearlerLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1322-1664 1.77e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 68.00  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1322 LGRARhtqAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANAsrgQVEQANQELreliQNVKDFLSQegadpds 1401
Cdd:COG4372      8 VGKAR---LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREEL----EQLEEELEQ------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1402 iemvatrvldisipaSPEQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQRARSRAEGERQKaetVQAALE 1481
Cdd:COG4372     71 ---------------ARSELEQLEEELEELNEQLQAAQAELA-------QAQEELESLQEEAEELQEELEE---LQKERQ 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1482 EAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLnsasERARQLHALLEALKLKRAGNSLaASTAEETAGSAQ 1561
Cdd:COG4372    126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL----AALEQELQALSEAEAEQALDEL-LKEANRNAEKEE 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1562 SRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1641
Cdd:COG4372    201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280

                          330       340
                   ....*....|....*....|...
gi 1958794731 1642 LDGLEARMRSVLQAINLQVQIYN 1664
Cdd:COG4372    281 AALELEALEEAALELKLLALLLN 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1415-1648 1.97e-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: 1.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1415 PASPEQIQRLASEIAERVRSLADVdtilahtMGDVRRAEQLLQDAQRARSRAEgerQKAETVQAALEEAQRAQGAAQGAI 1494
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSL-------QSELRRIENRLDELSQELSDAS---RKIGEIEKEIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1495 RGAVVDTKNTEQTLQQVQERMAGTEQSLnsaSERARQLHALLEALklkragNSLAASTAEETAGSAQSRAREAEKQLREQ 1574
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARI---EELEEDLHKLEEAL------NDLEARLSHSRIPEIQAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1575 VGdqyqTVRALaERKAEGVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELEGTYEENERELEVKAAQLDGLEAR 1648
Cdd:TIGR02169  811 EA----RLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLESR 883
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1012-1059 2.15e-11

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.06  E-value: 2.15e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1012 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGvFPACHPC 1059
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQ 47
growth_prot_Scy NF041483
polarized growth protein Scy;
1324-1642 2.42e-11

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 69.08  E-value: 2.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1324 RARhTQAELQRALVEG-----GGILSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELR---ELIQNVKDFLSQE 1395
Cdd:NF041483   158 RAR-TESQARRLLDESraeaeQALAAARAEAERLAEEARQRLGS---EAESARAEAEAILRRARkdaERLLNAASTQAQE 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1396 GADpdsiemvATRVLDISIPASPEQIQRLASEIAervrsladvdtilahtmgdvRRAEQLLQDAQRA--RSRAEGERQKA 1473
Cdd:NF041483   234 ATD-------HAEQLRSSTAAESDQARRQAAELS--------------------RAAEQRMQEAEEAlrEARAEAEKVVA 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 ETVQAALEEAQRAQGAAQGAIRGAvvdtknTEQTLQQVQERMAGTEqSLNSASERARQlHALLEALKL-KRAGNSLAAST 1552
Cdd:NF041483   287 EAKEAAAKQLASAESANEQRTRTA------KEEIARLVGEATKEAE-ALKAEAEQALA-DARAEAEKLvAEAAEKARTVA 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1553 AEETAGSAQSRAREAEKQLREQVGDQYQTVRALAErKAEGVLA-AQARAEQLRDE----ARGLLQAAQD--KLQRLQELE 1625
Cdd:NF041483   359 AEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE-EAERIRReAEAEADRLRGEaadqAEQLKGAAKDdtKEYRAKTVE 437

                          330
                   ....*....|....*..
gi 1958794731 1626 gtYEENERELEVKAAQL 1642
Cdd:NF041483   438 --LQEEARRLRGEAEQL 452
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 390-431 2.55e-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: 60.06  E-value: 2.55e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958794731  390 PCDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFRP 431
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
391-430 3.56e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.63  E-value: 3.56e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1958794731   391 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 430
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 1329-1650 4.62e-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: 67.85  E-value: 4.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1329 QAELQRAL--------VEGGGI------LSRVSETRRQAEE----AQQRAQAALDKANASRGQVEQANQELREL---IQN 1387
Cdd:pfam07111  354 QAILQRALqdkaaeveVERMSAkglqmeLSRAQEARRRQQQqtasAEEQLKFVVNAMSSTQIWLETTMTRVEQAvarIPS 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1388 VKDFLSQEGADPDSIEMVATRVLDISipaspeQIQRLASEIAERVRSL-ADVDTILAHTMGDVRR--------AEQLLQD 1458
Cdd:pfam07111  434 LSNRLSYAVRKVHTIKGLMARKVALA------QLRQESCPPPPPAPPVdADLSLELEQLREERNRldaelqlsAHLIQQE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1459 AQRARSRAEGERQKAETVQAALeeaqraqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSAseRARQLHALLEA 1538
Cdd:pfam07111  508 VGRAREQGEAERQQLSEVAQQL------------------------EQELQRAQESLASVGQQLEVA--RQGQQESTEEA 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1539 LKLKRagnslAASTAEETAGSA-QSRAREAEKQLREQVGDqyqTVRALAERKAEGVLAA------QARAEQ--------- 1602
Cdd:pfam07111  562 ASLRQ-----ELTQQQEIYGQAlQEKVAEVETRLREQLSD---TKRRLNEARREQAKAVvslrqiQHRATQekernqelr 633

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1603 -LRDEARGllQAAQDKLQRLQELegtyeENERELEVKAAQLDGLEARMR 1650
Cdd:pfam07111  634 rLQDEARK--EEGQRLARRVQEL-----ERDKNLMLATLQQEGLLSRYK 675
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
1314-1663 6.34e-11

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


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 66.21  E-value: 6.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQR----ALVEGGGIlsrvsetRRQAEEAQQRAQAAldkanasrgqVEQANQELRELIQNV- 1388
Cdd:COG1538     17 RAARARVEAARAQLRQARAGLlpsqELDLGGKR-------RARIEAAKAQAEAA----------EADLRAARLDLAAEVa 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1389 KDFLSQEGADpdsiemvatRVLDISipaspEQIQRLASEIAERVRSLADVDTIlahTMGDVRRAEQLLQDAQRARSRAEG 1468
Cdd:COG1538     80 QAYFDLLAAQ---------EQLALA-----EENLALAEELLELARARYEAGLA---SRLDVLQAEAQLAQARAQLAQAEA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1469 ERQKAEtvqAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAserARQLHALLEALKLKRAGN-- 1546
Cdd:COG1538    143 QLAQAR---NALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAA---EAQLEAAEAEIGVARAAFlp 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1547 --SLAASTAEE------------------------TAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARA 1600
Cdd:COG1538    217 slSLSASYGYSssddlfsggsdtwsvglslslplfDGGRNRARVRAAKAQLEQAE-AQYEQTVLQALQEVEDALAALRAA 295

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731 1601 EQLRDEARGLLQAAQDKLQRLQELegtYEENERE-LEVKAAQLDGLEARMRSV---LQAINLQVQIY 1663
Cdd:COG1538    296 REQLEALEEALEAAEEALELARAR---YRAGLASlLDVLDAQRELLQAQLNLIqarYDYLLALVQLY 359
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1330-1654 6.35e-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: 67.51  E-value: 6.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1330 AELQRALVEgggILSRVSETRRQ---AEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGAD-------- 1398
Cdd:pfam01576  218 TDLQEQIAE---LQAQIAELRAQlakKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqr 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1399 ---PDSIEMVATRVLDI--SIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRR---------AEQLLQdAQRARS 1464
Cdd:pfam01576  295 rdlGEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQkhtqaleelTEQLEQ-AKRNKA 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1465 RAEGERQKAETVQAAL-EEAQRAQGAAQGAIRGavvdTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL---- 1539
Cdd:pfam01576  374 NLEKAKQALESENAELqAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssll 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1540 -----KLKRAGNSLAASTA----------EET----AGSAQSRAREAEKQ-LREQVGDQYQTVRALaERKAEGVLAAQAR 1599
Cdd:pfam01576  450 neaegKNIKLSKDVSSLESqlqdtqellqEETrqklNLSTRLRQLEDERNsLQEQLEEEEEAKRNV-ERQLSTLQAQLSD 528

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1600 AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyeenERELEVKAAQLDGLEaRMRSVLQ 1654
Cdd:pfam01576  529 MKKKLEEDAGTLEALEEGKKRLQrELEAL----TQQLEEKAAAYDKLE-KTKNRLQ 579
PTZ00121 PTZ00121
MAEBL; Provisional
 1324-1641 9.74e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 9.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1324 RARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE 1403
Cdd:PTZ00121  1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1404 mVATRVLDisipASPEQIQRLASEI--AERVRSLADVDTI-LAHTMGDVRRAEQlLQDAQRARsRAEgERQKAETVQAAL 1480
Cdd:PTZ00121  1168 -EARKAED----AKKAEAARKAEEVrkAEELRKAEDARKAeAARKAEEERKAEE-ARKAEDAK-KAE-AVKKAEEAKKDA 1239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1481 EEAQRAQgaaqgAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSA 1560
Cdd:PTZ00121  1240 EEAKKAE-----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA 1314

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1561 QsRAREAEKQlREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQ-DKLQRLQELEGTYEENERELEVKA 1639
Cdd:PTZ00121  1315 K-KADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKADAAKKKAEEKKK 1392


                   ..
gi 1958794731 1640 AQ 1641
Cdd:PTZ00121  1393 AD 1394
PTZ00121 PTZ00121
MAEBL; Provisional
 1343-1642 1.06e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 1.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisiPASPEQIQ 1422
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEE-----------AKKADEAK 1450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLLQDAQRARsRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVD 1500
Cdd:PTZ00121  1451 KKAEEAkkAEEAKKKAE----------EAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1501 TKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRA---REAEKQLREQVGD 1577
Cdd:PTZ00121  1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeeaKKAEEARIEEVMK 1599

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731 1578 QYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYE--ENERELEVKAAQL 1642
Cdd:PTZ00121  1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEE 1666
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 279-336 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        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731  279 CDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLSASNPRGC 336
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.
 964-1012 1.38e-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: 1.38e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  964 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQCRAC 1012
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
growth_prot_Scy NF041483
polarized growth protein Scy;
1312-1636 2.23e-10

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 66.00  E-value: 2.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1312 SGAAATADLALGRARHTQAELqralvegggilsrVSETRRQAEEAQQRAQAALDKANASRGQV----EQANQELRELIQN 1387
Cdd:NF041483   720 GSARAEADQERERAREQSEEL-------------LASARKRVEEAQAEAQRLVEEADRRATELvsaaEQTAQQVRDSVAG 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1388 VKDFLSQEGADPDSI-EMVATRVldisipaspeqiQRLASEIAERVRSLADVDTilahtmgdvrraEQLLQDAQRARSRA 1466
Cdd:NF041483   787 LQEQAEEEIAGLRSAaEHAAERT------------RTEAQEEADRVRSDAYAER------------ERASEDANRLRREA 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1467 EGERQKAE-----TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQ--VQERMAGTEQSLNSASERARQLHALL--- 1536
Cdd:NF041483   843 QEETEAAKalaerTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQdaARTRADAREDANRIRSDAAAQADRLIgea 922

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1537 --EALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1614
Cdd:NF041483   923 tsEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEA 1002

                          330       340
                   ....*....|....*....|..
gi 1958794731 1615 QDKLQRLQelEGTYEENERELE 1636
Cdd:NF041483  1003 AAEAERLR--TEAREEADRTLD 1022
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1011-1060 2.56e-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: 2.56e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1011 ACDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGVFPACHPCH 1060
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1314-1615 2.72e-10

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 65.04  E-value: 2.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLAlGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDfls 1393
Cdd:COG0840    273 AASAEELA-AGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE--- 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 qegadpdsiemVATRVLDISipASPEQIqrlaSEIaervrsladVDTIlahtmGDVrrAEQ--LLqdaqrarsraegerq 1471
Cdd:COG0840    349 -----------TAETIEELG--ESSQEI----GEI---------VDVI-----DDI--AEQtnLL--------------- 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1472 kaetvqaALE---EAQRA--QGaaqgaiRG-AVV-D------------TKNTEQTLQQVQERMAGTEQSLNSASERARQL 1532
Cdd:COG0840    381 -------ALNaaiEAARAgeAG------RGfAVVaDevrklaersaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEG 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1533 HALLEalklkRAGNSLA--ASTAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEAR 1608
Cdd:COG0840    448 VELVE-----EAGEALEeiVEAVEEVSDLIQEIAAASEEQSAgtEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAE 522


                   ....*..
gi 1958794731 1609 GLLQAAQ 1615
Cdd:COG0840    523 ELQELVS 529
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1309-1565 2.74e-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: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1309 LGCSGAAATADlalgRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNV 1388
Cdd:COG4942     10 LLALAAAAQAD----AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1389 KDFLSQEGADPDSIE----MVATRVLDISIPASPEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRA 1462
Cdd:COG4942     86 AELEKEIAELRAELEaqkeELAELLRALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1463 RSRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLK 1542
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

                          250       260
                   ....*....|....*....|...
gi 1958794731 1543 ragnslAASTAEETAGSAQSRAR 1565
Cdd:COG4942    236 ------AAAAAERTPAAGFAALK 252
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1456-1651 3.09e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 65.17  E-value: 3.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1456 LQDAQRARSRAEGerQKAETVQAALEEAQRAQGAAQGAIRgavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHAL 1535
Cdd:COG4717     51 LEKEADELFKPQG--RKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1536 LEALKLKRAGNSLAASTAEEtagsaQSRAREAEKQLRE--QVGDQYQTVRA-LAERKAEGVLAAQARAEQLRDEARGLLQ 1612
Cdd:COG4717    125 LQLLPLYQELEALEAELAEL-----PERLEELEERLEElrELEEELEELEAeLAELQEELEELLEQLSLATEEELQDLAE 199

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958794731 1613 AAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1651
Cdd:COG4717    200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1344-1650 3.32e-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: 65.36  E-value: 3.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1344 SRVSETRRQAEE-AQQRAQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-I 1421
Cdd:COG3096    785 KRLEELRAERDElAEQYAKASFDV------------QKLQRLHQAFSQFVGGH--------------LAVAFAPDPEAeL 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 QRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRAQG--AAQGAi 1494
Cdd:COG3096    839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQEAQAfiQQHGK- 917

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1495 RGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK--LKR--------AGNSLAASTAE--------ET 1556
Cdd:COG3096    918 ALAQLEPL--VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevVQRrphfsyedAVGLLGENSDLneklrarlEQ 995

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1557 AGSAQSRAREAEKQLREQVgDQY---------------QTVRALAERKAE-GVLA---AQARAEQLRDEARGLLQAAQdk 1617
Cdd:COG3096    996 AEEARREAREQLRQAQAQY-SQYnqvlaslkssrdakqQTLQELEQELEElGVQAdaeAEERARIRRDELHEELSQNR-- 1072

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1958794731 1618 lQRLQELEGTYEENERElevkaaqLDGLEARMR 1650
Cdd:COG3096   1073 -SRRSQLEKQLTRCEAE-------MDSLQKRLR 1097
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 700-748 3.59e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 3.59e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  700 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFPNCRPCVC 748
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1314-1655 3.65e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 65.32  E-value: 3.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEgggiLSRVSETRRQAEEAQQRAQAALDKANASR-----GQVEQANQELRELIQNV 1388
Cdd:COG4913    286 AQRRLELLEAELEELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRleqleREIERLERELEERERRR 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1389 KDFlsqegadpdsieMVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEG 1468
Cdd:COG4913    362 ARL------------EALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEA 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1469 ER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRGA------------------- 1497
Cdd:COG4913    427 EIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGFaltllvppehyaaalrwvn 506

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1498 --------------------------------VVDTKN---------------------TEQTLQQV------------- 1511
Cdd:COG4913    507 rlhlrgrlvyervrtglpdperprldpdslagKLDFKPhpfrawleaelgrrfdyvcvdSPEELRRHpraitragqvkgn 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1512 -----------------------------QERMAGTEQSLNSASERARQLHALLEAL-KLKRAGNSLAASTAEET-AGSA 1560
Cdd:COG4913    587 gtrhekddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEALEAELDALqERREALQRLAEYSWDEIdVASA 666

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1561 QSRAREAEKQLR---------EQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTY 1628
Cdd:COG4913    667 EREIAELEAELErldassddlAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                          490       500
                   ....*....|....*....|....*..
gi 1958794731 1629 EENERELEVKAAQLDGLEARMRSVLQA 1655
Cdd:COG4913    747 LRALLEERFAAALGDAVERELRENLEE 773
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 907-961 3.70e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 56.59  E-value: 3.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731  907 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNF--TSGRGC 961
Cdd:pfam00053    1 CDCNPHGSLSD--------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1324-1658 4.24e-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: 4.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1324 RARHTQAELQRALvegGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFLSQegadpd 1400
Cdd:TIGR02169  678 RLRERLEGLKREL---SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeekLKERLEELEEDLSS------ 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1401 siemvatrvLDISIPASPEQIQRLASEIAERVRSLADVDTILAhtmgDVRR--AEQLLQDAQRARSRAEGERQKAEtvqA 1478
Cdd:TIGR02169  749 ---------LEQEIENVKSELKELEARIEELEEDLHKLEEALN----DLEArlSHSRIPEIQAELSKLEEEVSRIE---A 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1479 ALEEAQRAQGAAQgairgavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG 1558
Cdd:TIGR02169  813 RLREIEQKLNRLT-------LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1559 SAQSRAREAEKQLREQvGDQYQTVRALAERKAEGVLAAQARAEQLRDEarglLQAAQDKLQRLQElegtYEENERELEVK 1638
Cdd:TIGR02169  886 DLKKERDELEAQLREL-ERKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEE----IPEEELSLEDV 956

                          330       340
                   ....*....|....*....|
gi 1958794731 1639 AAQLDGLEARMRSvLQAINL 1658
Cdd:TIGR02169  957 QAELQRVEEEIRA-LEPVNM 975
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1450-1661 4.39e-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: 4.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1450 RRAEQLLQdaQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAvvdtkntEQtlQQVQERMAGTEQSLNSASERA 1529
Cdd:COG3064      8 KAAEAAAQ--ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQA-------EE--EAREAKAEAEQRAAELAAEAA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1530 RQLhalleaLKLKRAGNSLAASTAEETAgsaqSRAREAEKQLREQVGDQYQTVRALAE--RKAEGvlAAQARAEQLRDEA 1607
Cdd:COG3064     77 KKL------AEAEKAAAEAEKKAAAEKA----KAAKEAEAAAAAEKAAAAAEKEKAEEakRKAEE--EAKRKAEEERKAA 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958794731 1608 RGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1661
Cdd:COG3064    145 EAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1300-1648 4.63e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.68  E-value: 4.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1300 EDGQPRCGGLGCSGAAATADLALGRARHTQAELQRALVEgggilSRVSETRRQAEEAQQRAQAALDKANASRG---QVEQ 1376
Cdd:PRK02224   282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELE-----DRDEELRDRLEECRVAAQAHNEEAESLREdadDLEE 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1377 ANQELREL-------IQN----VKDFLSQEGADPDSIEMVATRVLDIsiPASPEQIQRLASEIAE---RVRS-LADVDTI 1441
Cdd:PRK02224   357 RAEELREEaaeleseLEEareaVEDRREEIEELEEEIEELRERFGDA--PVDLGNAEDFLEELREerdELRErEAELEAT 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1442 LAHTMGDVRRAEQLLQ---------------------DAQRARSRAEGERQKAETVQAALEEA-QRAQGAAQGAIRgavV 1499
Cdd:PRK02224   435 LRTARERVEEAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERlERAEDLVEAEDR---I 511

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1500 DTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQL-------- 1571
Cdd:PRK02224   512 ERL--EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaelkerie 589

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1572 -----------REQVGDQYQTVR----ALAE--------------RKAE--------GVLAAQA---RAEQLRDEARGLL 1611
Cdd:PRK02224   590 slerirtllaaIADAEDEIERLRekreALAElnderrerlaekreRKREleaefdeaRIEEAREdkeRAEEYLEQVEEKL 669

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1958794731 1612 QAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEAR 1648
Cdd:PRK02224   670 DELREERDDLQAEIGAVENELEELEELRERREALENR 706
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1315-1661 5.80e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 64.55  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1315 AATADLALGRARHTQAELQRALVEgggilsrvsETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdfLSQ 1394
Cdd:COG4913    271 LAELEYLRAALRLWFAQRRLELLE---------AELEELRAELARLEAELERL---EARLDALREELDELEAQI---RGN 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1395 EGADPDSIE--------------------MVATRVLDISIPASPEQIQRLASEIAERvrsLADVDTILAHTMGDVRRAEQ 1454
Cdd:COG4913    336 GGDRLEQLEreierlereleererrrarlEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEA 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1455 LLQDAQRARSRAEGER-----------QKAETVQAALEEA---------------------QRAQGAAQGAIRG------ 1496
Cdd:COG4913    413 ALRDLRRELRELEAEIaslerrksnipARLLALRDALAEAlgldeaelpfvgelievrpeeERWRGAIERVLGGfaltll 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1497 ----------AVVDTKNTEQTLQ--------QVQERMAGTEQSL--------NSASERARQL------HALLEALK-LKR 1543
Cdd:COG4913    493 vppehyaaalRWVNRLHLRGRLVyervrtglPDPERPRLDPDSLagkldfkpHPFRAWLEAElgrrfdYVCVDSPEeLRR 572

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1544 AGNSLAAS---------------------------------TAEETAGSAQSRAREAEKQLR--EQVGDQYQTVRALAER 1588
Cdd:COG4913    573 HPRAITRAgqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEalEAELDALQERREALQR 652

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1589 KAE------GVLAAQARAEQLRDEaRGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1661
Cdd:COG4913    653 LAEyswdeiDVASAEREIAELEAE-LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1448-1645 5.93e-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: 5.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1448 DVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT-------------KNTEQTLQQVQER 1514
Cdd:pfam12795   21 DLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEIlaslsleeleqrlLQTSAQLQELQNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1515 MAGTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETA-GSAQSRAREAEKQLREQVGDQYQ------TVR-A 1584
Cdd:pfam12795  101 LAQLNSQLIELQTRPERAQQQLSEARqrLQQIRNRLNGPAPPGEPlSEAQRWALQAELAALKAQIDMLEqellsnNNRqD 180

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1585 LAERKAEgvlAAQARAEQLRDEARgLLQAAQDKlQRLQELEGTYEENERELEVKAAQLDGL 1645
Cdd:pfam12795  181 LLKARRD---LLTLRIQRLEQQLQ-ALQELLNE-KRLQEAEQAVAQTEQLAEEAAGDHPLV 236
PTZ00121 PTZ00121
MAEBL; Provisional
 1343-1654 7.73e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 7.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQE---LRELIQNVKDFL--SQEGADPDSIEMVATRvldisipAS 1417
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEAeaAEEKAEAAEKKKEEAK-------KK 1379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1418 PEQIQRLASEI--AERVRSLADVDTILAHtmgDVRRAEQLLQDAQRARSRAEgERQKAETVQAALEEAQRAQGAAQGAir 1495
Cdd:PTZ00121  1380 ADAAKKKAEEKkkADEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKA-- 1453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1496 gavvDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSL-----AASTAEETAGSAQSR----ARE 1566
Cdd:PTZ00121  1454 ----EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaaeAKKKADEAKKAEEAKkadeAKK 1529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1567 AEKQLREQVGDQYQTVRALAE-RKAEGVLAAQA--------RAEQLRDEA-RGLLQAAQDKLQRLQELEGTYEEN----- 1631
Cdd:PTZ00121  1530 AEEAKKADEAKKAEEKKKADElKKAEELKKAEEkkkaeeakKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYEEEkkmka 1609

                          330       340
                   ....*....|....*....|....*...
gi 1958794731 1632 -----ERELEVKAAQLDGLEARMRSVLQ 1654
Cdd:PTZ00121  1610 eeakkAEEAKIKAEELKKAEEEKKKVEQ 1637
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 1328-1647 8.18e-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: 62.78  E-value: 8.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1328 TQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGADPDSIEMVAT 1407
Cdd:pfam19220   39 ILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE--AEAAKEELRIELRDK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1408 RvldisipASPEQIQRLASEIAERVRSLADvdtilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQ 1487
Cdd:pfam19220  117 T-------AQAEALERQLAAETEQNRALEE----------ENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1488 gaaqgairgavvdTKNTEQTLQQVQE---RMAGTEQSLNSASERARQLHAllealklkragnSLAASTAEetagsaqsRA 1564
Cdd:pfam19220  180 -------------QALSEEQAAELAEltrRLAELETQLDATRARLRALEG------------QLAAEQAE--------RE 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1565 ReAEKQLREQVGdQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLqaaQDKLQRLQELEGTYEENERELEVKAAQLDG 1644
Cdd:pfam19220  227 R-AEAQLEEAVE-AHRAERASLRMKLEALTARAAATEQLLAEARNQL---RDRDEAIRAAERRLKEASIERDTLERRLAG 301


                   ...
gi 1958794731 1645 LEA 1647
Cdd:pfam19220  302 LEA 304
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1065-1661 9.11e-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: 63.83  E-value: 9.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1065 DWDRVVQDLAARTRRLeqwAQELQQTGVLGAFESSFLNLQGKLGMVQAiVAARNTSAASTAKLVEATEGLRHEIgktTER 1144
Cdd:TIGR00618  308 QAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHTL---TQH 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1145 LTQLEAELTDVQDENFNANHALSGLERD-GLALNLTLRQLDQHLDILkhsnflgaydsirHAHSQSTEAERRANASTFAI 1223
Cdd:TIGR00618  381 IHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLA-------------HAKKQQELQQRYAELCAAAI 447

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1224 pSPVSNSADTRRRAEVLMgAQRENFNRQHLANQQALGRLSTHTHTLSLTGVNELvcgapgdapcATSPCggagcrdedgq 1303
Cdd:TIGR00618  448 -TCTAQCEKLEKIHLQES-AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL----------QEEPC----------- 504

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1304 PRCGGLGCSGAAATADLALG-------RARHTQAELQRALV----EGGGILSRVSETRRQAEEAQQRAQAALDKANASRG 1372
Cdd:TIGR00618  505 PLCGSCIHPNPARQDIDNPGpltrrmqRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1373 QVEQanqeLRELIQNVKDFLSQEGADPDSIEMVATRVLdisIPASPEQ-IQRLASEIAERVRSLADVDTILAhtmgdvRR 1451
Cdd:TIGR00618  585 DIPN----LQNITVRLQDLTEKLSEAEDMLACEQHALL---RKLQPEQdLQDVRLHLQQCSQELALKLTALH------AL 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1452 AEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQGAAQGairgavvdtknTEQTLQQVQERMAGTEQSLNSASERA 1529
Cdd:TIGR00618  652 QLTLTQERVREHALSirVLPKELLASRQLALQKMQSEKEQLTY-----------WKEMLAQCQTLLRELETHIEEYDREF 720

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1530 RQLHALLEALKLKRAGNSlaaSTAEETAGSAQsraREAEKQLREQVGDQyqtvralaERKAEGVLAAQARaeqlrdearg 1609
Cdd:TIGR00618  721 NEIENASSSLGSDLAARE---DALNQSLKELM---HQARTVLKARTEAH--------FNNNEEVTAALQT---------- 776

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1610 llqaaqdkLQRLQELEGTYEENERELEVKAAQLDGLEARMR----SVLQAINLQVQ 1661
Cdd:TIGR00618  777 --------GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCE 824
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1012-1056 9.24e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.40  E-value: 9.24e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731  1012 CDCDPRGIDKPQCHRSTGHCSCRPGVSGVRCDQCARGFSGV-FPAC 1056
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 338-389 1.07e-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: 55.44  E-value: 1.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958794731  338 RCQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLLGCR 389
Cdd:cd00055      1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PTZ00121 PTZ00121
MAEBL; Provisional
 1345-1638 1.11e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1345 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEmvatrvldisipaspeqiQRL 1424
Cdd:PTZ00121  1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE------------------ARK 1279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1425 ASEI--AERVRSLADvdtilAHTMGDVRRAEQLLQDAQRARS------RAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1496
Cdd:PTZ00121  1280 ADELkkAEEKKKADE-----AKKAEEKKKADEAKKKAEEAKKadeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1497 AVVDTKNTEQTLQQVQERmagTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE-ETAGSAQSRAREAEKQLREQV 1575
Cdd:PTZ00121  1355 AADEAEAAEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKK 1431

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1576 GDQYQTVRALAERKAEgvlAAQARAEQLRdEARGLLQAAQDKlQRLQELEGTYEENERELEVK 1638
Cdd:PTZ00121  1432 KADEAKKKAEEAKKAD---EAKKKAEEAK-KAEEAKKKAEEA-KKADEAKKKAEEAKKADEAK 1489
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 906-962 1.15e-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: 55.44  E-value: 1.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731  906 RCTCNLLGTDPQRCpstdlchcDPSTGQCPCLPHVQGLSCDRCAPNFWNFTS-GRGCQ 962
Cdd:cd00055      1 PCDCNGHGSLSGQC--------DPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
1313-1662 1.26e-09

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


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 63.00  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1313 GAAATADLALGRARHTQAELQRALVegggILSRVSETRRQAEEAQ--QRA------QAALDKANASRGQVEQANQELREL 1384
Cdd:COG5278     23 VLGVLSYLSLNRLREASEWVEHTYE----VLRALEELLSALLDAEtgQRGylltgdESFLEPYEEARAEIDELLAELRSL 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1385 IQNvkdflsqegadpdsiemvatrvldisipaSPEQIQRLAS--EIAERVRSLADvDTILAHTMGDVRRAEQLLQ----- 1457
Cdd:COG5278     99 TAD-----------------------------NPEQQARLDEleALIDQWLAELE-QVIALRRAGGLEAALALVRsgegk 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1458 ---DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1534
Cdd:COG5278    149 almDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1535 LLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAA 1614
Cdd:COG5278    229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1615 QDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:COG5278    309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 339-393 1.50e-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: 55.05  E-value: 1.50e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731  339 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLSHDLlgcrPCDC 393
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1320-1641 1.65e-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: 62.22  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1320 LALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAAldkanasRGQVEQANQELRELIQNVKDFLSQEGADP 1399
Cdd:pfam07888   24 LVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD-------REQWERQRRELESRVAELKEELRQSREKH 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARsRAEGERQKAET---- 1475
Cdd:pfam07888   97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK-KAGAQRKEEEAerkq 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1476 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRagNSLAAS--TA 1553
Cdd:pfam07888  176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ--ERLNASerKV 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1554 E------ETAGSAQSRAREAEKQLREQVGDqyqtvraLAERKAEGVLAAQARAEQLRDEARGLLQAAQ---DKLQRL--- 1621
Cdd:pfam07888  254 EglgeelSSMAAQRDRTQAELHQARLQAAQ-------LTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLsae 326

                          330       340
                   ....*....|....*....|....
gi 1958794731 1622 -QELEGTYEEN--ERE-LEVKAAQ 1641
Cdd:pfam07888  327 lQRLEERLQEErmEREkLEVELGR 350
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1321-1655 1.71e-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: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1321 ALGRARHTQA-ELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQV--------------EQANQELRELI 1385
Cdd:pfam01576  629 AEAREKETRAlSLARALEE-------ALEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskralEQQVEEMKTQL 701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1386 QNVKDFLsQEGADpdsiemvATRVLDISIPASPEQIQRLAS---EIAE-RVRSLADvdtilahtmgDVRRAEQLLQDAQR 1461
Cdd:pfam01576  702 EELEDEL-QATED-------AKLRLEVNMQALKAQFERDLQardEQGEeKRRQLVK----------QVRELEAELEDERK 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1462 ARSRAEGERQKAET-------------------------VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQ------- 1509
Cdd:pfam01576  764 QRAQAVAAKKKLELdlkeleaqidaankgreeavkqlkkLQAQMKDLQRELEEARASRDEILAQSKESEKKLKnleaell 843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1510 QVQERMAgteqslnsASERARQlHALLEALKLKragNSLAASTAEETAGSAQSRAREAE-KQLREQVGDQYQTVRALAER 1588
Cdd:pfam01576  844 QLQEDLA--------ASERARR-QAQQERDELA---DEIASGASGKSALQDEKRRLEARiAQLEEELEEEQSNTELLNDR 911

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1589 KAEGV---------LAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGT----YEENERELEVKAAQL-DGLEARMRSVL 1653
Cdd:pfam01576  912 LRKSTlqveqltteLAAERSTSQKSESARQQLERQNKELKaKLQEMEGTvkskFKSSIAALEAKIAQLeEQLEQESRERQ 991


                   ..
gi 1958794731 1654 QA 1655
Cdd:pfam01576  992 AA 993
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1450-1658 1.84e-09

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 61.70  E-value: 1.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1450 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERA 1529
Cdd:COG4942     27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------ALEQELAALEAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1530 RQLHALLEAL--KLKRAGNS------LAASTAEETAGSAQ-----SRAREAE-KQLREQVGDQYQTVRALAERKAE---- 1591
Cdd:COG4942    100 EAQKEELAELlrALYRLGRQpplallLSPEDFLDAVRRLQylkylAPARREQaEELRADLAELAALRAELEAERAEleal 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1592 --GVLAAQARAEQLRDEARGLLQAAQDKL----QRLQELegtyEENERELEVKAAQLDGLEARMRSVLQAINL 1658
Cdd:COG4942    180 laELEEERAALEALKAERQKLLARLEKELaelaAELAEL----QQEAEELEALIARLEAEAAAAAERTPAAGF 248
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1419-1657 1.84e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.75  E-value: 1.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRLASEIAERVRS------------LADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEaqra 1486
Cdd:PRK02224   187 GSLDQLKAQIEEKEEKdlherlngleseLAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED---- 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1487 qgaaqgairgavvdtknteqtlqqVQERMAGTEQSLNSASERARQLHALLEALKLKRAGnSLAASTAEETAGSAQSRARE 1566
Cdd:PRK02224   263 ------------------------LRETIAETEREREELAEEVRDLRERLEELEEERDD-LLAEAGLDDADAEAVEARRE 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1567 AEKQLREQVGDQYQTVRALAERKAEgvlaaqaRAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLE 1646
Cdd:PRK02224   318 ELEDRDEELRDRLEECRVAAQAHNE-------EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390

                          250
                   ....*....|.
gi 1958794731 1647 ARMRSVLQAIN 1657
Cdd:PRK02224   391 EEIEELRERFG 401
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1066-1621 2.19e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.09  E-value: 2.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1066 WDRVVQDLAARTRRLEQWAQELQQTgvlgafESSFLNLQGKLGMVQAIVAARntsaastaKLVEATEGLRHEIGKTTERL 1145
Cdd:COG4717     83 AEEKEEEYAELQEELEELEEELEEL------EAELEELREELEKLEKLLQLL--------PLYQELEALEAELAELPERL 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1146 TQLEAELTDVQDenfnanhalsgLERDGLALNLTLRQLDQHLDILKHSNFLGAYDSIRHAHSQSTEAERRANASTFAIps 1225
Cdd:COG4717    149 EELEERLEELRE-----------LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-- 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1226 pvsnsADTRRRAEVLMgAQRENFNRQHLAnQQALGRLSTHTHTLSLTGVnelvcgapgdapcatspcggagcrdedgqpR 1305
Cdd:COG4717    216 -----EEAQEELEELE-EELEQLENELEA-AALEERLKEARLLLLIAAA------------------------------L 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1306 CGGLGCSGAAATADLALGRArhtqaelqrALVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasrgqveqANQELREli 1385
Cdd:COG4717    259 LALLGLGGSLLSLILTIAGV---------LFLVLGLLALLFLLLAREKASLGKEAEELQALP---------ALEELEE-- 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1386 QNVKDFLSQEGADPD-SIEMVATRVLDIsipaspEQIQRLASEIAERVRSL------ADVDTILAHtmGDVRRAEQLLQD 1458
Cdd:COG4717    319 EELEELLAALGLPPDlSPEELLELLDRI------EELQELLREAEELEEELqleeleQEIAALLAE--AGVEDEEELRAA 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1459 AQRARSRAEgERQKAETVQAALEEAQRAQGAAQgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEA 1538
Cdd:COG4717    391 LEQAEEYQE-LKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1539 LklkragnslaastaeETAGSAqSRAREAEKQLREQvgdqyqtVRALAERKAEGVLAAQArAEQLRDEAR-----GLLQA 1613
Cdd:COG4717    465 L---------------EEDGEL-AELLQELEELKAE-------LRELAEEWAALKLALEL-LEEAREEYReerlpPVLER 520


                   ....*...
gi 1958794731 1614 AQDKLQRL 1621
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 ...
 1598-1667 2.59e-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: 2.59e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1598 ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTCQ 1667
Cdd:cd22303      2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
growth_prot_Scy NF041483
polarized growth protein Scy;
1422-1644 2.95e-09

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 62.15  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 QRLASEIAERVRsladvdTILAHTMGDVRRAEQL----------LQDAQRARS-------RAEGERQKAETVQAALEEAQ 1484
Cdd:NF041483   130 QQLDQELAERRQ------TVESHVNENVAWAEQLrartesqarrLLDESRAEAeqalaaaRAEAERLAEEARQRLGSEAE 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1485 RAQGAAQGAIRGAVVDTknteqtlqqvqERMagteqsLNSASERARQLHALLEALKLKRAGNSLAA-STAEETAGSAQSR 1563
Cdd:NF041483   204 SARAEAEAILRRARKDA-----------ERL------LNAASTQAQEATDHAEQLRSSTAAESDQArRQAAELSRAAEQR 266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1564 AREAEKQLREqvgdqyqtvralaerkaegvlaAQARAEQLRDEARgllqaaQDKLQRLQELEGTYEENERELEVKAAQLD 1643
Cdd:NF041483   267 MQEAEEALRE----------------------ARAEAEKVVAEAK------EAAAKQLASAESANEQRTRTAKEEIARLV 318


                   .
gi 1958794731 1644 G 1644
Cdd:NF041483   319 G 319
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 278-337 2.96e-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: 54.28  E-value: 2.96e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  278 PCDCDPMGSQdGGRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGLsASNPRGCQ 337
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.
 391-430 3.48e-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: 53.90  E-value: 3.48e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958794731  391 CDCDVGGALDPQCDEATGQCRCRPHMIGRRCEQVQPGYFR 430
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1419-1657 3.74e-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: 61.73  E-value: 3.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRLASEIA---ERVRSLADVDTILAHTMGDV----RRAEQLLQDAQRARSRAEGE---------------------- 1469
Cdd:pfam01576  159 ERISEFTSNLAeeeEKAKSLSKLKNKHEAMISDLeerlKKEEKGRQELEKAKRKLEGEstdlqeqiaelqaqiaelraql 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1470 RQKAETVQAAL---EEAQRAQGAAQGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERARQLHALLEALK--LKRA 1544
Cdd:pfam01576  239 AKKEEELQAALarlEEETAQKNNALKKIREL-------EAQISELQEDLESERAARNKAEKQRRDLGEELEALKteLEDT 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1545 GNSLAAS----TAEETAGSAQSRAREAEKQLRE-QVGD----QYQTVRALAE-----RKAEGVL--AAQA----RAEqLR 1604
Cdd:pfam01576  312 LDTTAAQqelrSKREQEVTELKKALEEETRSHEaQLQEmrqkHTQALEELTEqleqaKRNKANLekAKQAleseNAE-LQ 390

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1605 DEARGLLQAAQDKLQR-------LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1657
Cdd:pfam01576  391 AELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLN 450
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
964-1009 4.42e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 4.42e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958794731   964 CACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDPGLQC 1009
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 963-1010 5.17e-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: 53.51  E-value: 5.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731  963 PCACHPSRARGPTCNEFTGQCHCHAGFGGRTCSECQELHWGDP--GLQCR 1010
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1419-1635 7.09e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 7.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRLASEIAERVRSLADVDTILA------HTMGDVRRAEQLLQD----------AQRARSRAEGERQKAE-------T 1475
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEaleaelDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDassddlaA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1476 VQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ-LHALLEALKlkragnslaastae 1554
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERF-------------- 755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1555 etagsAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARA-EQLRDEARGL---LQAAQDKLQRLQELEGT--- 1627
Cdd:COG4913    756 -----AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLdadLESLPEYLALLDRLEEDglp 830


                   ....*....
gi 1958794731 1628 -YEENEREL 1635
Cdd:COG4913    831 eYEERFKEL 839
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
907-961 1.04e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.70  E-value: 1.04e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731   907 CTCNLLGTDPQrcpstdlcHCDPSTGQCPCLPHVQGLSCDRCAPNFWNFtSGRGC 961
Cdd:smart00180    1 CDCDPGGSASG--------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 1458-1623 1.13e-08

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: 56.42  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1458 DAQRARSRAEGERQKAETVQAALEeaqrAQGAAQGAIRG--AVVD-----TKNTEQTLQQVQERMAGTEQSLNSASERAR 1530
Cdd:pfam05335   22 DAQAAAAEAAARQVKNQLADKALQ----AAKAAEAALAGkqQIVEqleqeLREAEAVVQEESASLQQSQANANAAQRAAQ 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1531 QLHALLEALKlkragNSLAAstAEETAGSAQSRAREAEKQLREQvgdqyqtvRALAErkaegvlAAQARAEQLRDEargl 1610
Cdd:pfam05335   98 QAQQQLEALT-----AALKA--AQANLENAEQVAAGAQQELAEK--------TQLLE-------AAKKRVERLQRQ---- 151

                          170
                   ....*....|...
gi 1958794731 1611 LQAAQDKLQRLQE 1623
Cdd:pfam05335  152 LAEARADLEKTKK 164
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 855-897 1.53e-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: 51.97  E-value: 1.53e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958794731  855 CECSGNIDPTDPgaCDPHTGQCLrCLHHTEGPHCGHCKPGFHG 897
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1343-1663 2.37e-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: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQAEEAQQRAQAaldKANASRGQVEQANQELRELIQNVKdflsqegadpdsiemvatrvldisipasPEQIQ 1422
Cdd:COG3064     18 LEQAEAEKRAAAEAEQKAKE---EAEEERLAELEAKRQAEEEAREAK----------------------------AEAEQ 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEIAERVRSLADvdtilahtmgdvrrAEQLLQDAQRarsRAEGERQKAETVQAALEEAQRAQGAAQgairgavvdTK 1502
Cdd:COG3064     67 RAAELAAEAAKKLAE--------------AEKAAAEAEK---KAAAEKAKAAKEAEAAAAAEKAAAAAE---------KE 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1503 NTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAG--SAQSRAREAEKQLREQVGDQYQ 1580
Cdd:COG3064    121 KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAgaAAALVAAAAAAVEAADTAAAAA 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1581 TVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQV 1660
Cdd:COG3064    201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280


                   ...
gi 1958794731 1661 QIY 1663
Cdd:COG3064    281 VAA 283
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1421-1643 2.60e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1421 IQRLASEIAERVRSLADVDTILahtMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG--AV 1498
Cdd:COG4717     48 LERLEKEADELFKPQGRKPELN---LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1499 VDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaasTAEETAGSAQSRAREAEKQLREQvgdQ 1578
Cdd:COG4717    125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-----------ELEAELAELQEELEELLEQLSLA---T 190

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1579 YQTVRALAERKAEgvlaAQARAEQLRDEarglLQAAQDKLQRLQElEGTYEENERELEVKAAQLD 1643
Cdd:COG4717    191 EEELQDLAEELEE----LQQRLAELEEE----LEEAQEELEELEE-ELEQLENELEAAALEERLK 246
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1416-1643 3.29e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 56.09  E-value: 3.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1416 ASPEQIQRLaseiaervRSLADVDTILAHTMgdvRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgair 1495
Cdd:COG1579      1 AMPEDLRAL--------LDLQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1496 gavvdtKNTEQTLQQVQERMAGTEQSLNSASErARQLHAL---LEALKLKRAgnslaastaeetagsaqsrarEAEKQLR 1572
Cdd:COG1579     62 ------KRLELEIEEVEARIKKYEEQLGNVRN-NKEYEALqkeIESLKRRIS---------------------DLEDEIL 113

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1573 EqvgdqyqtvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLD 1643
Cdd:COG1579    114 E------------LMERIEELEEELAELEAELAELEAELEEKKAELDeELAELEAELEELEAEREELAAKIP 173
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1457-1657 3.32e-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: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1457 QDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALL 1536
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1537 EALKLKRAgnslaastaeETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQD 1616
Cdd:COG4942    100 EAQKEELA----------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAE 168

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958794731 1617 KLQRLQELEGTYEENERELevkaAQLDGLEARMRSVLQAIN 1657
Cdd:COG4942    169 LEAERAELEALLAELEEER----AALEALKAERQKLLARLE 205
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1458-1656 3.45e-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: 3.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1458 DAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLhalle 1537
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1538 ALKLKRAGNS-------LAASTAEETAGSAQSRAREAEKQlREQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEargl 1610
Cdd:COG3883     92 ARALYRSGGSvsyldvlLGSESFSDFLDRLSALSKIADAD-ADLLEELKADKAELEAKKAE-LEAKLAELEALKAE---- 165

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958794731 1611 LQAAQDKLQRLQElegtyeenereleVKAAQLDGLEARMRSVLQAI 1656
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 ...
 1421-1622 3.50e-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: 3.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1421 IQRLASEIAERVR---SLADVDTILAHTMGDVRRAEqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGA 1497
Cdd:pfam00529   31 VTRVLVKEGDRVKagdVLFQLDPTDYQAALDSAEAQ--LAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1498 VVDTKNTEQTLQQVQERMAGTEqslNSASERARQLHALLEalklkrAGNSLAastaeetagSAQSRAREAEKQLREQVGD 1577
Cdd:pfam00529  109 QAAVKAAQAQLAQAQIDLARRR---VLAPIGGISRESLVT------AGALVA---------QAQANLLATVAQLDQIYVQ 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958794731 1578 QYQTVRALAERKAEGVLAAQARAEQLRDEarglLQAAQDKLQRLQ 1622
Cdd:pfam00529  171 ITQSAAENQAEVRSELSGAQLQIAEAEAE----LKLAKLDLERTE 211
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 1352-1624 3.51e-08

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 58.53  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1352 QAE--EAQQRAQAALDKANASRGQVEQANQ---ELRELIQNVKDFLSQEGADPDSIEmvatrvLDISIPASPEQIQRLAS 1426
Cdd:PRK10929    43 QAEivEALQSALNWLEERKGSLERAKQYQQvidNFPKLSAELRQQLNNERDEPRSVP------PNMSTDALEQEILQVSS 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1427 EIAE----------RVRSLADVDTILAhtmgdvrraeQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRG 1496
Cdd:PRK10929   117 QLLEksrqaqqeqdRAREISDSLSQLP----------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALK 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1497 AVVDtkntEQTLQQV-----QE--RMagteqSLNSASERARQLHALLEALKlkragNSLAASTAEETagsaqSRAREAEK 1569
Cdd:PRK10929   187 ALVD----ELELAQLsannrQElaRL-----RSELAKKRSQQLDAYLQALR-----NQLNSQRQREA-----ERALESTE 247

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1570 QLREQVGD-------QYQTVRALAErkaegVLAAQA-RAEQLRDEARgllQAAQDKLQRLQEL 1624
Cdd:PRK10929   248 LLAEQSGDlpksivaQFKINRELSQ-----ALNQQAqRMDLIASQQR---QAASQTLQVRQAL 302
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 699-741 3.96e-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: 3.96e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958794731  699 ACQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 741
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1493-1652 4.52e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1493 AIRGAVVDTKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnslaastaEETAGSAQSRAREAEKQLR 1572
Cdd:COG4913    239 RAHEALEDAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAELEELRAELA 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1573 EqvgdqyqtvraLAERKAEgvlaAQARAEQLRDEARGLLQA-AQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1651
Cdd:COG4913    306 R-----------LEAELER----LEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370


                   .
gi 1958794731 1652 V 1652
Cdd:COG4913    371 L 371
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1351-1609 4.61e-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: 55.77  E-value: 4.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1351 RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNvkdfLSQEGADPDSiemvatrvldisipASPEQIQRLaseiae 1430
Cdd:pfam12795   23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAEA--------------APKEILASL------ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1431 rvrSLADVDTILAHTMGDVRRAEQLLQDAQrarSRAEGERQKAETVQAALEEAQRaqgaAQGAIRGAVVDTKNTEQTLQQ 1510
Cdd:pfam12795   79 ---SLEELEQRLLQTSAQLQELQNQLAQLN---SQLIELQTRPERAQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1511 VQERMAGTEQSLnsaserarqLHALLEALKLKRAGNS----LAASTAEETAgsAQSRAREAEKQ-LREQVGDQYQtvrAL 1585
Cdd:pfam12795  149 AQRWALQAELAA---------LKAQIDMLEQELLSNNnrqdLLKARRDLLT--LRIQRLEQQLQaLQELLNEKRL---QE 214

                          250       260
                   ....*....|....*....|....
gi 1958794731 1586 AERkaegvlaAQARAEQLRDEARG 1609
Cdd:pfam12795  215 AEQ-------AVAQTEQLAEEAAG 231
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1321-1550 4.75e-08

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 55.22  E-value: 4.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1321 ALGRARHTQAEL--QRALVEgggilSRVSETRRQAEEAQQRAQAALDKANasrgqveqanqelreliqnvkdflsqegad 1398
Cdd:COG1842     38 DLVEARQALAQViaNQKRLE-----RQLEELEAEAEKWEEKARLALEKGR------------------------------ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1399 pdsiEMVATRVLdisipaspEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKAETVqA 1478
Cdd:COG1842     83 ----EDLAREAL--------ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEL----------KAKKDTL-K 139

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1479 ALEEAQRAQGAAQGAIRGavVDTKNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRAGNS-LAA 1550
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 ...
 1448-1654 4.90e-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: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1448 DVRRAEQLLQDAQRARSRAEGERQKAETV-QAALEEAQRAQGAAQGAirgavvdtknTEQTLQQVQERMAGTEQSLNSAS 1526
Cdd:TIGR02794   61 PAAKKEQERQKKLEQQAEEAEKQRAAEQArQKELEQRAAAEKAAKQA----------EQAAKQAEEKQKQAEEAKAKQAA 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1527 ERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQyqtvrALAERKAEGVlAAQARAEQLRDE 1606
Cdd:TIGR02794  131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK-----AEAEAKAKAE-EAKAKAEAAKAK 204

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1607 ARgllQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ 1654
Cdd:TIGR02794  205 AA---AEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1409-1641 6.20e-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: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1409 VLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQG 1488
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1489 AAQGAIRGAVVDTKNTEQTLQQVQERMAGTE--------QSLNSASERARQLHALLEALKlkRAGNSLAASTAEETAgsA 1560
Cdd:COG4942     90 KEIAELRAELEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARR--EQAEELRADLAELAA--L 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1561 QSRAREAEKQLREQVGDQYQTVRALAERKAEgvlaAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAA 1640
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAE----RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241


                   .
gi 1958794731 1641 Q 1641
Cdd:COG4942    242 R 242
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
700-741 6.34e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 50.39  E-value: 6.34e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958794731   700 CQCSPDGALSALCEGTSGQCLCRTGAFGLRCDHCQRGQWGFP 741
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1354-1656 7.17e-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: 7.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1354 EEAQQRAQAALDKANASRGQVEQANQELRELIQNVkDFLSQEGADPDSIEMVATRVLDI-------SIPASPEQIQRLAS 1426
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREYegyellkEKEALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1427 EIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQrARSRAEGERQKAEtVQAALEEAQRAQGAAQGAIRGAvvdtkntEQ 1506
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEK-------ER 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1507 TLQQVQERMAGTEQSLNSASERARQLhallealklkragnslaastaeetagsaqSRAREAEKQLREQVGDQY---QTVR 1583
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEEL-----------------------------EREIEEERKRRDKLTEEYaelKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1584 ALAERKAEGVLAAQARA-----------EQLRDEaRGLLQAAQDKLQ-RLQELEGTYEENERELEVKAAQLDGLEARMRS 1651
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETrdelkdyreklEKLKRE-INELKRELDRLQeELQRLSEELADLNAAIAGIEAKINELEEEKED 445


                   ....*
gi 1958794731 1652 VLQAI 1656
Cdd:TIGR02169  446 KALEI 450
growth_prot_Scy NF041483
polarized growth protein Scy;
1420-1636 8.64e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.53  E-value: 8.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1420 QIQRLASEIAERVRSLAdvdTILAHTMGDV-RRAEQLLQDAQ----RARSRAEGE-RQKAETVQAALEEAQRAQGAAQGA 1493
Cdd:NF041483    44 QVEVLRAKLHEARRSLA---SRPAYDGADIgYQAEQLLRNAQiqadQLRADAERElRDARAQTQRILQEHAEHQARLQAE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1494 IRGAVVDTKntEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRArEAEK---Q 1570
Cdd:NF041483   121 LHTEAVQRR--QQLDQELAERRQTVESHVNENVAWAEQLRARTES----QARRLLDESRAEAEQALAAARA-EAERlaeE 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1571 LREQVGDQYQTVRALAE-------RKAEGVLAA---QAR-----AEQLR-------DEARG----LLQAAQdklQRLQEL 1624
Cdd:NF041483   194 ARQRLGSEAESARAEAEailrrarKDAERLLNAastQAQeatdhAEQLRsstaaesDQARRqaaeLSRAAE---QRMQEA 270

                          250
                   ....*....|..
gi 1958794731 1625 EGTYEENERELE 1636
Cdd:NF041483   271 EEALREARAEAE 282
growth_prot_Scy NF041483
polarized growth protein Scy;
1325-1655 9.40e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 57.14  E-value: 9.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1325 ARHTQAELQRALVEgggilsRVSETRRQAEEAQQRAQAALDKANASRGQ----VEQAN-QELRELIQNVKDFLSQEGADP 1399
Cdd:NF041483   252 ARRQAAELSRAAEQ------RMQEAEEALREARAEAEKVVAEAKEAAAKqlasAESANeQRTRTAKEEIARLVGEATKEA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEMVATRVLDisiPASPEQiQRLASEIAERVRSLADVDTIlAHTMGDVRRAEQLL---------------QDAQRARS 1464
Cdd:NF041483   326 EALKAEAEQALA---DARAEA-EKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLtkasedakattraaaEEAERIRR 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1465 RAEGE--RQKAETVQAA---------------------LEEAQRAQGAAQ-----GAIRGAVVDTKNTEQTLQQVQERMA 1516
Cdd:NF041483   401 EAEAEadRLRGEAADQAeqlkgaakddtkeyraktvelQEEARRLRGEAEqlraeAVAEGERIRGEARREAVQQIEEAAR 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1517 GTEQSLNSASERARQLH--ALLEALKLkRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKA---- 1590
Cdd:NF041483   481 TAEELLTKAKADADELRstATAESERV-RTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArelr 559

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1591 -EGVLAAQARAEQLRDEARGLLQAAQDKLQRLQE-LEGTYEENERELEVKAAQLDGLEA----RMRSvLQA 1655
Cdd:NF041483   560 eETERAIAARQAEAAEELTRLHTEAEERLTAAEEaLADARAEAERIRREAAEETERLRTeaaeRIRT-LQA 629
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 855-901 1.09e-07

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.66  E-value: 1.09e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958794731  855 CECSGNIDPtdPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHGQAAR 901
Cdd:cd00055      2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
279-336 1.14e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.62  E-value: 1.14e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731   279 CDCDPMGSQDGgRCDSHddpvlglvSGQCRCKEHVVGTRCQQCRDGFFGlsaSNPRGC 336
Cdd:smart00180    1 CDCDPGGSASG-TCDPD--------TGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
339-382 1.20e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 49.62  E-value: 1.20e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958794731   339 CQCNSRGTVPGGtpCDSSSGTCFCKRLVTGDGCDRCLPGHWGLS 382
Cdd:smart00180    1 CDCDPGGSASGT--CDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1451-1651 1.39e-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: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAEQLLQDAQRARSRAEGERQKAETVQAAL--------EEAQRAQG--------------AAQGAIRGavvdTKNTEQTL 1508
Cdd:pfam00261   12 EAEERLKEAMKKLEEAEKRAEKAEAEVAALnrriqlleEELERTEErlaealekleeaekAADESERG----RKVLENRA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1509 QQVQERMAGTEQSLNSASERARQLHALLE--ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLReQVGDQYQTVRALA 1586
Cdd:pfam00261   88 LKDEEKMEILEAQLKEAKEIAEEADRKYEevARKLVVVEGDL--ERAEERAELAESKIVELEEELK-VVGNNLKSLEASE 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1587 ErkaegvlAAQARAEQLRDEARgLLQAaqdklqRLQELEGTYEENERELEVKAAQLDGLEARMRS 1651
Cdd:pfam00261  165 E-------KASEREDKYEEQIR-FLTE------KLKEAETRAEFAERSVQKLEKEVDRLEDELEA 215
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1312-1652 1.75e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.20  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1312 SGAAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASrgqveqanqelrELIQNVKDF 1391
Cdd:PRK02224   397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP------------ECGQPVEGS 464

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1392 LSQEGADPD--SIEMVATRVLDISipaspEQIQRLASEIaERVRSLADVDTILAHTMGDVRRAEQLLQD----AQRARSR 1465
Cdd:PRK02224   465 PHVETIEEDreRVEELEAELEDLE-----EEVEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAErretIEEKRER 538

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1466 AEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERArQLHALLEALKLKRAG 1545
Cdd:PRK02224   539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA 617

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1546 -------------------NSLAASTAEETAGSAQSRAREAEKQLrEQVGDQyqtVRALAERKAE------GVLAAQARA 1600
Cdd:PRK02224   618 laelnderrerlaekrerkRELEAEFDEARIEEAREDKERAEEYL-EQVEEK---LDELREERDDlqaeigAVENELEEL 693

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1601 EQLRDEarglLQAAQDKLQRLQELegtYEENErELEVKAAQLDGlEARMRSV 1652
Cdd:PRK02224   694 EELRER----REALENRVEALEAL---YDEAE-ELESMYGDLRA-ELRQRNV 736
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1318-1647 2.94e-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: 55.57  E-value: 2.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1318 ADLALGRARHTQAELQRALVEG--GGILSRVSETRRQAEEAQQR---AQAALDKANASRGQVEQAN-------------- 1378
Cdd:pfam01576  391 AELRTLQQAKQDSEHKRKKLEGqlQELQARLSESERQRAELAEKlskLQSELESVSSLLNEAEGKNiklskdvsslesql 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1379 QELRELIQ-------NVKDFLSQEGADPDSI------EMVATRVLDisipaspEQIQRLASEIAERVRSLADVDTILaht 1445
Cdd:pfam01576  471 QDTQELLQeetrqklNLSTRLRQLEDERNSLqeqleeEEEAKRNVE-------RQLSTLQAQLSDMKKKLEEDAGTL--- 540

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1446 mgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQ---TLQQVQ---ERMAGTE 1519
Cdd:pfam01576  541 -------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsNLEKKQkkfDQMLAEE 613

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1520 QSLNS--ASERARQlhallEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQY-------QTVRAL--AER 1588
Cdd:pfam01576  614 KAISAryAEERDRA-----EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHELerSKR 688

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794731 1589 KAEGVLAA-QARAEQLRDEarglLQAAQDKLQRLQ------------ELEGTYEENE--RELEVKaaQLDGLEA 1647
Cdd:pfam01576  689 ALEQQVEEmKTQLEELEDE----LQATEDAKLRLEvnmqalkaqferDLQARDEQGEekRRQLVK--QVRELEA 756
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1380-1662 3.17e-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: 3.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1380 ELRELIQNVKDFLSQEGADpdsIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGD---------VR 1450
Cdd:pfam12128  143 EYRSIIQNDRTLLGRERVE---LRSLARQFALCDSESPLRHIDKIAKAMHSKEGKFRDVKSMIVAILEDdgvvppksrLN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAE--------QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSL 1522
Cdd:pfam12128  220 RQQvehwirdiQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1523 NSASERARQ-LHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARAE 1601
Cdd:pfam12128  300 KEKRDELNGeLSAADAAVAKDRS----ELEALEDQHGAFLDADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVT 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1602 QLRDEARGLL-QAAQDKLQRL-QELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:pfam12128  375 AKYNRRRSKIkEQNNRDIAGIkDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNE 437
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1330-1642 3.22e-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: 3.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1330 AELQRALVEGGGILSRVSETRRQaeEAQQRAQAALDKANAS-RGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATR 1408
Cdd:pfam12128  256 AELRLSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTlDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGA 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1409 VLDISIP---ASPEQIQRLASEIAERVRSLAdvdtILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETvqaaleEAQR 1485
Cdd:pfam12128  334 FLDADIEtaaADQEQLPSWQSELENLEERLK----ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL------AKIR 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1486 aqgaaQGAIRGAVVDTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKragnsLAASTAEETAGSAQSRAR 1565
Cdd:pfam12128  404 -----EARDRQLAVAEDDLQALESELREQL---EAGKLEFNEEEYRLKSRLGELKLR-----LNQATATPELLLQLENFD 470

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731 1566 EAEKQLREQVGDQYQTVRALAErkaegvlaAQARAEQLRDEArglLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1642
Cdd:pfam12128  471 ERIERAREEQEAANAEVERLQS--------ELRQARKRRDQA---SEALRQASRRLEERQSALDELELQLFPQAGTL 536
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1350-1601 3.66e-07

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 54.60  E-value: 3.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1350 RRQAEEAQQRAQAALdkanASRGQVEQANQELreliQNVKDFLSQEGADPDSIEmvatrvldisipaspEQIQRLASEIA 1429
Cdd:PRK07735    12 KEAARRAKEEARKRL----VAKHGAEISKLEE----ENREKEKALPKNDDMTIE---------------EAKRRAAAAAK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1430 ERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-EGERQKAETVQAALEE--AQRAQGAAQGAIRGAVVDTKNTEQ 1506
Cdd:PRK07735    69 AKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAaALAKQKREGTEEVTEEekAAAKAKAAAAAKAKAAALAKQKRE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1507 TLQQVQERMAGTEQSL--NSASERARQLHALLEALKLKRAGNSLAASTAEE-------TAGSAQSRAREAEKQLREQV-- 1575
Cdd:PRK07735   149 GTEEVTEEEEETDKEKakAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEkakakakAAAAAKAKAAALAKQKASQGng 228

                          250       260
                   ....*....|....*....|....*...
gi 1958794731 1576 --GDQYQTVRALAERKAEGVLAAQARAE 1601
Cdd:PRK07735   229 dsGDEDAKAKAIAAAKAKAAAAARAKTK 256
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1456-1616 3.75e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.43  E-value: 3.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1456 LQDAQRARSRAEGERQKAETVQAalEEAQRAQGAAQgairgavvdtknteQTLQQV-QERMAGTEQslNSASERARQLHA 1534
Cdd:PRK09510    67 QQQQQKSAKRAEEQRKKKEQQQA--EELQQKQAAEQ--------------ERLKQLeKERLAAQEQ--KKQAEEAAKQAA 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1535 L----LEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVgDQYQTVRALAERKAEGVLAAQARAE-QLRDEARG 1609
Cdd:PRK09510   129 LkqkqAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA-EAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEA 207


                   ....*..
gi 1958794731 1610 LLQAAQD 1616
Cdd:PRK09510   208 KKKAAAE 214
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1502-1662 4.07e-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: 4.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1502 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAA-----STAEETAGSAQSRAREAEKQLREQ 1574
Cdd:COG4942     23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALerRIAALARRIRAleqelAALEAELAELEKEIAELRAELEAQ 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1575 VGDQYQTVRALAER----------KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDG 1644
Cdd:COG4942    103 KEELAELLRALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                          170
                   ....*....|....*...
gi 1958794731 1645 LEARMRSVLQAINLQVQI 1662
Cdd:COG4942    183 LEEERAALEALKAERQKL 200
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 746-793 4.57e-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: 4.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731  746 CVCNGRA---DECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPyGGQC 793
Cdd:pfam00053    1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP-PQGC 49
PTZ00121 PTZ00121
MAEBL; Provisional
 1345-1641 4.68e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 4.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1345 RVSETRRQAEEA---QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVAtrvldisipaspEQI 1421
Cdd:PTZ00121  1558 KKAEEKKKAEEAkkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------------EEL 1625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 QRlaseiAERVRSlaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGaaqgairgavvDT 1501
Cdd:PTZ00121  1626 KK-----AEEEKK--KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE-----------DE 1687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1502 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSA-QSRAREAEKQLREQVGDQYQ 1580
Cdd:PTZ00121  1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeEAKKDEEEKKKIAHLKKEEE 1767

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1581 TVRALAERKAEGVLAAQARAE--QLRDEARGLLQAAQDKLQRLQE--LEGT-YEENERELEVKAAQ 1641
Cdd:PTZ00121  1768 KKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIEggKEGNlVINDSKEMEDSAIK 1833
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1400-1657 5.69e-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: 54.59  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEMVATRVLDIS------IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDA-------------- 1459
Cdd:TIGR00618  176 DQYTQLALMEFAKKkslhgkAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQShayltqkreaqeeq 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 ---QRARSRAEGERQKAETVQAALEEAQRA-----QGAAQGAIRGAVVDT-KNTEQTLQQVQERMA-------------- 1516
Cdd:TIGR00618  256 lkkQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIeQQAQRIHTELQSKMRsrakllmkraahvk 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1517 ---------GTEQSLNSASERAR--------------QLHALLEALK--------LKRAGNSLAASTAEETAGSAQSRAR 1565
Cdd:TIGR00618  336 qqssieeqrRLLQTLHSQEIHIRdahevatsireiscQQHTLTQHIHtlqqqkttLTQKLQSLCKELDILQREQATIDTR 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1566 --------------EAEKQLREQVGDQYQ-----TVRALAERKAEGVLAAQA---RAEQLRDEARGLLQAAQDK------ 1617
Cdd:TIGR00618  416 tsafrdlqgqlahaKKQQELQQRYAELCAaaitcTAQCEKLEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKavvlar 495

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1958794731 1618 LQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1657
Cdd:TIGR00618  496 LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 745-790 6.73e-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: 47.35  E-value: 6.73e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731  745 PCVCNGRAD---ECDAHTGACLgCRDYTGGEHCERCIAGFHGDPRLPYG 790
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 ...
 1599-1666 6.89e-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: 6.89e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1599 RAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYNTC 1666
Cdd:cd22301      3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1400-1587 6.95e-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: 51.11  E-value: 6.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEMVATRVLDISipaspEQIQRLASEIAERV-RSLADVDTILAHTMGDVR-RAEQLLQDAQrarsraegerqkaETVQ 1477
Cdd:pfam01442    4 DSLDELSTYAEELQ-----EQLGPVAQELVDRLeKETEALRERLQKDLEEVRaKLEPYLEELQ-------------AKLG 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1478 AALEEAQRAQGAAQGAIRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASERAR-QLHALLEALKLK-----RAGNSLAAS 1551
Cdd:pfam01442   66 QNVEELRQRLEPYTEELRKRL--NADAEELQEKLAPYGEELRERLEQNVDALRaRLAPYAEELRQKlaerlEELKESLAP 143

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958794731 1552 TAEEtagsAQSRAREAEKQLREQVGDQYQTVRALAE 1587
Cdd:pfam01442  144 YAEE----VQAQLSQRLQELREKLEPQAEDLREKLD 175
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1343-1656 1.08e-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: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQAEEAQQRAQAALDKANASRGQVEQ-ANQELRELiqnvkDFLSQEGADPDSiemvatrvldisipaspEQI 1421
Cdd:pfam17380  308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERmAMEREREL-----ERIRQEERKREL-----------------ERI 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 --QRLASEIaERVRSLADVDtilahtMGDVRRAEQLLQDAQRARSRA--EGERQKAETVQAALEEAQRAQgaaQGAIRGa 1497
Cdd:pfam17380  366 rqEEIAMEI-SRMRELERLQ------MERQQKNERVRQELEAARKVKilEEERQRKIQQQKVEMEQIRAE---QEEARQ- 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1498 vVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETagsaQSRAREAEKQLREQVGD 1577
Cdd:pfam17380  435 -REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ----RRKILEKELEERKQAMI 509

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1578 QYQTVRALAERKAEGVLAAQARAEQLR--DEARGLLQAAQDKLQRLQELEGTYEENERelevkaaqLDGLEaRMRSVLQA 1655
Cdd:pfam17380  510 EEERKRKLLEKEMEERQKAIYEEERRReaEEERRKQQEMEERRRIQEQMRKATEERSR--------LEAME-REREMMRQ 580


                   .
gi 1958794731 1656 I 1656
Cdd:pfam17380  581 I 581
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1411-1641 1.44e-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: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1411 DISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE--AQRA-- 1486
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREelGERAra 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1487 ---QGAAQGAIrGAVVDTKNTEQTLQQVQermagteqSLNSASERARQLhalLEALKLKRAGNSLAASTAEETAGSAQSR 1563
Cdd:COG3883     95 lyrSGGSVSYL-DVLLGSESFSDFLDRLS--------ALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEAL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1564 AREAEKQLRE---QVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAA 1640
Cdd:COG3883    163 KAELEAAKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242


                   .
gi 1958794731 1641 Q 1641
Cdd:COG3883    243 A 243
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1318-1549 1.53e-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: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1318 ADLALGRARHTQAEL---QRALVEgggilsRVSETRRQAEEAQQRAQAALDKanasrgqveqANQEL-RELIQnvkdfls 1393
Cdd:pfam04012   34 MQSELVKARQALAQTiarQKQLER------RLEQQTEQAKKLEEKAQAALTK----------GNEELaREALA------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 qegadpdsiemvatrvldisipaspeQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAqrarsraegeRQKA 1473
Cdd:pfam04012   91 --------------------------EKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL----------KAKK 134

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1474 ETVQAAlEEAQRAQGAAQGAIRGAvvDTKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALLEALKLKRAGNSLA 1549
Cdd:pfam04012  135 NLLKAR-LKAAKAQEAVQTSLGSL--STSSATDSFERIEEKIEEREARADAAAELAsaVDLDAKLEQAGIQMEVSEDV 209
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1452-1656 1.69e-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: 53.03  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1452 AEQLLQDAQRARsrAEgERQKAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERARQ 1531
Cdd:COG3096    290 LRRELFGARRQL--AE-EQYRLVEMARELEELSARESDLEQDYQAAS-DHLNLVQTALRQQEKIERYQEDLEELTERLEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1532 LHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQL--REQVGDQYQTvRALAERKAegvLAAQARAEQLRDEARG 1609
Cdd:COG3096    366 QEEVVEEAAEQLA-------EAEARLEAAEEEVDSLKSQLadYQQALDVQQT-RAIQYQQA---VQALEKARALCGLPDL 434

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958794731 1610 LLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1656
Cdd:COG3096    435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV 481
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1432-1647 1.84e-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: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1432 VRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAAL----EEAQRAQGAAQGAIRGAvvdtknteqt 1507
Cdd:pfam06008    1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELsslaQETEELQKKATQTLAKA---------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1508 lQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLaasTAEETAGSAQSRA-REAEKQLREQVGDQYQTVRALA 1586
Cdd:pfam06008   71 -QQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMlAEAQRMLGEIRSRDFGTQLQNA 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1587 E---RKAEGVLAA------------QARAEQLRD----------EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQ 1641
Cdd:pfam06008  147 EaelKAAQDLLSRiqtwfqspqeenKALANALRDslaeyeaklsDLRELLREAAAKTRDANRLNLANQANLREFQRKKEE 226


                   ....*.
gi 1958794731 1642 LDGLEA 1647
Cdd:pfam06008  227 VSEQKN 232
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1319-1531 1.85e-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: 51.08  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1319 DLALGRARHTQAELQRALVEgggilsrVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegad 1398
Cdd:COG1579     16 DSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN---- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1399 pdsiemvatrvldisiPASPEQIQRLASEIAervrSLAdvdtilahtmgdvRRAEQLLQDAQRARSRAEGERQKAETVQA 1478
Cdd:COG1579     85 ----------------VRNNKEYEALQKEIE----SLK-------------RRISDLEDEILELMERIEELEEELAELEA 131

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958794731 1479 ALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGT-EQSLNSASERARQ 1531
Cdd:COG1579    132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYERIRK 185
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1380-1657 2.01e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1380 ELRELIQNVKDFLSQEgadpdsiemvatrvldisipaspEQIQRLASEIAERvrsladvdtiLAHTMGDVRRAEQLLQDA 1459
Cdd:PRK03918   173 EIKRRIERLEKFIKRT-----------------------ENIEELIKEKEKE----------LEEVLREINEISSELPEL 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 QRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ------SLNSASERARQLH 1533
Cdd:PRK03918   220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLS 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1534 ALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEK---QLREQVGDQYQTVRALAE-----RKAEGVLAAQARAEQLRD 1605
Cdd:PRK03918   300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEEleerhELYEEAKAKKEELERLKK 379

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1606 EARGLlqaAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1657
Cdd:PRK03918   380 RLTGL---TPEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
1314-1662 2.31e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 52.33  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLS 1393
Cdd:COG0840     16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 QEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKA 1473
Cdd:COG0840     96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1474 ETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQ-------SLNSASER---ARQLHALLEALK--- 1540
Cdd:COG0840    176 AAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgdltvriDVDSKDEIgqlADAFNRMIENLRelv 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1541 --LKRAGNSLAAStAEETAGSAQSRAREAEKQlREQVgdqyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKL 1618
Cdd:COG0840    256 gqVRESAEQVASA-SEELAASAEELAAGAEEQ-AASL----EETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGG 329

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1958794731 1619 QRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:COG0840    330 EVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDI 373
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1345-1662 2.32e-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: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1345 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKdfLSQEGADPDSIEMVATRVLDISipASPEQIQRL 1424
Cdd:COG3064     17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK--AEAEQRAAELAAEAAKKLAEAE--KAAAEAEKK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1425 ASEIAERVRSLADVDTIL--AHTMGDVRRAEQLLQDAQR-ARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1501
Cdd:COG3064     93 AAAEKAKAAKEAEAAAAAekAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAA 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1502 KNTEQTLQQVQERMAGTEQSLNSASERARQLHAllEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQT 1581
Cdd:COG3064    173 RAAAGAAAALVAAAAAAVEAADTAAAAAAALAA--AAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEE 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1582 VRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQ 1661
Cdd:COG3064    251 AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVR 330


                   .
gi 1958794731 1662 I 1662
Cdd:COG3064    331 G 331
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 1330-1633 2.92e-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: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1330 AELQrALVEGggILSRVSETRRQAEEAQQRAQAALDKANAS----RGQVEQANQE---LRELIQNVKDFLSQEGADPDSI 1402
Cdd:pfam05701  264 AELA-AYMES--KLKEEADGEGNEKKTSTSIQAALASAKKEleevKANIEKAKDEvncLRVAAASLRSELEKEKAELASL 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1403 ---EMVATrvldISIPASPEQIQRLASEIA---ERVRSLADVDTILAHTMGDVRR-AEQLLQDAQRAR-----SRAEGER 1470
Cdd:pfam05701  341 rqrEGMAS----IAVSSLEAELNRTKSEIAlvqAKEKEAREKMVELPKQLQQAAQeAEEAKSLAQAAReelrkAKEEAEQ 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1471 QKAE--TVQAALEEAQRAQGAAQGAIRGAVVdtknteqTLQQVQERMAGTEQSLNSASERARQLhALLEALKL-KRagns 1547
Cdd:pfam05701  417 AKAAasTVESRLEAVLKEIEAAKASEKLALA-------AIKALQESESSAESTNQEDSPRGVTL-SLEEYYELsKR---- 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1548 laASTAEETAG----SAQSR---AREAEKQLREQVGDQYqtvRALAERKaEGVLAAQARAEQLRDEargllqaaqdKLQR 1620
Cdd:pfam05701  485 --AHEAEELANkrvaEAVSQieeAKESELRSLEKLEEVN---REMEERK-EALKIALEKAEKAKEG----------KLAA 548

                          330
                   ....*....|...
gi 1958794731 1621 LQELEGTYEENER 1633
Cdd:pfam05701  549 EQELRKWRAEHEQ 561
GAF COG2203
GAF domain [Signal transduction mechanisms];
1315-1662 3.12e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 52.12  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1315 AATADLALGRARHTQAELQRALvegggilsrvsETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1394
Cdd:COG2203    337 ADQAAIAIERARLYEALEAALA-----------ALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1395 EGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAE 1474
Cdd:COG2203    406 LLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLA 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1475 TVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAE 1554
Cdd:COG2203    486 ALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVG 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1555 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERE 1634
Cdd:COG2203    566 VLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLR 645

                          330       340
                   ....*....|....*....|....*...
gi 1958794731 1635 LEVKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:COG2203    646 LALALASLVLLRALLATELDLILDSSLL 673
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
855-897 3.57e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 45.38  E-value: 3.57e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958794731   855 CECsgNIDPTDPGACDPHTGQCLrCLHHTEGPHCGHCKPGFHG 897
Cdd:smart00180    1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 795-853 3.61e-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: 45.42  E-value: 3.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731  795 PCPCPeGPGSQRHfatSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDPSKPGGrCQ 853
Cdd:cd00055      1 PCDCN-GHGSLSG---QCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
1370-1572 3.65e-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: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1370 SRGQVEQANQELreliqNVKDFLSQEGADP-------DSIE--------MVATR------VLDISIPA-SPEQIQRLA-- 1425
Cdd:COG3524     84 SRDAVERLDAEL-----DLRAHYSRPGIDPlsrldpdASIEdlykyyrrRVKVEydstsgIITLEVRAfDPEDAQAIAea 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1426 ----SE-----IAERVRSladvDTIlAHTMGDVRRAEQLLQDAQRA----RSR---------AEG--------ERQKAET 1475
Cdd:COG3524    159 llaeSEelvnqLSERARE----DAV-RFAEEEVERAEERLRDAREAllafRNRngildpeatAEAllqliatlEGQLAEL 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1476 vQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAG--TEQSLNSASERarqlhalLEALKLKRAgnslaasTA 1553
Cdd:COG3524    234 -EAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGasGGDSLASLLAE-------YERLELERE-------FA 298

                          250       260
                   ....*....|....*....|...
gi 1958794731 1554 EETAGSAQS---RAR-EAEKQLR 1572
Cdd:COG3524    299 EKAYTSALAaleQARiEAARQQR 321
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 1351-1661 3.67e-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: 51.61  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1351 RQAEEAQQRAQ--AALDKANASRGQVEQANQELRELiqnvKDFLSQEG--ADPDSIEMvatRVLDISIPASPEQIQRLAS 1426
Cdd:pfam05622  160 RNAEYMQRTLQleEELKKANALRGQLETYKRQVQEL----HGKLSEESkkADKLEFEY---KKLEEKLEALQKEKERLII 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1427 E---------------IAERVRSLADVDTILAHTMGDVRRAE-----------QLLQDAQRARSRAEG-ERQKAETVQAA 1479
Cdd:pfam05622  233 ErdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEimpaeirekliRLQHENKMLRLGQEGsYRERLTELQQL 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1480 LEEAQRAQGAAQGAIRgavvdtKNTEQ--TLQQVQERMAGTEQSLNSASERARQLHALLEAL--KLKRAGNSLAASTA-- 1553
Cdd:pfam05622  313 LEDANRRKNELETQNR------LANQRilELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHleKLHEAQSELQKKKEqi 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1554 EETAGSAQSRAREAEKQLREQVGDQYQTVRALAER------KAEGVLAA-QARAEQLR-DEARGLLQAAQDKLQRLQELE 1625
Cdd:pfam05622  387 EELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERykkyveKAKSVIKTlDPKQNPASpPEIQALKNQLLEKDKKIEHLE 466

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1626 GTYEEN--ERELEVK-----------AAQLDGLEARmrsvLQAINLQVQ 1661
Cdd:pfam05622  467 RDFEKSklQREQEEKlivtawynmgmALHRKAIEER----LAGLSSPGQ 511
PTZ00121 PTZ00121
MAEBL; Provisional
 1343-1638 4.07e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQAEEAQQRAQAAlDKANASRGQVEQAnQELRELIQNVKDFLSQEGADPDSIEmvATRVLDISIPAspEQIQ 1422
Cdd:PTZ00121  1423 AKKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKKKA--EEAK 1496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEI--AERVRSLADvdtilahtmgDVRRAEQLlQDAQRARsRAEgERQKAETVQAAlEEAQRAQGAAQGAIRGAVVD 1500
Cdd:PTZ00121  1497 KKADEAkkAAEAKKKAD----------EAKKAEEA-KKADEAK-KAE-EAKKADEAKKA-EEKKKADELKKAEELKKAEE 1562

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1501 TKNTEQTLQQVQER-MAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQY 1579
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKnMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1580 QTVRALAE--RKAE---GVLAAQ--ARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVK 1638
Cdd:PTZ00121  1643 AEEKKKAEelKKAEeenKIKAAEeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
mukB PRK04863
chromosome partition protein MukB;
1478-1651 4.40e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.88  E-value: 4.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1478 AALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSAS--------ERARQLHALLEALK-----LKRA 1544
Cdd:PRK04863   837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetlaDRVEEIREQLDEAEeakrfVQQH 916

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1545 GNSL------AASTAEETAGSAQSRAR--EAEKQLReqvgDQYQTVRALAE----------RKAEGVLAA---------- 1596
Cdd:PRK04863   917 GNALaqlepiVSVLQSDPEQFEQLKQDyqQAQQTQR----DAKQQAFALTEvvqrrahfsyEDAAEMLAKnsdlneklrq 992

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1597 -QARAEQLRDEARGLLQAAQDKL----QRLQELEGTYE-------ENERELEVKAAQLD-GLEARMRS 1651
Cdd:PRK04863   993 rLEQAEQERTRAREQLRQAQAQLaqynQVLASLKSSYDakrqmlqELKQELQDLGVPADsGAEERARA 1060
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1321-1621 4.76e-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: 51.05  E-value: 4.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1321 ALGRARHTQAELQRALVEGGGILSRVSETR----RQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEG 1396
Cdd:pfam07888   88 ELRQSREKHEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1397 ADPDSiemvaTRVLDISIPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQR--------------A 1462
Cdd:pfam07888  168 EEEAE-----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaenealleelrsL 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1463 RSRAEGERQKAETVQAALEE--AQRAQGAA---QGAIRGAvvdtkntEQTLQQVQERMAGTEQSLNSASERAR-QLHALL 1536
Cdd:pfam07888  243 QERLNASERKVEGLGEELSSmaAQRDRTQAelhQARLQAA-------QLTLQLADASLALREGRARWAQERETlQQSAEA 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1537 EALKLKRAgnSLAASTAEETAGSAQSRAREAEKQL-REQVGDQYQ---TVRALAERKAeGVLAAQARAEQLRDEARGLLQ 1612
Cdd:pfam07888  316 DKDRIEKL--SAELQRLEERLQEERMEREKLEVELgREKDCNRVQlseSRRELQELKA-SLRVAQKEKEQLQAEKQELLE 392


                   ....*....
gi 1958794731 1613 AAQDKLQRL 1621
Cdd:pfam07888  393 YIRQLEQRL 401
mukB PRK04863
chromosome partition protein MukB;
1345-1655 6.12e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.50  E-value: 6.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1345 RVSETRRQAEEAQQR-AQAALDKanasrgqveqanQELRELIQNVKDFLSQEgadpdsiemvatrvLDISIPASPEQ-IQ 1422
Cdd:PRK04863   787 RIEQLRAEREELAERyATLSFDV------------QKLQRLHQAFSRFIGSH--------------LAVAFEADPEAeLR 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRA-----EGERQKAETVQAALEEAQRA------QGAAQ 1491
Cdd:PRK04863   841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladETLADRVEEIREQLDEAEEAkrfvqqHGNAL 920

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1492 GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLE---ALKLKRAGNSLAASTA--------EETAGSA 1560
Cdd:PRK04863   921 AQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrraHFSYEDAAEMLAKNSDlneklrqrLEQAEQE 1000

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1561 QSRAREAEKQLREQVgDQYQTVRA------------LAERKAE----GVLA---AQARAEQLRDEARGLLQAAQdklQRL 1621
Cdd:PRK04863  1001 RTRAREQLRQAQAQL-AQYNQVLAslkssydakrqmLQELKQElqdlGVPAdsgAEERARARRDELHARLSANR---SRR 1076

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1958794731 1622 QELEGTYEENERELE-----VKAAQLDGLEARmRSVLQA 1655
Cdd:PRK04863  1077 NQLEKQLTFCEAEMDnltkkLRKLERDYHEMR-EQVVNA 1114
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 1357-1651 6.19e-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: 6.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1357 QQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIE----M--VATR---VLDISIPASPEQIQ---RL 1424
Cdd:pfam10174  337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRdlkdMldVKERkinVLQKKIENLQEQLRdkdKQ 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1425 ASEIAERVRSL----ADVDTILAhTMgdvrraEQLLQDAQRARSRAEGERQKAEtvQAALEEAQRAQGaaqgairgavvD 1500
Cdd:pfam10174  417 LAGLKERVKSLqtdsSNTDTALT-TL------EEALSEKERIIERLKEQRERED--RERLEELESLKK-----------E 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1501 TKNTEQTLQQVQERMAGTEQSLNSASERARQL--HALLEALKLKRAGNSLAASTAEETAGSAQS-RAREAEKQLR--EQV 1575
Cdd:pfam10174  477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLkKAHNAEEAVRtnPEI 556

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1576 GDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRS 1651
Cdd:pfam10174  557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
DUF4175 pfam13779
Domain of unknown function (DUF4175);
1298-1624 8.27e-06

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 50.76  E-value: 8.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1298 RDEDGQprcgglgcSGAAATADLALGRARHTQaELQRALVEgggilsrvsetrrqaeeaqQRAQAALDKANASRgqveqA 1377
Cdd:pfam13779  379 TDGAGQ--------EGRSEPLEIRLPERRFSD-PLARALIE-------------------QRRRLALDRENRPR-----V 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1378 NQELRELIqnvkdfLSQEGADPDSIEMVATRVL--DISIPASPEQIQRLAS---EIAERVRSladvdtilahtmGDVRRA 1452
Cdd:pfam13779  426 ARALDALT------LAPEEFGPDAGVYLGLRSAlaRLELARSDEALDEVADllwELALRIED------------GDLSDA 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1453 EQLLQDAQRARSRA------EGERQK-AETVQAALEE-----AQRAQGAAQGAIRGAVVDTK-NTEQTLQQVQERMAgtE 1519
Cdd:pfam13779  488 ERRLRAAQERLSEAlergasDEEIAKlMQELREALDDymqalAEQAQQNPQDLQQPDDPNAQeMTQQDLQRMLDRIE--E 565

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1520 QSLNSASERARQlhaLLEAlkLKRAGNSLAASTAEETAGSAQSRAREAEKQLRE-------------------------Q 1574
Cdd:pfam13779  566 LARSGRRAEAQQ---MLSQ--LQQMLENLQAGQPQQQQQQGQSEMQQAMDELGDllreqqqlldetfrqlqqqggqqqgQ 640

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1575 VGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQEL 1624
Cdd:pfam13779  641 PGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEEL 690
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1416-1660 9.14e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 9.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1416 ASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAEtVQAALEEAQRaqgaAQGAIR 1495
Cdd:COG4717     85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE-LPERLEELEE----RLEELR 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1496 GAVVDTKNTEQTLQQVQERMA--------GTEQSLNSASERARQLHALLEALK--LKRAGNSLAASTAEETAGSAQSRAR 1565
Cdd:COG4717    160 ELEEELEELEAELAELQEELEelleqlslATEEELQDLAEELEELQQRLAELEeeLEEAQEELEELEEELEQLENELEAA 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1566 EAEKQLREQ----------------VGDQYQTVRALAE----------------RKAEGVLAAQARAEQLRDEARGLLQA 1613
Cdd:COG4717    240 ALEERLKEArlllliaaallallglGGSLLSLILTIAGvlflvlgllallflllAREKASLGKEAEELQALPALEELEEE 319

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1614 AQDKLQRLQELEGTYEENE-RELEVKAAQLDGLEARMRSVLQAINLQV 1660
Cdd:COG4717    320 ELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEE 367
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1451-1663 9.62e-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: 49.53  E-value: 9.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgAIRGAVV-----DTKNTEQTLQQVQERMAGTEQSlNSA 1525
Cdd:pfam13868   61 EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQERE-QMDEIVEriqeeDQAEAEEKLEKQRQLREEIDEF-NEE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1526 SERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQ-----LREQvgdQYQTVRALAERkaEGVLAAQARA 1600
Cdd:pfam13868  139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEreiarLRAQ---QEKAQDEKAER--DELRAKLYQE 213

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1601 EQLRDEARGLLQAAQDKLQRLQELEGTYEE---NERELEVKAAQLDglEARMRSVLQAINLQVQIY 1663
Cdd:pfam13868  214 EQERKERQKEREEAEKKARQRQELQQAREEqieLKERRLAEEAERE--EEEFERMLRKQAEDEEIE 277
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1346-1550 9.68e-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: 48.95  E-value: 9.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1346 VSETRRQAEEAQQ-RAQAALDKANASR--GQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDisipASPEQIQ 1422
Cdd:pfam06008   53 AQETEELQKKATQtLAKAQQVNAESERtlGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLS----RMLAEAQ 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEIAERvrslaDVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQK-AETVQAALEEAQRAQGAAQGAIRGAVVDT 1501
Cdd:pfam06008  129 RMLGEIRSR-----DFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAlANALRDSLAEYEAKLSDLRELLREAAAKT 203

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1502 KNTEQTLQQVQERMagteQSLNSASERARQLHALLEALkLKRAGNSLAA 1550
Cdd:pfam06008  204 RDANRLNLANQANL----REFQRKKEEVSEQKNQLEET-LKTARDSLDA 247
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1348-1662 1.30e-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: 49.89  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1348 ETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvKDFLSQEGADPDSIEMVATRvldisipaspEQIQRLASE 1427
Cdd:pfam07888   10 EEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQ--AQEAANRQREKEKERYKRDR----------EQWERQRRE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1428 IAERVrslADVDTILAHTMGDVRRAEQLLQDAQRARsraegerqkaetvqAALEEAQRAQGAAQGAirgAVVDTKNTEQT 1507
Cdd:pfam07888   78 LESRV---AELKEELRQSREKHEELEEKYKELSASS--------------EELSEEKDALLAQRAA---HEARIRELEED 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1508 LQQVQERMAGTEQSLNSASERARQLHALL-------EALKLKragnsLAASTAEETAGSAQ---SRAREAEK-----QLR 1572
Cdd:pfam07888  138 IKTLTQRVLERETELERMKERAKKAGAQRkeeeaerKQLQAK-----LQQTEEELRSLSKEfqeLRNSLAQRdtqvlQLQ 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1573 EQVGDQYQTVRALAERKAEgvlaaqarAEQLRDEARGLlqaaQDklqRLQELEGTYEENERELEVKAAQLDGLEARM-RS 1651
Cdd:pfam07888  213 DTITTLTQKLTTAHRKEAE--------NEALLEELRSL----QE---RLNASERKVEGLGEELSSMAAQRDRTQAELhQA 277

                          330
                   ....*....|.
gi 1958794731 1652 VLQAINLQVQI 1662
Cdd:pfam07888  278 RLQAAQLTLQL 288
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1342-1613 1.54e-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: 1.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1342 ILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflSQEGAD--PDSIEMVATRVLDISipaspE 1419
Cdd:smart00283    2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQS--AAEAAEegREAVEDAITAMDQIR-----E 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1420 QIQRLAS---EIAERVRSLADV----DTIlahtmgdvrrAEQ--LLQ-----DAQRArsraeGERQK-----AETVQaAL 1480
Cdd:smart00283   75 VVEEAVSaveELEESSDEIGEIvsviDDI----------ADQtnLLAlnaaiEAARA-----GEAGRgfavvADEVR-KL 138

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1481 eeAQRAQGAAqgairgavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTaEETAGSA 1560
Cdd:smart00283  139 --AERSAESA-----------KEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVE--ETGDALEEIVDSV-EEIADLV 202

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731  1561 QSRAREAEKQLR--EQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQA 1613
Cdd:smart00283  203 QEIAAATDEQAAgsEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDEL 257
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1505-1657 1.63e-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: 48.00  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1505 EQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLrEQVGD--QYQtv 1582
Cdd:COG1579     23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEEQL-GNVRNnkEYE-- 92

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1583 rALAERKAegvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAIN 1657
Cdd:COG1579     93 -ALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
PRK15374 PRK15374
type III secretion system needle tip complex protein SipB;
1455-1648 1.67e-05

type III secretion system needle tip complex protein SipB;


Pssm-ID: 185272 [Multi-domain]  Cd Length: 593  Bit Score: 49.58  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1455 LLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEqSLNSASerarQLHA 1534
Cdd:PRK15374    13 YTQNPRLAEAAFEGVRKNTDFLKAADKAFKDVVATKAGDLKAGTKSGESAINTVGLKPPTDAARE-KLSSEG----QLTL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1535 LLEALKLKRAGNSLAASTAEETAGSAQsraREAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRDEARGLL 1611
Cdd:PRK15374    88 LLGKLMTLLGDVSLSQLESRLAVWQAM---IESQKEMGIQVSKEFQTALGEAQeatDLYEASIKKTDTAKSVYDAAEKKL 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958794731 1612 QAAQDKLQRLQELEGTYEENERELEVKAAqlDGLEAR 1648
Cdd:PRK15374   165 TQAQNKLQSLDPADPGYAQAEAAVEQAGK--EATEAK 199
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 216-268 1.88e-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: 1.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731  216 CECNGH---SHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTK 268
Cdd:cd00055      2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1345-1661 1.95e-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: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1345 RVSETRRQAEE-AQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQR 1423
Cdd:COG3064    121 KAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1424 LASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKN 1503
Cdd:COG3064    201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1504 TEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAG-------NSLAASTAEETAGSAQSRAREAEK------Q 1570
Cdd:COG3064    281 VAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAaagalvvRGGGAASLEAALSLLAAGAAAAAAgagalaT 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1571 LREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1650
Cdd:COG3064    361 GALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKL 440

                          330
                   ....*....|.
gi 1958794731 1651 SVLQAINLQVQ 1661
Cdd:COG3064    441 VADLAGGLVGI 451
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 216-267 2.02e-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: 2.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731  216 CECNGH---SHSCHFdmavylasgnvSGGVCDgCQHNTAGRHCELCRPFFYRDPT 267
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.
 822-852 2.10e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.10e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958794731  822 VCHCRAGYTGLRCEACAPGHFGDPSKPGGRC 852
Cdd:pfam00053   19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1341-1631 2.16e-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: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1341 GILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQegadpdsiemvATRVLdisipASPEQ 1420
Cdd:pfam06008    9 GALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKK-----------ATQTL-----AKAQQ 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1421 IQRLASEIAERVRSLADvdtilahtmgdvrRAEQLLQDAQRARSRAEGERQKAE-----TVQAALEEAQRAQGAaqgaIR 1495
Cdd:pfam06008   73 VNAESERTLGHAKELAE-------------AIKNLIDNIKEINEKVATLGENDFalpssDLSRMLAEAQRMLGE----IR 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1496 GavvdtKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEETAgsAQSRAREAEKQLREqv 1575
Cdd:pfam06008  136 S-----RDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA-NALRDSLAEYEAKLSD--LRELLREAAAKTRD-- 205

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1576 gdqyqtvralaerkAEGVLAAQARAeqlrdearglLQAAQDKLQRLQELEGTYEEN 1631
Cdd:pfam06008  206 --------------ANRLNLANQAN----------LREFQRKKEEVSEQKNQLEET 237
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1318-1539 2.20e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1318 ADLALGRARHTQAELQ---RALVEGGGILSRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ 1394
Cdd:COG4913    659 DEIDVASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1395 --EGADPDSIEMVATRVLDISIPASPEQIQRlasEIAERVRSLAdvdtilahtmGDVRRAEQLLQDAQRA-RSRAEGERQ 1471
Cdd:COG4913    739 aeDLARLELRALLEERFAAALGDAVERELRE---NLEERIDALR----------ARLNRAEEELERAMRAfNREWPAETA 805

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1472 KAETVQAALEEAQR------AQG--AAQGAIRGAVvdTKNTEQTLQQVQERMagtEQSLNSASERARQLHALLEAL 1539
Cdd:COG4913    806 DLDADLESLPEYLAlldrleEDGlpEYEERFKELL--NENSIEFVADLLSKL---RRAIREIKERIDPLNDSLKRI 876
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1450-1650 2.40e-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: 48.38  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1450 RRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgAIRGAvvdtknteQTL-QQVQERmagteqslnsasER 1528
Cdd:pfam13868   33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE-----RKRYR--------QELeEQIEER------------EQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1529 ARQL---HALLEALKLKRAgnsLAASTAEETAgsAQSRAREAEKQLREQVgDQYQtvRALAERKaegvlaaQARAEQLRD 1605
Cdd:pfam13868   88 KRQEeyeEKLQEREQMDEI---VERIQEEDQA--EAEEKLEKQRQLREEI-DEFN--EEQAEWK-------ELEKEEERE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958794731 1606 EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1650
Cdd:pfam13868  153 EDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ 197
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 152-204 2.42e-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: 43.11  E-value: 2.42e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731  152 CFCYGHAS---QCApapgapahaegMVHGACICKHNTRGLNCEQCQDFYQDLPWHP 204
Cdd:cd00055      2 CDCNGHGSlsgQCD-----------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1473-1657 2.43e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1473 AETVQAALEEAQRAQGAAQGAIRGavvdtKNTEQTLQQVQErmagTEQSLNSASERARQLHALLEALKLKRAgnSLAAST 1552
Cdd:COG4717     40 LAFIRAMLLERLEKEADELFKPQG-----RKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEE--ELEELE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1553 AEETAgsAQSRAREAEKQLreQVGDQYQTVRALAERKAEGvlaaQARAEQLRDEarglLQAAQDKLQRLQELEGTYEENE 1632
Cdd:COG4717    109 AELEE--LREELEKLEKLL--QLLPLYQELEALEAELAEL----PERLEELEER----LEELRELEEELEELEAELAELQ 176

                          170       180
                   ....*....|....*....|....*.
gi 1958794731 1633 RELEVKAAQLD-GLEARMRSVLQAIN 1657
Cdd:COG4717    177 EELEELLEQLSlATEEELQDLAEELE 202
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1420-1662 2.54e-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: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1420 QIQRLAS-EIAERVRSLADVDTILAHTMGDVRRAEQLLQDA----QRARSR-----AEGE-RQKA-ETVQAALEEAQRAQ 1487
Cdd:COG3206     86 QIEILKSrPVLERVVDKLNLDEDPLGEEASREAAIERLRKNltvePVKGSNvieisYTSPdPELAaAVANALAEAYLEQN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1488 GAAQgairgavvdTKNTEQTLQQVQERMAGTEQSLNSAsERArqlhalLEALKLKRAGNSLaastaEETAGSAQSRAREA 1567
Cdd:COG3206    166 LELR---------REEARKALEFLEEQLPELRKELEEA-EAA------LEEFRQKNGLVDL-----SEEAKLLLQQLSEL 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1568 EKQLREqvgdqyqtvrALAERKAegvlaAQARAEQLRDEARGLLQAA---------QDKLQRLQELEGTYEENEREL--- 1635
Cdd:COG3206    225 ESQLAE----------ARAELAE-----AEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYtpn 289

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958794731 1636 --EVKA--AQLDGLEARMRSVLQAINLQVQI 1662
Cdd:COG3206    290 hpDVIAlrAQIAALRAQLQQEAQRILASLEA 320
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1453-1642 2.56e-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: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1453 EQLLQDAQRARSRAEGERQKAETVQAALEeaQRAqgaaqgairgavvdtkntEQTLQQVQERMAGTEQSLNSASER-ARq 1531
Cdd:pfam04012   28 EQAIRDMQSELVKARQALAQTIARQKQLE--RRL------------------EQQTEQAKKLEEKAQAALTKGNEElAR- 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1532 lhallEAL-KLKRAGNSLAASTAEetagsaQSRAREAEKQLREQVGDQYQTVRALaERKAEGVLA--AQARAEQLRDEAR 1608
Cdd:pfam04012   87 -----EALaEKKSLEKQAEALETQ------LAQQRSAVEQLRKQLAALETKIQQL-KAKKNLLKArlKAAKAQEAVQTSL 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958794731 1609 GLLQA--AQDKLQRLQ----ELEGTYE-----ENERELEVKAAQL 1642
Cdd:pfam04012  155 GSLSTssATDSFERIEekieEREARADaaaelASAVDLDAKLEQA 199
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 1343-1655 2.72e-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: 49.18  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETRRQA-------EEAQQRAQAA-LDKANASRGQVEQANQELRELIQNVKDFLSQEgadpdsiemvatrvldisi 1414
Cdd:COG3096    245 LEAIRVTQSDRdlfkhliTEATNYVAADyMRHANERRELSERALELRRELFGARRQLAEEQ------------------- 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1415 paspEQIQRLASEIAERVRSLADVDTilahtmgDVRRAE---QLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQ 1491
Cdd:COG3096    306 ----YRLVEMARELEELSARESDLEQ-------DYQAASdhlNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAA 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1492 GAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRA---GNSLAASTAEETAGSAQSRAREAE 1568
Cdd:COG3096    375 EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcgLPDLTPENAEDYLAAFRAKEQQAT 454

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1569 KQLREQ-----VGD----QYQTVRALAERKAEGVLAAQA--RAEQLRDEARGLlqaaQDKLQRLQELEGTYEENERELEV 1637
Cdd:COG3096    455 EEVLELeqklsVADaarrQFEKAYELVCKIAGEVERSQAwqTARELLRRYRSQ----QALAQRLQQLRAQLAELEQRLRQ 530

                          330       340
                   ....*....|....*....|.
gi 1958794731 1638 KAA---QLDGLEARMRSVLQA 1655
Cdd:COG3096    531 QQNaerLLEEFCQRIGQQLDA 551
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1350-1650 3.15e-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: 47.99  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1350 RRQAEEAQQRAQAALDKANA-SRGQVEQANQELRELIQNVKDFLSQegadpdsiemvatrvldisipaspeQIQRLASEI 1428
Cdd:pfam13868  118 AEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDERILEYLKE-------------------------KAEREEERE 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1429 AERVRSLADVDtilahtmgdvRRAEQLLQDAQRARS-RAEGERQKAETVQAALEEAQRAqgaaqgairgavvdtknteqt 1507
Cdd:pfam13868  173 AEREEIEEEKE----------REIARLRAQQEKAQDeKAERDELRAKLYQEEQERKERQ--------------------- 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1508 lqqvQERMAgteqslnsASERARQLHALLEALKLKRAGNSLaastaeetagsAQSRAREAEKQLREQVgdqyqtVRALAE 1587
Cdd:pfam13868  222 ----KEREE--------AEKKARQRQELQQAREEQIELKER-----------RLAEEAEREEEEFERM------LRKQAE 272

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1588 RKAEGVLAAQARAEQLRDEARGLLQAAQDK-LQRLQELEGTYEENERELEVKAAQLDGL-EARMR 1650
Cdd:pfam13868  273 DEEIEQEEAEKRRMKRLEHRRELEKQIEEReEQRAAEREEELEEGERLREEEAERRERIeEERQK 337
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1350-1656 3.27e-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: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1350 RRQAEEAQQRA-QAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEI 1428
Cdd:COG3064    119 KEKAEEAKRKAeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1429 AERVRSLADVDTILAHTMGDVRRAEqllQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL 1508
Cdd:COG3064    199 AAAALAAAAAAAAADAALLALAVAA---RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1509 QQVQERMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAER 1588
Cdd:COG3064    276 SGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGA 355

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1589 KAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQAI 1656
Cdd:COG3064    356 GALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
HBM pfam16591
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ...
 1430-1651 3.61e-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: 47.01  E-value: 3.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1430 ERVRSLADVDTILaHTMGDVRRAEqlLQDAQrarsrAEGERQKAETVQAALEE--AQRAQGAAQ----------GAIRGA 1497
Cdd:pfam16591    3 ERSDRMTDISQLN-DTLTDLRIAR--LQYML-----SNGDATAAQAVQKKLDElkQQLQQLKTTftspenvrllQEQLQL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1498 VVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlklkRAGNSLAASTAEETAGSAQSRAREAEKQLREQV-G 1576
Cdd:pfam16591   75 IQAYRKSFNELRAAYESRNASRQVMDSAAERALEAIDQLEA----EVLQTPEADSRRAAQYQAISELKRQVQMARYQVrG 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1577 DQYQTVRALAERKAEGVLAAQARAEQLRDeargllQAAQDKLQRLQELE---GTYEENERELEVKAAQLDGLEARMRS 1651
Cdd:pfam16591  151 YTFTPNEDSEQAAYQQLDAALASLDQLRQ------ALAGDPGAALQQLTsalQGYRDALDTFKAAVAAIEQARQEMTS 222
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1479-1617 3.79e-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: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1479 ALEEAQRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMAGT----EQSLNSASERARQLHA--LLEALKLK----RAGNS 1547
Cdd:TIGR02794   22 SLYHSVKPEPGGGAEIIQAVlVDPGAVAQQANRIQQQKKPAakkeQERQKKLEQQAEEAEKqrAAEQARQKeleqRAAAE 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1548 LAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEArgllQAAQDK 1617
Cdd:TIGR02794  102 KAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA----AEAKKK 167
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 1550-1661 4.15e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 45.70  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1550 ASTAEETAGSAQSRAREAEkQLREQVG---DQYQTVRALAERKAEGVL-AAQARAEQLRDEARGLLQAAQDKLQRLQELE 1625
Cdd:PRK14475    36 AGALDAYAAKIQAELDEAQ-RLREEAQallADVKAEREEAERQAAAMLaAAKADARRMEAEAKEKLEEQIKRRAEMAERK 114

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958794731 1626 GTYEENERELEVKAAQLDgLEARMRSVLQAINLQVQ 1661
Cdd:PRK14475   115 IAQAEAQAAADVKAAAVD-LAAQAAETVLAARLAGA 149
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 1343-1513 4.21e-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: 45.47  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1343 LSRVSETR-RQAEEAQQRAQAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvatrvldisipaSPEQI 1421
Cdd:pfam07321    4 LLRVKHLReDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAW--------------------------------RPQEE 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 QRLASEIAERVRSLADVDTILaHTMGDVRRAEQLL-QDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAIRGAVVD 1500
Cdd:pfam07321   52 QRLYAEIQGKLVLLKELEKVK-QQVALLRENEADLeKQVAEARQQLEAEREALRQARQALAEARRAV--EKFAELVRLVQ 128

                          170
                   ....*....|...
gi 1958794731 1501 TKntEQTLQQVQE 1513
Cdd:pfam07321  129 AE--ELRQQERQE 139
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
796-845 4.28e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 42.30  E-value: 4.28e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1958794731   796 CPCPEGpgsqRHFATSCHRDGYsqqiVCHCRAGYTGLRCEACAPGHFGDP 845
Cdd:smart00180    1 CDCDPG----GSASGTCDPDTG----QCECKPNVTGRRCDRCAPGYYGDG 42
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1355-1640 4.52e-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: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1355 EAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQEGADPDSIEMVATRVLDISIPASPEQIQRLASEIAERVRS 1434
Cdd:COG5185    272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1435 LADVDTILahtmgdVRRAEQLLQDAQRARSRAEGERQKA--ETVQAALEEAQRAQGAAQGAIRGAVVDT-KNTEQTLQQV 1511
Cdd:COG5185    352 LTENLEAI------KEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEEL 425

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1512 QERMAGTEQSLNSASERARQLHALLEalKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALaerkae 1591
Cdd:COG5185    426 QRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL------ 497

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1592 gvlaaQARAEQLRDEARGLLQAAQDKLQRLQELEGTyEENERELEVKAA 1640
Cdd:COG5185    498 -----KATLEKLRAKLERQLEGVRSKLDQVAESLKD-FMRARGYAHILA 540
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1420-1584 4.91e-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: 46.46  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1420 QIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGErqkAETVQAALEEAQRAQG---------AA 1490
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGnvrnnkeyeAL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1491 QGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKLKRAgNSLAASTAEETAgsAQSRAREAEKQ 1570
Cdd:COG1579     95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEE--LEAEREELAAK 171

                          170
                   ....*....|....
gi 1958794731 1571 LREQVGDQYQTVRA 1584
Cdd:COG1579    172 IPPELLALYERIRK 185
PRK09039 PRK09039
peptidoglycan -binding protein;
1513-1642 4.96e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.27  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1513 ERMAGTEQSLNsasERARQLHALLEALKLKRAGN-SLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAERKAE 1591
Cdd:PRK09039    46 REISGKDSALD---RLNSQIAELADLLSLERQGNqDLQDSVANLRASLSAA---EAERSRLQALLAELAGAGAAAEGRAG 119

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1592 GVLAAQARAEQLRDEARG---LLQ----AAQDKLQRLQELEGTYEENERELEVKAAQL 1642
Cdd:PRK09039   120 ELAQELDSEKQVSARALAqveLLNqqiaALRRQLAALEAALDASEKRDRESQAKIADL 177
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1503-1650 5.18e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 46.36  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1503 NTEQTLQQVQERMagtEQSLNSASERARQLHALLEALKLKRAgnslaasTAEETAGSAQSRAREAEKQLREQVGdqyqtv 1582
Cdd:COG1842     23 DPEKMLDQAIRDM---EEDLVEARQALAQVIANQKRLERQLE-------ELEAEAEKWEEKARLALEKGREDLA------ 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1583 RALAERKAEgvlaAQARAEQLRdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARMR 1650
Cdd:COG1842     87 REALERKAE----LEAQAEALE-AQLAQLEEQVEKLKEaLRQLESKLEELKAKKDTLKARAKAAKAQEK 150
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1398-1617 5.92e-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: 5.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1398 DPDSIEMVATRV-LDISIPASPEQ-----IQRLASE-----IAERVRSLADVDTILAHTmgDVRRAEQLLQDAQRARSRA 1466
Cdd:TIGR02794   44 DPGAVAQQANRIqQQKKPAAKKEQerqkkLEQQAEEaekqrAAEQARQKELEQRAAAEK--AAKQAEQAAKQAEEKQKQA 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1467 EGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTL--QQVQERMAGTEQSLNSASERARQlhALLEALKLKra 1544
Cdd:TIGR02794  122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEAEAK--AKAEEAKAK-- 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1545 gnslaASTAEETAGS-AQSRArEAEKQLREqvgdqyqtvRALAERKAE-------GVLAAQARAEQLRDEARGLLQAAQD 1616
Cdd:TIGR02794  198 -----AEAAKAKAAAeAAAKA-EAEAAAAA---------AAEAERKADeaelgdiFGLASGSNAEKQGGARGAAAGSEVD 262


                   .
gi 1958794731 1617 K 1617
Cdd:TIGR02794  263 K 263
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1419-1657 6.05e-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: 6.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1419 EQIQRLASEIAERVRSLADVDTILAHTMgdvrraEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAqgAAQGAIRgav 1498
Cdd:smart00283    7 EEIAAGAEEQAEELEELAERMEELSASI------EEVAANADEIAATAQSAAEAAEEGREAVEDAITA--MDQIREV--- 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1499 vdTKNTEQTLQQVQERMAGTEQSLNSASERARQ-----LHALLEAlklKRAGNS------LAA---STAEETAGSA---Q 1561
Cdd:smart00283   76 --VEEAVSAVEELEESSDEIGEIVSVIDDIADQtnllaLNAAIEA---ARAGEAgrgfavVADevrKLAERSAESAkeiE 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  1562 SRAREAEKQLREQVGDQYQTVR------ALAERK-------AEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTY 1628
Cdd:smart00283  151 SLIKEIQEETNEAVAAMEESSSeveegvELVEETgdaleeiVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVT 230

                           250       260
                    ....*....|....*....|....*....
gi 1958794731  1629 EENERELEVKAAQLDGLEARMRSVLQAIN 1657
Cdd:smart00283  231 QETAAMSEEISAAAEELSGLAEELDELVE 259
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
1344-1623 7.07e-05

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 46.58  E-value: 7.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1344 SRVSETRRQAEEAQQRAqAALDKANASRGQVEQANQELRELiqnvkdflsqegadpdsiemvATRVLDISIPASPEQIQR 1423
Cdd:COG4223      7 AAVAELPAQLTALEQRL-AALEAAPAAAAATAALEARLAAL---------------------RAALAAAREAVAAAAAAA 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1424 LASEIAErvrsladvdtilahtmgdvrraeqlLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQG------AIRGA 1497
Cdd:COG4223     65 LEARLAA-------------------------LEAKAAAPEAEAAAAARAAALALAAAALRAAVERGQPfaaelaALEAL 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1498 VVDTKNTEQtLQQVQERmaGTEqslnSASERARQLHALLEALklkragnsLAASTAEETAGSAQSRAREAekqLREQVgd 1577
Cdd:COG4223    120 APDAPALAA-LAAFAAT--GVP----TLAALRAEFPAAARAA--------LAAARAPEADASWLDRLLAF---ARSLV-- 179

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958794731 1578 qyqTVRALAERKAEGVLAAQARAEQ-LRdeaRGLLQAAQDKLQRLQE 1623
Cdd:COG4223    180 ---TVRRVGPVEGDDPDAILARAEAaLA---AGDLAGALAELEALPE 220
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1345-1572 7.22e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.83  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1345 RVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQ------NVKDFLSQEGADPDSIE--------MVATRVL 1410
Cdd:COG1340     51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREeldelrKELAELNKAGGSIDKLRkeierlewRQQTEVL 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1411 disipaSPEQIQRLASEIAErvrsladvdtiLAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEE-AQRAQga 1489
Cdd:COG1340    131 ------SPEEEKELVEKIKE-----------LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQ-- 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1490 aqgAIRGAVVDTKnteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK---------LKRAGNSLAASTAEETAGSA 1560
Cdd:COG1340    192 ---ELHEEMIELY---KEADELRKEADELHKEIVEAQEKADELHEEIIELQkelrelrkeLKKLRKKQRALKREKEKEEL 265

                          250
                   ....*....|..
gi 1958794731 1561 QSRAREAEKQLR 1572
Cdd:COG1340    266 EEKAEEIFEKLK 277
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 1443-1626 7.97e-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: 46.83  E-value: 7.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1443 AHTMGDVRRAEQLLqdaQRARSRAEGERQKAETVQAaleEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSL 1522
Cdd:COG3071     60 AQALGDYERRDEYL---AQALELAPEAELAVLLTRA---ELLLDQGQAEQAL-----------ATLEALRAGAPRHPQVL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1523 NSASERARQLHALLEALKLKRAGNSLAASTAEEtagsAQSRAREAEKQLREQVGDQYQTVRAL------AERKAEGVLAA 1596
Cdd:COG3071    123 RLLLQAYRQLGDWEELLELLPALRKHKALSAEE----AQALERRAYLGLLRQAARDAEALKALwkalprAERRDPELAAA 198

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958794731 1597 QARA-EQLRD--EARGLLQAAQDK------LQRLQELEG 1626
Cdd:COG3071    199 YARAlIALGDhdEAERLLREALKRqwdprlVRLYGRLQG 237
Alanine_zipper pfam11839
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ...
 1450-1491 7.98e-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: 7.98e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958794731 1450 RRAEQLLQDAQRARSRAEGERQKA----ETVQAALEEAQRAQGAAQ 1491
Cdd:pfam11839    8 SKADQAEQDAAAAQSAADSAKAKAdeaaARANAAEAAAEEAQQAAE 53
PRK12472 PRK12472
hypothetical protein; Provisional
 1472-1616 8.78e-05

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 47.17  E-value: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1472 KAETVQAALEEAQRAQGAAQGAIRGAVvDTKNTEQTLQQVQERMAGTEQSLNSASERArqlhallEAlKLKRAGNSLAAS 1551
Cdd:PRK12472   181 KAEALAAAPARAETLAREAEDAARAAD-EAKTAAAAAAREAAPLKASLRKLERAKARA-------DA-ELKRADKALAAA 251

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1552 TAEETAGSAQSRAREAEKQLREqVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAQD 1616
Cdd:PRK12472   252 KTDEAKARAEERQQKAAQQAAE-AATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATD 315
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1562-1657 8.78e-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: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1562 SRAREAEKQLREQVgDQYQTVRALAERKAEgvlaAQARAEQLRDEARGL-LQAAQDKL----QRLQELEGTYEENERELE 1636
Cdd:COG4913    238 ERAHEALEDAREQI-ELLEPIRELAERYAA----ARERLAELEYLRAALrLWFAQRRLelleAELEELRAELARLEAELE 312

                           90       100
                   ....*....|....*....|.
gi 1958794731 1637 VKAAQLDGLEARMRSVLQAIN 1657
Cdd:COG4913    313 RLEARLDALREELDELEAQIR 333
T3SSipB pfam16535
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ...
 1529-1647 9.20e-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: 9.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1529 ARQLHALLEALKLKRAGNSLAASTAEETAGSAQSrarEAEKQLREQVGDQYQTVRALAE---RKAEGVLAAQARAEQLRD 1605
Cdd:pfam16535    1 AGQLTLLLGNLMSLLGEVSLSQLESRIAAWKAMQ---EAQQQKGLELSDEFQTALSEAEeatDAYEKAINKLKNAKSKAK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958794731 1606 EARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEA 1647
Cdd:pfam16535   78 AAEKKIDQAQTRLQSLAPDSPGKAKLEAAEQQAGIKKDALQA 119
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1446-1641 9.70e-05

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 46.90  E-value: 9.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1446 MGDVRRAEQLLQDA-QRARSRAEGE---RQKAEtvQAALEEAQRAQGAAQgairgavvdTKNTEQTLQQVQERMAgtEQS 1521
Cdd:PRK07735     1 MDPEKDLEDLKKEAaRRAKEEARKRlvaKHGAE--ISKLEEENREKEKAL---------PKNDDMTIEEAKRRAA--AAA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1522 LNSASERARQLHALLEALklkrAGNSLAASTAEeTAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGvlAAQARAE 1601
Cdd:PRK07735    68 KAKAAALAKQKREGTEEV----TEEEKAKAKAK-AAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAA--AAKAKAA 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958794731 1602 QLRDEARGllqaaqdklqrlQELEGTYEENERELEVKAAQ 1641
Cdd:PRK07735   141 ALAKQKRE------------GTEEVTEEEEETDKEKAKAK 168
FliJ pfam02050
Flagellar FliJ protein;
1471-1606 1.22e-04

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 43.42  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1471 QKAETvqaALEEAQRAQGAAQGAIRgavvdtkNTEQTLQQVQERMAGTEQSLNSASERARQ--LHALLEALKLKRagNSL 1548
Cdd:pfam02050    1 DEAAR---ELAEAQRELQQAEEKLE-------ELQQYRAEYQQQLSGAGQGISAAELRNYQafISQLDEAIAQQQ--QEL 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1549 AASTAEetagsaQSRAREA--EKQLReqvgdqYQTVRALAERKAEGVLAAQARAEQLR-DE 1606
Cdd:pfam02050   69 AQAEAQ------VEKAREEwqEARQE------RKSLEKLREREKKEERKEQNRREQKQlDE 117
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1311-1661 1.32e-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: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1311 CSGAAATADLALGRARHTQAELQRALVEGGGIL-------------------SRVSETRRQAEEAQQRAQAAL----DKA 1367
Cdd:TIGR00606  632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLrlapDKL 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1368 NASRGQVEQANQELRELI------QNVKDFLSQEgadpdsiemvatrvldisIPASPEQIQRLASEIAERVRSLADVDTI 1441
Cdd:TIGR00606  712 KSTESELKKKEKRRDEMLglapgrQSIIDLKEKE------------------IPELRNKLQKVNRDIQRLKNDIEEQETL 773

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1442 LAHTMGDVRRAEQLLQDAqrarsraegerQKAETVQAALEEAQR--AQGAAQgairgavVDTKNTEQTLQQVQERMAGTE 1519
Cdd:TIGR00606  774 LGTIMPEEESAKVCLTDV-----------TIMERFQMELKDVERkiAQQAAK-------LQGSDLDRTVQQVNQEKQEKQ 835

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1520 QSLNSASERARQLHALLE-----ALKLKRAGNSLaaSTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVL 1594
Cdd:TIGR00606  836 HELDTVVSKIELNRKLIQdqqeqIQHLKSKTNEL--KSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1595 AAQARaEQLRDEARGLL-------QAAQDKLQRLQE-----------LEGTYEE--------NERELEVKAAQLDGLEAR 1648
Cdd:TIGR00606  914 LETFL-EKDQQEKEELIssketsnKKAQDKVNDIKEkvknihgymkdIENKIQDgkddylkqKETELNTVNAQLEECEKH 992

                          410       420
                   ....*....|....*....|
gi 1958794731 1649 -------MRSVLQAINLQVQ 1661
Cdd:TIGR00606  993 qekinedMRLMRQDIDTQKI 1012
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1318-1657 1.35e-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: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1318 ADLALGRARHTQAELQRALVEGGGILSRVSETRRQAEEAQQRA-----QAAL----DKANASRGQVEQANQELRELIQNV 1388
Cdd:pfam12128  651 ARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQldkkhQAWLeeqkEQKREARTEKQAYWQVVEGALDAQ 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1389 KDFLSQE--------GADPDSIEMVATRVLDiSIPASPEQIQRLASEIAERVRSLADVdtilAHTMGDVRRAEQLLQDA- 1459
Cdd:pfam12128  731 LALLKAAiaarrsgaKAELKALETWYKRDLA-SLGVDPDVIAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETw 805

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 ----QRARSRAEGERQKAETVQ---AALEEAQRAQGAA----QGAIRGAVVDTKNTEQTLQQVQERMA------GTEQSL 1522
Cdd:pfam12128  806 lqrrPRLATQLSNIERAISELQqqlARLIADTKLRRAKlemeRKASEKQQVRLSENLRGLRCEMSKLAtlkedaNSEQAQ 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1523 NSASERARQlhalLEALKLKRAGNSLAASTAEE---TAGSAQSRAREAEKQLREQVGDQYQT---VRALAERKAEGVLA- 1595
Cdd:pfam12128  886 GSIGERLAQ----LEDLKLKRDYLSESVKKYVEhfkNVIADHSGSGLAETWESLREEDHYQNdkgIRLLDYRKLVPYLEq 961

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794731 1596 -AQARAEQ----LRDEARGLLQAAQDKLQRLQELEGTYEENEREL--EVKA-AQLDGL---EARMRSVLQAIN 1657
Cdd:pfam12128  962 wFDVRVPQsimvLREQVSILGVDLTEFYDVLADFDRRIASFSRELqrEVGEeAFFEGVsesAVRIRSKVSELE 1034
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 1453-1639 1.43e-04

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: 44.18  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1453 EQLLQDAQRARSRAEGERQKA-ETVQAALEEAqraqgaaqgaiRGAVvdTKNTEQTLQQVQERMAGTEQSLNSASER--- 1528
Cdd:pfam01442   18 EQLGPVAQELVDRLEKETEALrERLQKDLEEV-----------RAKL--EPYLEELQAKLGQNVEELRQRLEPYTEElrk 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1529 --ARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVgdqyqtvralaerkaegvlaaQARAEQLRDE 1606
Cdd:pfam01442   85 rlNADAEELQEKLAPYGEE---LRERLEQNVDALRARLAPYAEELRQKL---------------------AERLEELKES 140

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958794731 1607 ARGLLQAAQDKL-QRLQELEGTYEENERELEVKA 1639
Cdd:pfam01442  141 LAPYAEEVQAQLsQRLQELREKLEPQAEDLREKL 174
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1565-1661 2.00e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.43  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1565 REAEKQL---REQVGDQyQTVRALAERKAEgvlAAQARAEQLRDEARGLLQAAQDKL-----QRLQELEGTYEENERELE 1636
Cdd:COG1842     33 RDMEEDLveaRQALAQV-IANQKRLERQLE---ELEAEAEKWEEKARLALEKGREDLarealERKAELEAQAEALEAQLA 108

                           90       100
                   ....*....|....*....|....*
gi 1958794731 1637 vkaaQLDGLEARMRSVLQAINLQVQ 1661
Cdd:COG1842    109 ----QLEEQVEKLKEALRQLESKLE 129
Filament pfam00038
Intermediate filament protein;
1419-1664 2.02e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.30  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQ----RLASEIaERVRSLADVDTILAhtmgdvRRAEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQGAI 1494
Cdd:pfam00038    4 EQLQelndRLASYI-DKVRFLEQQNKLLE------TKISELRQKKGAEPSRLY------SLYEKEIEDLRRQLDTLTVER 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1495 RGAVVDTKNTEQTLQQVQERMAgTEQSLNSASERA-----RQLHAL-LEALKLKRAGNSLAastaEETAgsAQSRAREAE 1568
Cdd:pfam00038   71 ARLQLELDNLRLAAEDFRQKYE-DELNLRTSAENDlvglrKDLDEAtLARVDLEAKIESLK----EELA--FLKKNHEEE 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1569 -KQLREQVGDQYQTV-----------RALAERKAE-GVLAA----------QARAEQLRDEARGLLQAAQDKLQRLQELE 1625
Cdd:pfam00038  144 vRELQAQVSDTQVNVemdaarkldltSALAEIRAQyEEIAAknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELR 223

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958794731 1626 GTYEENERELEVKAAQLDGLEARMRSVLQAINLQVQIYN 1664
Cdd:pfam00038  224 RTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQ 262
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1513-1620 2.06e-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: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1513 ERMAGTEQSLNSASERARQLHALLEALKLKRAGnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEg 1592
Cdd:COG0711     31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAE---ARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE- 106

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958794731 1593 vlAAQARA-EQLRDEARGL-LQAAQDKLQR 1620
Cdd:COG0711    107 --QERAKAlAELRAEVADLaVAIAEKILGK 134
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1419-1603 2.13e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 45.74  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRLASEIAERVRSLADVDTIlahtmgDVRRAEQLLQDAQRARSrAEGERQKAETVQAALEE--AQRAQGAAQGAIRG 1496
Cdd:PRK07735    32 AEISKLEEENREKEKALPKNDDM------TIEEAKRRAAAAAKAKA-AALAKQKREGTEEVTEEekAKAKAKAAAAAKAK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1497 AVVDTKNTEQTLQQVQE------RMAGTEQSLNSASERARQLHALLEALKLKRAGNSLAASTAEETAGS-AQSRAREAEK 1569
Cdd:PRK07735   105 AAALAKQKREGTEEVTEeekaaaKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAkAKAAALAKQK 184

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958794731 1570 QLREQVGDQYQTVRALAERKAEGVLAAQARAEQL 1603
Cdd:PRK07735   185 AAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAL 218
PRK11281 PRK11281
mechanosensitive channel MscK;
1454-1657 2.38e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1454 QLLQDAQRARSRAEGERQKAETVQAALEEAQRaQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASErarqlh 1533
Cdd:PRK11281    70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA-ELEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQN------ 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1534 ALLEAlklkragNSLAAS--TAEETAGSAQSRAREAEKQLREQvgdqyqtvraLAERKAEGvlaaqaraEQLRDEARGLL 1611
Cdd:PRK11281   143 DLAEY-------NSQLVSlqTQPERAQAALYANSQRLQQIRNL----------LKGGKVGG--------KALRPSQRVLL 197

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1612 QA------AQDKLQRlQELEG-----TYEENERELevKAAQLDGLEaRMRSVLQ-AIN 1657
Cdd:PRK11281   198 QAeqallnAQNDLQR-KSLEGntqlqDLLQKQRDY--LTARIQRLE-HQLQLLQeAIN 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1314-1534 2.46e-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: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1314 AAATADLALGRARHTQAELQRALVEGggILSRVSETRRQAEEAQQRAQAALDKANASRgQVEQANQELRELIqnvkdfls 1393
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEA--ELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLD-------- 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1394 qegadpdsiemvatrvldisipASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA 1473
Cdd:COG4913    682 ----------------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---QDRL 736

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1474 ETVQAALEEAQRAQGAAQgaiRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHA 1534
Cdd:COG4913    737 EAAEDLARLELRALLEER---FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1560-1662 2.59e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.04  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1560 AQSRAREAEKQLrEQVGDQYQTVRALAERKAEgVLAAQARAEQLRDEARGLLQAAQDKL---QRLQELEGTYEENERELE 1636
Cdd:COG1566     88 AEAQLAAAEAQL-ARLEAELGAEAEIAAAEAQ-LAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDAAQAQLE 165

                           90       100
                   ....*....|....*....|....*.
gi 1958794731 1637 VKAAQLDGLEARMRSVLQAINLQVQI 1662
Cdd:COG1566    166 AAQAQLAQAQAGLREEEELAAAQAQV 191
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1321-1516 2.64e-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: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1321 ALGRARHTQ----AELQRALVEGGGILsRVSETRRQAEEAQQRAQAALDKAnasrgQVEQANQELRELIQNVKdfLSQEG 1396
Cdd:COG2268    188 ALGRRKIAEiirdARIAEAEAERETEI-AIAQANREAEEAELEQEREIETA-----RIAEAEAELAKKKAEER--REAET 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1397 AdpdsiEMVATRVLDISIPASPEQIQRLAsEIAERVRSLAdvdtiLAHtmgdvRRAEQLLQDAQRA-RSRAEGERQKAET 1475
Cdd:COG2268    260 A-----RAEAEAAYEIAEANAEREVQRQL-EIAEREREIE-----LQE-----KEAEREEAELEADvRKPAEAEKQAAEA 323

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1476 VQAALEEAQRAQGAAQGAIRGAVVDTKNTE----------QTLQQVQERMA 1516
Cdd:COG2268    324 EAEAEAEAIRAKGLAEAEGKRALAEAWNKLgdaaillmliEKLPEIAEAAA 374
PRK12472 PRK12472
hypothetical protein; Provisional
 1414-1569 2.65e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 45.63  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1414 IPASPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEgerqkaetvqAALEEAQRAQGAAQga 1493
Cdd:PRK12472   185 LAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARAD----------AELKRADKALAAAK-- 252

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1494 irgavvdtknTEQTLQQVQERMAGTEQslnSASERARQLHALLEALKLKRAgnslAASTAEETAGSAQSRAREAEK 1569
Cdd:PRK12472   253 ----------TDEAKARAEERQQKAAQ---QAAEAATQLDTAKADAEAKRA----AAAATKEAAKAAAAKKAETAK 311
Ala_zip_lipo NF040598
Lpp/OprI family alanine-zipper lipoprotein; This model derives from PF11839 but is more ...
 1451-1486 2.88e-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: 2.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAEQLLQDAQRARSRAEGERQKAE----TVQAALEEAQRA 1486
Cdd:NF040598    37 KVDQASSDAAAAQSRADEAAAKAEqaeaAANAAQQEADEA 76
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1504-1656 2.88e-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: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1504 TEQTLQQVQERMA-----GTE-----QSLNSASERARQLHALLEALKLKRAgnSLAASTAEEtagsAQSRAREAEKQLRE 1573
Cdd:COG1196    177 AERKLEATEENLErlediLGElerqlEPLERQAEKAERYRELKEELKELEA--ELLLLKLRE----LEAELEELEAELEE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1574 qvgdqyqtvralAERKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQ----ELEGTYEENERELEVKAAQLDGLEARM 1649
Cdd:COG1196    251 ------------LEAELEELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERL 318


                   ....*..
gi 1958794731 1650 RSVLQAI 1656
Cdd:COG1196    319 EELEEEL 325
DUF4398 pfam14346
Domain of unknown function (DUF4398); This family of proteins is functionally uncharacterized. ...
 1312-1377 2.92e-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: 2.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1312 SGAAATADLALGRARHTQAELQRALVEGggilsRVSETRRQAEEAQQRAQAALDKANA--SRGQVEQA 1377
Cdd:pfam14346   16 DGAAQYAPLELKRARDALAKAEAAMAEK-----DYEKARHLAYLAEADAELAEAKARAakAEAAAAQA 78
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 1320-1575 3.10e-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: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1320 LALGRARHTQAELQRALvegggilsRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQnvkdflsqegADP 1399
Cdd:COG2956     46 LALGNLYRRRGEYDRAI--------RIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE----------LDP 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEmVATRVLDISipaspEQIQRL--ASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQ 1477
Cdd:COG2956    108 DDAE-ALRLLAEIY-----EQEGDWekAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1478 AALEEAQRAQGAAQGAIrgavvdtknteQTLQQVQERMAGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEET 1556
Cdd:COG2956    182 LLLAELYLEQGDYEEAI-----------AALERALEQDPDYLPALPRLAELYEKLGDPEEALElLRKALELDPSDDLLLA 250

                          250       260
                   ....*....|....*....|..
gi 1958794731 1557 AGS---AQSRAREAEKQLREQV 1575
Cdd:COG2956    251 LADlleRKEGLEAALALLERQL 272
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 1502-1649 3.59e-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: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1502 KNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlkragnslaastaeETAGSAQSRAREAEKQLREQVgdqyqt 1581
Cdd:pfam04012   25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQT--------------EQAKKLEEKAQAALTKGNEEL------ 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1582 VRALAERKAEgvLAAQARAEQlrdEARGLLQAAQDKLQR-LQELEGTYEENERELEVKAAQLDGLEARM 1649
Cdd:pfam04012   85 AREALAEKKS--LEKQAEALE---TQLAQQRSAVEQLRKqLAALETKIQQLKAKKNLLKARLKAAKAQE 148
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1430-1650 3.74e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1430 ERVRSLADVDTILAHTMGDVRRaeQLLQDAQRARSRAEGERQKA-ETVQAALEEA-----QRAQGAAQG----------- 1492
Cdd:PHA03247  1552 ERVDQSPVKDTAYAEYVAFVAR--RDLAEAKDALVRAKQQRAEAtDRVTAALREAlaaheRRAQSEAESlanlktllrva 1629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1493 AIRGAVVDT----KNTEQTLQQVQERMAGTEQS--LNSAS----ERARQL---HALLEALK-----LKRAGNSLAASTAE 1554
Cdd:PHA03247  1630 AIPATAAKTldqaRSVAEIVDQIELLLEQTEKAaeLDVAAvdwlEHARRVfeaHPLTAARGggpdpLARLHARLDALGET 1709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1555 ETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLRDEARGLL----QAAQDKL-QRLQELEGTyE 1629
Cdd:PHA03247  1710 RRRTEALRRSLEAAEAEWDEVWGRFGRVRGGAWKSPEALRAAREQLRALQTATNTVLglraDAHYERLpAKYQGALGA-K 1788

                          250       260
                   ....*....|....*....|....*.
gi 1958794731 1630 ENER-----ELEVKAAQLDGLEARMR 1650
Cdd:PHA03247  1789 SAERagaveELGAAVARHDGLLARLR 1814
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1350-1650 3.80e-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: 44.52  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1350 RRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDflsQEgadpdsiemvatRVLDisipaspEQIQRLASEIA 1429
Cdd:pfam13868  108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EE------------REED-------ERILEYLKEKA 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1430 ERVRSladvdtilahtmgdvRRAEQLLQDAQRARsraegERQKaetVQAALEEAQRAQgAAQGAIRgavvdtkntEQTLQ 1509
Cdd:pfam13868  166 EREEE---------------REAEREEIEEEKER-----EIAR---LRAQQEKAQDEK-AERDELR---------AKLYQ 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1510 QVQERMagteqslnsasERARQLHALLEALKLKRAgnslaastaeetagsaQSRAREAEKQLREQvgdQYQTVRALAERK 1589
Cdd:pfam13868  213 EEQERK-----------ERQKEREEAEKKARQRQE----------------LQQAREEQIELKER---RLAEEAEREEEE 262

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794731 1590 AEGVLAAQA---RAEQLRDEARgllqaAQDKLQRLQELEGTYEENE--RELEVKAAQLDGLEARMR 1650
Cdd:pfam13868  263 FERMLRKQAedeEIEQEEAEKR-----RMKRLEHRRELEKQIEEREeqRAAEREEELEEGERLREE 323
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 ...
 1507-1603 3.94e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 42.30  E-value: 3.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1507 TLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQtvRALA 1586
Cdd:pfam00430   38 EIAEAEERRKDAAAALAEAEQQLKE--ARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKD--RALA 113

                           90
                   ....*....|....*..
gi 1958794731 1587 ERKAEGVLAAQARAEQL 1603
Cdd:pfam00430  114 ELRQQVVALAVQIAEKL 130
COG4223 COG4223
Uncharacterized conserved protein [Function unknown];
1478-1655 4.00e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443367 [Multi-domain]  Cd Length: 259  Bit Score: 44.27  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1478 AALEEAQRAQGA-AQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEALKlKRAGNSLAASTAEET 1556
Cdd:COG4223     24 AALEAAPAAAAAtAALEARLAALRAALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAA-RAAALALAAAALRAA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1557 AGSAQSRAREAEkQLREQVGDQyQTVRALAERKAEGVLAAQARAEQLRDEARGLLQAAqdklqrlqelegtyeeneRELE 1636
Cdd:COG4223    103 VERGQPFAAELA-ALEALAPDA-PALAALAAFAATGVPTLAALRAEFPAAARAALAAA------------------RAPE 162

                          170
                   ....*....|....*....
gi 1958794731 1637 VKAAQLDGLEARMRSVLQA 1655
Cdd:COG4223    163 ADASWLDRLLAFARSLVTV 181
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 1335-1622 4.37e-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: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1335 ALVEGGGILSRVSETRRQaEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLsqEGADPDSIEMVATRVLDiSI 1414
Cdd:NF012221  1536 ATSESSQQADAVSKHAKQ-DDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQL--ESTDQNALETNGQAQRD-AI 1611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1415 PASPEQIQRLASEIAERVRSLADVDTiLAHTMGDVRR---AEQLLQDAQRARSRAEgerqkaETVQAALEEAQRAQGAAQ 1491
Cdd:NF012221  1612 LEESRAVTKELTTLAQGLDALDSQAT-YAGESGDQWRnpfAGGLLDRVQEQLDDAK------KISGKQLADAKQRHVDNQ 1684

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1492 GAIRGAVvdtKNTEQTLQQVQERMAGTEQSLNSASERA--RQLHALL---EALKLKRAGNSLA----------ASTAEET 1556
Cdd:NF012221  1685 QKVKDAV---AKSEAGVAQGEQNQANAEQDIDDAKADAekRKDDALAkqnEAQQAESDANAAAndaqsrgeqdASAAENK 1761

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1557 AGSAQSRAR-----EAEKQLREQV------GDQYqTVRALAER----KAEGVLAAQAR-AEQLRDEARGLLQAAQDKLQR 1620
Cdd:NF012221  1762 ANQAQADAKgakqdESDKPNRQGAagsglsGKAY-SVEGVAEPgshiNPDSPAAADGRfSEGLTEQEQEALEGATNAVNR 1840


                   ..
gi 1958794731 1621 LQ 1622
Cdd:NF012221  1841 LQ 1842
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 1437-1636 4.41e-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: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1437 DVDTILAHTMGDVRRAEQLLQDAQRARSRAEGERQkaETVQAALEEAQRAQGAAQgairgavVDTKNTeQTLQQVQERMA 1516
Cdd:cd07596      1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRR--ELGSALGEFGKALIKLAK-------CEEEVG-GELGEALSKLG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1517 GTEQSLNSASERA--RQLHALLEALKlkragnslaastaeETAGSAQSrAREAEKQlREQVGDQYQTV-------RALAE 1587
Cdd:cd07596     71 KAAEELSSLSEAQanQELVKLLEPLK--------------EYLRYCQA-VKETLDD-RADALLTLQSLkkdlaskKAQLE 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958794731 1588 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEgtyEENERELE 1636
Cdd:cd07596    135 KLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEIS---ERLKEELK 180
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
746-785 4.76e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 4.76e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1958794731   746 CVCNGR---ADECDAHTGACLgCRDYTGGEHCERCIAGFHGDP 785
Cdd:smart00180    1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1428-1625 4.95e-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: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1428 IAErVRSLADVDTILAHTMGDVRRAEQ--------LLQDAQRAR---SRAEGERQKAEtvQAALEEAQRAQGAAQgairg 1496
Cdd:COG2268    194 IAE-IIRDARIAEAEAERETEIAIAQAnreaeeaeLEQEREIETariAEAEAELAKKK--AEERREAETARAEAE----- 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1497 avvdtknteqtlQQVQERMAGTEQSLNSASERARQLHALleALKLKRagnslaastaeetagsAQSRAREAEKQLREQVG 1576
Cdd:COG2268    266 ------------AAYEIAEANAEREVQRQLEIAEREREI--ELQEKE----------------AEREEAELEADVRKPAE 315

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1577 DQYQTVRALAERKAEGVLA---AQARAEQLRDEARGLLQAAQDKLQRLQELE 1625
Cdd:COG2268    316 AEKQAAEAEAEAEAEAIRAkglAEAEGKRALAEAWNKLGDAAILLMLIEKLP 367
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 1451-1641 5.10e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAEQLLQDAQRA-----RSRAEGERqKAETVQAALEEAqraqgaaqgairgavVDTKNTEQT-LQQVQERMAGTEQSLNS 1524
Cdd:pfam05557   10 RLSQLQNEKKQMelehkRARIELEK-KASALKRQLDRE---------------SDRNQELQKrIRLLEKREAEAEEALRE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1525 ASERARQLHALLEALKLKRAGNSLAASTAEETAGSAQSRARE-------AEKQLREQVGDQYQTVRALAERKAEgvlaaQ 1597
Cdd:pfam05557   74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSElrrqiqrAELELQSTNSELEELQERLDLLKAK-----A 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1598 ARAEQLRDEarglLQAAQDKL----QRLQELEgtYE---ENERELEVKAAQ 1641
Cdd:pfam05557  149 SEAEQLRQN----LEKQQSSLaeaeQRIKELE--FEiqsQEQDSEIVKNSK 193
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 1443-1614 5.26e-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: 44.13  E-value: 5.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1443 AHTMGDVRRAEQLLQ--DAQRARSRAEGERQKA---ETVQAALEEAQRAQGAAQGAI--------RGAVvdtknTEQTLQ 1509
Cdd:COG3071     83 AELAVLLTRAELLLDqgQAEQALATLEALRAGAprhPQVLRLLLQAYRQLGDWEELLellpalrkHKAL-----SAEEAQ 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1510 QVQERMAgtEQSLNSASERARQLHALLEAL-KLKRAGNSLAASTAEetAGSAQSRAREAEKQLREQVGDQYQT--VRALA 1586
Cdd:COG3071    158 ALERRAY--LGLLRQAARDAEALKALWKALpRAERRDPELAAAYAR--ALIALGDHDEAERLLREALKRQWDPrlVRLYG 233

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1587 ERKAEGVLAAQARAE-----------------------QLRDEARGLLQAA 1614
Cdd:COG3071    234 RLQGGDPAKQLKRAEkwlkkhpndpdlllalgrlclrnQLWGKAREYLEAA 284
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 1482-1629 5.53e-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: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1482 EAQRAQGAAQGAIRGAVVDTKnTEQTLQQVQERMAGTEQSLNsaseRARQLHALLEALKLKRAgnslAASTAEETAGSAQ 1561
Cdd:pfam15070   10 QTERDQYAENLKEEGAVWQQK-MQQLSEQVRTLREEKERSVS----QVQELETSLAELKNQAA----VPPAEEEQPPAGP 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1562 SrarEAEKQLREQVGDQYQTVRALAerkaegvlaAQARAeQLRDEArGLLQAAQDKLQRLQELEGTYE 1629
Cdd:pfam15070   81 S---EEEQRLQEEAEQLQKELEALA---------GQLQA-QVQDNE-QLSRLNQEQEQRLLELERAAE 134
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 1351-1526 6.09e-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: 6.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1351 RQAEEA-QQRAQAAL---------DKA-NASRGQVeqaNQELRELIQnvkdflsqEGADPDSIEMVATRVLDISIPaspE 1419
Cdd:COG0330    102 ENAEEAlRQLAESALrevigkmtlDEVlSTGRDEI---NAEIREELQ--------EALDPYGIEVVDVEIKDIDPP---E 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1420 QIQRlaseiaervrsladvdtilahTMGDVRRAEQllqDAQRARSRAEGERQKAETVqaALEEAQR----AQGAAQGAIR 1495
Cdd:COG0330    168 EVQD---------------------AMEDRMKAER---EREAAILEAEGYREAAIIR--AEGEAQRaiieAEAYREAQIL 221

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958794731 1496 GAVVDTKNTEQTLQQ-------VQERMAGT-EQSLNSAS 1526
Cdd:COG0330    222 RAEGEAEAFRIVAEAysaapfvLFYRSLEAlEEVLSPNS 260
PTZ00491 PTZ00491
major vault protein; Provisional
 1484-1656 6.91e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 44.62  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1484 QRAQGAAQGAIRGAV-VDTKNTEQTLQQVQERMagtEQSLNSASERAR---QLHALLEALKLKRAgnsLAASTAEETAGS 1559
Cdd:PTZ00491   643 ERTRDSLQKSVQLAIeITTKSQEAAARHQAELL---EQEARGRLERQKmhdKAKAEEQRTKLLEL---QAESAAVESSGQ 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1560 AQSRAR-EAEKqlreqvgdqyqtvrALAERKAEgVLAAQARAEQLRDEARGLLqaaqDKLQRLQELEGTYEENERELEV- 1637
Cdd:PTZ00491   717 SRAEALaEAEA--------------RLIEAEAE-VEQAELRAKALRIEAEAEL----EKLRKRQELELEYEQAQNELEIa 777

                          170       180
                   ....*....|....*....|
gi 1958794731 1638 KAAQLDGLEA-RMRSVLQAI 1656
Cdd:PTZ00491   778 KAKELADIEAtKFERIVEAL 797
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
1336-1483 7.39e-04

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


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 43.87  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1336 LVEGGGILSRVSETRRQAEEAQQRAQAALDKAnasRGQVEQANQELRELIQNVkdflsqegadpdsiemvatRVLDISIP 1415
Cdd:COG1538    250 LFDGGRNRARVRAAKAQLEQAEAQYEQTVLQA---LQEVEDALAALRAAREQL-------------------EALEEALE 307

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794731 1416 ASpEQIQRLAseiaeRVRSLADVDTILahtmgDVRRAEQLLQDAQRARSRAEGERQKAetvQAALEEA 1483
Cdd:COG1538    308 AA-EEALELA-----RARYRAGLASLL-----DVLDAQRELLQAQLNLIQARYDYLLA---LVQLYRA 361
DUF6781 pfam20572
Family of unknown function (DUF6781); This family of proteins is functionally uncharacterized. ...
 1486-1620 7.99e-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: 42.63  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1486 AQGAAQGAIRGAVVDTkntEQTLQQVqerMAGTEQSLNSASErARQLhALLEALK---------LKRAGNSLAA------ 1550
Cdd:pfam20572   56 TEGASQGANAARGGEV---EALLKQA---VAGLDDALLKAAE-ASRL-ALEEAVDqgaafseqdLKKALDDLEKledtff 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1551 ----STAEETAGSAQS------------------RAREAEKQLREQVGDqyqtvrALAERKAEGVLAAQARAEQLRDEAR 1608
Cdd:pfam20572  128 dtlrKAAKSAGGPLKGpwgdlldhlkrsgtdtgaQARAAVEQLAAQLQA------ALREGRAAGSRAARALADSYAALAS 201

                          170
                   ....*....|..
gi 1958794731 1609 GLLQAAQDKLQR 1620
Cdd:pfam20572  202 GVLIGLSEALQP 213
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 1335-1519 8.47e-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: 8.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1335 ALVEGGGILSRVSETRRQAEEAQqrAQAALDKAnasRGQVEQANQELRELiQNVKDFLSQEGADPDSIEmVATRVLDISI 1414
Cdd:pfam00529   40 DRVKAGDVLFQLDPTDYQAALDS--AEAQLAKA---QAQVARLQAELDRL-QALESELAISRQDYDGAT-AQLRAAQAAV 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1415 PASPEQIQrLASEIAERVRSLADVDTILAHTMGDVRRaeqLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaAQGAI 1494
Cdd:pfam00529  113 KAAQAQLA-QAQIDLARRRVLAPIGGISRESLVTAGA---LVAQAQANLLATVAQLDQIYVQITQSAAENQAE--VRSEL 186

                          170       180
                   ....*....|....*....|....*
gi 1958794731 1495 RGAVVDTKNTEQTLQQVQERMAGTE 1519
Cdd:pfam00529  187 SGAQLQIAEAEAELKLAKLDLERTE 211
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 1422-1511 8.76e-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: 40.50  E-value: 8.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1422 QRLASEIAERVRSLAD-VDTILAHTMGDVRRAEQ----LLQDAQ----------RARSRAEGERQKAETVQAALEEAQRA 1486
Cdd:pfam16999    4 SRLLSELAEREAALDQqIEAARKEAEREVEAAEAeaarILREAEakakalqaeyRQELAAETARIREEARARAEAEAQAV 83

                           90       100
                   ....*....|....*....|....*
gi 1958794731 1487 QGAAQGAIRGAVvdtkntEQTLQQV 1511
Cdd:pfam16999   84 RTRAEGRLQQAV------ELILRAV 102
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 1506-1644 9.48e-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: 43.90  E-value: 9.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1506 QTLQQVQERmagteqsLNSASERARQLHALLEALKLKRAGNSLAASTAEETA---------------------GSAQSRA 1564
Cdd:pfam15070  288 QELQETQER-------LEALTQQNQQLQAQLSLLANPGEGDGLESEEEEEEAprpslsipedfesreamvaffNSALAQA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1565 REAEKQLREQVGDQYQTVRALAERKAEG-------VLAAQARAEQLRDEARGLLQAAQDKLQ-RLQEL-EGTYEENER-- 1633
Cdd:pfam15070  361 EEERAELRRQLKEQKRRCRRLAQQAAPAqeepeheAHAPGTGGDSVPVEVHQALQVAMEKLQsRFTELmQEKADLKERve 440

                          170
                   ....*....|.
gi 1958794731 1634 ELEVKAAQLDG 1644
Cdd:pfam15070  441 ELEHRCIQLSG 451
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 1500-1626 1.12e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 41.48  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1500 DTKNTEQTLQQVQERMAGTEQSLNSASERARQLHALLEAlKLKRAGNSLAASTAEETAGSAQSRARE--AEKQlreqvgd 1577
Cdd:PRK07352    58 ALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKA-RAEAIRAEIEKQAIEDMARLKQTAAADlsAEQE------- 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1578 qyqtvRALAERKAEGVLAAQARAE-QLRDearGLLQAAQDKL--QRLQELEG 1626
Cdd:PRK07352   130 -----RVIAQLRREAAELAIAKAEsQLPG---RLDEDAQQRLidRSIANLGG 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1512-1662 1.14e-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: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1512 QERMAGTEQSLNSASERARQLHALLEalKLKRAgnslaASTAEEtAGSAQSRAREAEKQLReqvGDQYQTVRALAERKAE 1591
Cdd:COG1196    178 ERKLEATEENLERLEDILGELERQLE--PLERQ-----AEKAER-YRELKEELKELEAELL---LLKLRELEAELEELEA 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1592 GVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMRSVLQ-AINLQVQI 1662
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErRRELEERL 318
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1449-1623 1.21e-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: 42.05  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1449 VRRAEQLLQDAQRARS--RAEGERQKAETVQAALEEAQRA----QGAAQGAIRGAVVDTKNTEQTLQQVQER-------M 1515
Cdd:cd00176     16 LSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERvealNELGEQLIEEGHPDAEEIQERLEELNQRweelrelA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1516 AGTEQSLNSASERARQLHALLEALK-LKRAGNSLAASTAEETAGSAQSRAREaEKQLREQVgDQYQTVRALAERKAEGVL 1594
Cdd:cd00176     96 EERRQRLEEALDLQQFFRDADDLEQwLEEKEAALASEDLGKDLESVEELLKK-HKELEEEL-EAHEPRLKSLNELAEELL 173

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958794731 1595 AA---------QARAEQLRDEARGLLQAAQDKLQRLQE 1623
Cdd:cd00176    174 EEghpdadeeiEEKLEELNERWEELLELAEERQKKLEE 211
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1557-1656 1.31e-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: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1557 AGSAQSRAREAEKQLREQVGDQYQTVRAL---AERKAEGVLAAQARAEQLRDEARGLLQAAQdklQRLQELEGTYEENER 1633
Cdd:COG4942     14 AAAAQADAAAEAEAELEQLQQEIAELEKElaaLKKEEKALLKQLAALERRIAALARRIRALE---QELAALEAELAELEK 90

                           90       100
                   ....*....|....*....|...
gi 1958794731 1634 ELEVKAAQLDGLEARMRSVLQAI 1656
Cdd:COG4942     91 EIAELRAELEAQKEELAELLRAL 113
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
216-269 1.49e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 1.49e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794731   216 CECNG---HSHSCHFDmavylasgnvsGGVCDgCQHNTAGRHCELCRPFFYRDPTKD 269
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 1502-1659 1.65e-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: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1502 KNTEQTLQQVQERMAGTEQSLNSASERARQlhALLEALKLKRAGNSLaastaEETAGSAQSRAREAEKQLRE--QVGDQY 1579
Cdd:pfam00261    4 QQIKEELDEAEERLKEAMKKLEEAEKRAEK--AEAEVAALNRRIQLL-----EEELERTEERLAEALEKLEEaeKAADES 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1580 QTVR-ALAERKAEG-----VLAAQAR-AEQLRDEARGLLQAAQDKLQRLQ-ELEGTyEENERELEVKAAQldgLEARMRS 1651
Cdd:pfam00261   77 ERGRkVLENRALKDeekmeILEAQLKeAKEIAEEADRKYEEVARKLVVVEgDLERA-EERAELAESKIVE---LEEELKV 152


                   ....*...
gi 1958794731 1652 VLQaiNLQ 1659
Cdd:pfam00261  153 VGN--NLK 158
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1451-1642 1.69e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.25  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1451 RAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQgaIRGAVV----DTKNTEQTLQQVQERMAGTEQSL---- 1522
Cdd:PRK10246   251 RLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQ--LRPHWEriqeQSAALAHTRQQIEEVNTRLQSTMalra 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1523 ---NSASERARQLHALLEALKLKRAGNSLAASTAEETAG-----SAQSRAREAEKQLREQVGDQYQTVRALAE------- 1587
Cdd:PRK10246   329 rirHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLRQWQQQLTHAEQKLNALPAitltlta 408

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958794731 1588 RKAEGVLAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQL 1642
Cdd:PRK10246   409 DEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
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 ...
 1586-1662 2.05e-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: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1586 AERKAEGVLAAQARAEQL----RDEARGLLQAAQDKLQRL-QELEG-TYEENERELEVKAAQLDGLEARMRSVL--QAIN 1657
Cdd:pfam00430   42 AEERRKDAAAALAEAEQQlkeaRAEAQEIIENAKKRAEKLkEEIVAaAEAEAERIIEQAAAEIEQEKDRALAELrqQVVA 121


                   ....*
gi 1958794731 1658 LQVQI 1662
Cdd:pfam00430  122 LAVQI 126
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1419-1516 2.07e-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: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRLASEIAERVRSLADVDTILAhtmgdvrRAEQLLQDAQ------RARSRAEGERQKAETVQAALEEAQRAQGAAQG 1492
Cdd:COG0711     31 ERQEKIADGLAEAERAKEEAEAALA-------EYEEKLAEARaeaaeiIAEARKEAEAIAEEAKAEAEAEAERIIAQAEA 103

                           90       100
                   ....*....|....*....|....
gi 1958794731 1493 AIRGAVvdtkntEQTLQQVQERMA 1516
Cdd:COG0711    104 EIEQER------AKALAELRAEVA 121
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
1460-1641 2.19e-03

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 42.82  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1460 QRARSRAEGERQKAETVQAALEEAQRAQgaaqgairgavvdtkntEQTLQQVQERMagteqslnsasERARQLHALLEAL 1539
Cdd:COG1193    503 ERARELLGEESIDVEKLIEELERERREL-----------------EEEREEAERLR-----------EELEKLREELEEK 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1540 KLKragnslaastaeetagsaqsrAREAEKQLREQvgdqyqtvralAERKAEGVLA-AQARAEQLRDEAR---GLLQAAQ 1615
Cdd:COG1193    555 LEE---------------------LEEEKEEILEK-----------AREEAEEILReARKEAEELIRELReaqAEEEELK 602

                          170       180
                   ....*....|....*....|....*.
gi 1958794731 1616 DKLQRLQELEGTYEENERELEVKAAQ 1641
Cdd:COG1193    603 EARKKLEELKQELEEKLEKPKKKAKP 628
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1558-1662 2.44e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1558 GSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQLR---DEARGLLQAAQDKLQR----LQELEGTYEE 1630
Cdd:COG4372      5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQarseLEQLEEELEE 84

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958794731 1631 NERELEVKAAQLDGLEARMRSV-LQAINLQVQI 1662
Cdd:COG4372     85 LNEQLQAAQAELAQAQEELESLqEEAEELQEEL 117
PRK09039 PRK09039
peptidoglycan -binding protein;
1401-1616 2.58e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1401 SIEMVATRVLDISIPASPEQIQRLASEIAERVRSLA-------DVDTILAHTMGDVRRAEQL---LQ--DAQRARSRAEG 1468
Cdd:PRK09039    35 TVFVVAQFFLSREISGKDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQalLAELAGAGAAA 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1469 ERQKAETVQA-ALEEAQRAQGAAQgairgavVDTKNteQTLQQVQERMAGTEQSLNSASERARQLHALLEALklkraGNS 1547
Cdd:PRK09039   115 EGRAGELAQElDSEKQVSARALAQ-------VELLN--QQIAALRRQLAALEAALDASEKRDRESQAKIADL-----GRR 180

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1548 LAASTAEETAGSAQSRArEAEKQLREQVGDQyQTVRALAER---KAEgVLAAQARAE-------QLRDEARGLLQAAQD 1616
Cdd:PRK09039   181 LNVALAQRVQELNRYRS-EFFGRLREILGDR-EGIRIVGDRfvfQSE-VLFPTGSAElnpegqaEIAKLAAALIELAKE 256
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 1322-1410 2.72e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 40.29  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1322 LGRA-RHTQAELQRALVEGGGILSRVSEtRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSqegadpD 1400
Cdd:PRK14473    58 LANAkRDYEAELAKARQEAAKIVAQAQE-RARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIA------D 130

                           90
                   ....*....|
gi 1958794731 1401 SIEMVATRVL 1410
Cdd:PRK14473   131 LVTLTASRVL 140
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1344-1624 3.26e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.48  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1344 SRVSETRRQAEEAQQRAQAALDKANASRGQVEQANQELRELIQNVKDFLSQ-EGADPDSIEMVATRVLDISIPASPEQIQ 1422
Cdd:PRK10246   304 AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEhDRFRQWNNELAGWRAQFSQQTSDREQLR 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1423 RLASEIAERVRSLADV-DTILAHTMGDVRRAEqllqdAQRARSRAegERQKAETVQAALEEAQRAQGAAQGAIRGAVVDT 1501
Cdd:PRK10246   384 QWQQQLTHAEQKLNALpAITLTLTADEVAAAL-----AQHAEQRP--LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQ 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1502 KNTEQTLQQVQERMAGTEQSLNSAS---ERARQLHALLEALKLKRAGNS--LAASTAEETAGSAQSRAREAEKQLREQVg 1576
Cdd:PRK10246   457 TQRNAALNEMRQRYKEKTQQLADVKticEQEARIKDLEAQRAQLQAGQPcpLCGSTSHPAVEAYQALEPGVNQSRLDAL- 535

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958794731 1577 dqYQTVRALAERKAEGVLAAQARAEQLR---DEARGLLQAAQDKLQRLQEL 1624
Cdd:PRK10246   536 --EKEVKKLGEEGAALRGQLDALTKQLQrdeSEAQSLRQEEQALTQQWQAV 584
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 175-207 3.79e-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: 3.79e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958794731  175 VHGACICKHNTRGLNCEQCQDFYQDLPWHPAED 207
Cdd:pfam00053   16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
HrpE_YscL_not TIGR02499
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ...
 1429-1543 3.94e-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: 39.97  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1429 AERVRSLADVDTILAHTmgdVRRAEQLLQDAQRarsraEGERQKAETVQAALEEAQRAQgAAQGAirGAVVDtknTEQTL 1508
Cdd:TIGR02499    6 AEDLAALAQAQAILAAA---RQRAEAILADAEE-----EAEASRQLGYEQGLEQFWQEA-AAQLA--EWQQE---AEQLE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958794731 1509 QQVQERMAG-----TEQSLNSASERARQLHALLEALKLKR 1543
Cdd:TIGR02499   72 ASLEERLAElvlqaLEQILGEYDEPERLVRLLRQLLRAVA 111
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1586-1654 3.96e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 3.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1586 AERKAEgvlAAQARAEQLRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKaaqldgLEARMRSVLQ 1654
Cdd:cd16269    196 KEKEIE---AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK------MEEERENLLK 255
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
 1526-1658 3.97e-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: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1526 SERARQLHALLEALKLKRA------GNSLAASTAEETAGSAQsrAREAEKQLReqvgdqyQTVRALAERKAEGVLAAQAR 1599
Cdd:pfam05130    8 EEELELLEELLELLEEEQEalkagdIEALEELTEEKQELLQK--LAQLEKERR-------ELLAELGLSPEEATLSELLA 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794731 1600 AEQLRDEARGLLQAAQDKLQRLQELEgtyEENeRELevkaaqldgLEARMRSVLQAINL 1658
Cdd:pfam05130   79 KEEEDPELRELWQELLELLERLKELN---ELN-GEL---------IEQSLEFNNRSLNI 124
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 1419-1540 4.44e-03

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


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 38.72  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1419 EQIQRL---ASEIAERVRSLADVDTilahtmgDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQgaaqgaiR 1495
Cdd:pfam18595    9 EELAELerkARELQAKIDALQVVEK-------DLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEIEL-------R 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958794731 1496 GAVVDTKNTEQTLQQVQERMAGTEQslnSASERARQLHALLEALK 1540
Cdd:pfam18595   75 ELERREERLQRQLENAQEKLERLRE---QAEEKREAAQARLEELR 116
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1330-1482 4.91e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.60  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1330 AELQRALVEG-GGILSRVSETRRQAEEAQQ---RAQAALDKANASRGQVEQANQELRELIQNVkDFlsqegaDPDSIEMV 1405
Cdd:COG0497    229 QEALEALSGGeGGALDLLGQALRALERLAEydpSLAELAERLESALIELEEAASELRRYLDSL-EF------DPERLEEV 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1406 ATRVLDISIPA-----SPEQIQRLASEIAERVRSLADVDTILAHTMGDVRRAEQLLQDAQRARSRAegeRQKA-----ET 1475
Cdd:COG0497    302 EERLALLRRLArkygvTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA---RKKAakkleKA 378


                   ....*..
gi 1958794731 1476 VQAALEE 1482
Cdd:COG0497    379 VTAELAD 385
FUSC pfam04632
Fusaric acid resistance protein family; This family includes a conserved region found in two ...
 1397-1640 5.46e-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: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1397 ADPDSIEMVA-TRVLDISI-------------PASPEQiqRLASEIAERVRSLAdvdtilahtmgdvRRAEQLLQDAQRA 1462
Cdd:pfam04632  118 ADPEAIFDIAvARVSEISLgilcaalvsalvfPRSVGP--ALRARLRARLRDAL-------------RLAAAALAGAPGA 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1463 RSRAEGERQKAETVqAALEeAQRAQGAAQGA-IRGAVvdtknteQTLQQVQERMAgteqslnSASERARQLHALLEALkl 1541
Cdd:pfam04632  183 EAFEAARLRLAADI-LALE-ALRSHAAFESPrGRARA-------RALRRLLARML-------ALLPRLRSLARLLARL-- 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1542 kragnslAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERkaegVLAAQARAEQLRDEARGLLQAAQDKLQRL 1621
Cdd:pfam04632  245 -------RTEGAGTVPELAALLDELAAWEAALAAEALQAALAALRAR----LRALRPALPLDFDTAAELLARLADLLAEL 313

                          250
                   ....*....|....*....
gi 1958794731 1622 QELEGTYEENERELEVKAA 1640
Cdd:pfam04632  314 AEALASCRALRHPIAQGAR 332
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
 774-853 5.71e-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: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731  774 CERCIAGFHGDPRLPYGgqCRPC-PCPEGPGSQRHFATSCHRDgysqqIVCHCRAGYT-------GLRCEACAPGHFGDP 845
Cdd:cd13406     36 CSPCEPGFYNEAVNYEP--CKPCtQCNQRSGSEEKQKCTKTSD-----TVCRCRPGTQpldsykpGVDCVPCPPGHFSRG 108


                   ....*...
gi 1958794731  846 SkpGGRCQ 853
Cdd:cd13406    109 D--NQACK 114
COG3899 COG3899
Predicted ATPase [General function prediction only];
1443-1650 5.74e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 41.38  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1443 AHTMGDVRRAEQLLQDAQRARSRAEGERQKAETVQAALEEAQRAQGAAQGAIRGAVVDTKNTEQTLQQVQERMAGTEQSL 1522
Cdd:COG3899    755 LYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALF 834

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1523 NSASERARQLHaLLEALKLKRAGNSLAASTAEETAGSAQSRAREAEKQLREQVGDQYQTVRALAERKAEGVLAAQARAEQ 1602
Cdd:COG3899    835 NLGFILHWLGP-LREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAAL 913

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958794731 1603 LRDEARGLLQAAQDKLQRLQELEGTYEENERELEVKAAQLDGLEARMR 1650
Cdd:COG3899    914 AAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
DUF1631 pfam07793
Protein of unknown function (DUF1631); The members of this family are sequences derived from a ...
 1342-1533 6.21e-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: 41.15  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1342 ILSRVSETRRQAEEAQQRAQAAL---DKANASRGQVEqanQELRELIQN------VKDFLSQ------------EGAD-P 1399
Cdd:pfam07793  459 FEEFLERERRRAELAEQRTVDAAegrERLELARQQAA---DELEQRLAGrplpevVREFLRQawsdvlaltylrHGEDsE 535

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1400 DSIEMVAT------RVLDISIPASPEQIQRLASEIAERVRS-LADVdtilAHTMGDVRRAEQLLQDAQRARSRAEGERQK 1472
Cdd:pfam07793  536 EWQEALATaddlvwSVSPKPTAEERARLLALLPELLKRLRQgLASI----GYDPDESEAFFKELEALHAAAFRAKAAALA 611

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794731 1473 AETVQAALEEAQRAQGAaqgairgAVVDTKNTEQTLQQVQERMAGTEQSLNSAS-ERARQLH 1533
Cdd:pfam07793  612 AALKAAAAKPAPAAAPA-------SPVEAEEEEALLGADAPPLAVVASPEDDAYlAQARALP 666
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1560-1640 6.70e-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: 6.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794731 1560 AQSRAREAEKQLREqvgdqYQTVRALAERKAEGVLA-AQARAEQLRDEARgllQAAQDKLQRLQELegtyEENERELEVK 1638
Cdd:COG0711     43 AERAKEEAEAALAE-----YEEKLAEARAEAAEIIAeARKEAEAIAEEAK---AEAEAEAERIIAQ----AEAEIEQERA 110


                   ..
gi 1958794731 1639 AA 1640
Cdd:COG0711    111 KA 112
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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