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Conserved domains on  [gi|113865981|ref|NP_032510|]
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laminin subunit beta-3 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Laminin_N super family cl02806
Laminin N-terminal (Domain VI);
20-248 7.35e-70

Laminin N-terminal (Domain VI);


The actual alignment was detected with superfamily member smart00136:

Pssm-ID: 470680  Cd Length: 238  Bit Score: 233.79  E-value: 7.35e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981     20 ACSRGACYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981     96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136   77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136  156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234

                    ....
gi 113865981    245 RLQG 248
Cdd:smart00136  235 AVGG 238
cc_LAMB_C super family cl40438
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1098-1168 1.14e-23

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.


The actual alignment was detected with superfamily member cd22303:

Pssm-ID: 424069 [Multi-domain]  Cd Length: 71  Bit Score: 95.59  E-value: 1.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113865981 1098 GNRILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303     1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
376-425 1.24e-13

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.22  E-value: 1.24e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 113865981   376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGC 425
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
530-579 5.80e-12

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: 61.60  E-value: 5.80e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 113865981  530 ACDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
830-1161 4.79e-10

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 4.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVStsrlLMEEDVQRTRLLIQQVRGFLTDPDtDAATIQQVS 909
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS----ALRKDLARLEAEVEQLEERIAQLS-KELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   910 EAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDI----ARARRLQAEAEQARSRAHAVEGQVDDvvgnlrq 985
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLERRIAA------- 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   986 gtvalqeaqdtmqgTGRSLRLIQERVGEVQQVLVPAErlvkgmkEQMSGFWARMKELRRQ---AQEEQAQAMQARQLAEG 1062
Cdd:TIGR02168  836 --------------TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESEleaLLNERASLEEALALLRS 894
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  1063 ASQQAM----NAQEGFKRLKQKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgetmemmdkmkdmesELLRGSQAIML 1138
Cdd:TIGR02168  895 ELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ---------------ERLSEEYSLTL 953
                          330       340       350
                   ....*....|....*....|....*....|....
gi 113865981  1139 ---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168  954 eeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
428-475 1.08e-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: 1.08e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 113865981   428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053    1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
478-531 4.25e-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: 53.13  E-value: 4.25e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 113865981   478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGCRAC 531
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
249-301 1.45e-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: 51.97  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 113865981  249 SCFCHGHADRcapnpggSTTAVQVNNVCVCQHNTAGPNCDRCAPFYNNRPWRP 301
Cdd:cd00055     1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
313-367 1.99e-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: 42.73  E-value: 1.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981   313 CDCNGH---SETCHFdpavfaasqgtNGGVCDnCRDHTEGKNCERCQLHYFRNRRPSA 367
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
20-248 7.35e-70

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: 233.79  E-value: 7.35e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981     20 ACSRGACYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981     96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136   77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136  156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234

                    ....
gi 113865981    245 RLQG 248
Cdd:smart00136  235 AVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
26-248 1.16e-56

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 195.88  E-value: 1.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    26 CYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ-YGQWQMKCCKCDSRLPrnYNSHRVENVASSSG--PMRWWQSQNDVS 102
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILsGLEGGKKCFICDSRDP--HNSHPPSNLTDSNNgtNETWWQSETGVI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   103 P---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNW-QDVRCrplSQ 178
Cdd:pfam00055   77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVIC---TS 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981   179 RPNG--HLTGGKVQLNLMDLASAIP-ASQSKKIQELGDITNLRVNFTKLA-PVPQRGSYP---PSAYFAVSQLRLQG 248
Cdd:pfam00055  154 EYSDisPLTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtLGDELLDDPsvlRKYYYAISDISVGG 230
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
1098-1168 1.14e-23

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: 95.59  E-value: 1.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113865981 1098 GNRILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303     1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
376-425 1.24e-13

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.22  E-value: 1.24e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 113865981   376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGC 425
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
530-579 5.80e-12

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: 61.60  E-value: 5.80e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 113865981  530 ACDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
531-568 8.43e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 8.43e-12
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 113865981    531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
531-568 1.71e-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: 1.71e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 113865981   531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
375-426 3.61e-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: 59.29  E-value: 3.61e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 113865981  375 PCECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGLTfANPKGCH 426
Cdd:cd00055     1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
376-425 9.06e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.09  E-value: 9.06e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 113865981    376 CECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGltfANPKGC 425
Cdd:smart00180    1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
830-1161 4.79e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 4.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVStsrlLMEEDVQRTRLLIQQVRGFLTDPDtDAATIQQVS 909
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS----ALRKDLARLEAEVEQLEERIAQLS-KELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   910 EAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDI----ARARRLQAEAEQARSRAHAVEGQVDDvvgnlrq 985
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLERRIAA------- 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   986 gtvalqeaqdtmqgTGRSLRLIQERVGEVQQVLVPAErlvkgmkEQMSGFWARMKELRRQ---AQEEQAQAMQARQLAEG 1062
Cdd:TIGR02168  836 --------------TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESEleaLLNERASLEEALALLRS 894
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  1063 ASQQAM----NAQEGFKRLKQKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgetmemmdkmkdmesELLRGSQAIML 1138
Cdd:TIGR02168  895 ELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ---------------ERLSEEYSLTL 953
                          330       340       350
                   ....*....|....*....|....*....|....
gi 113865981  1139 ---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168  954 eeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
428-475 1.08e-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: 1.08e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 113865981   428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053    1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
427-476 1.10e-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: 55.05  E-value: 1.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 113865981  427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055     1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
834-1088 2.70e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  834 QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLlmeeDVQRTRLLIQQVRgfltdpdtdaATIQQVSEAVL 913
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQ----------AEEYELLAELA 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  914 ALwlptdSATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEA 993
Cdd:COG1196   299 RL-----EQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  994 QDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG 1073
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                         250
                  ....*....|....*
gi 113865981 1074 FKRLKQKYTELKDRL 1088
Cdd:COG1196   451 EAELEEEEEALLELL 465
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
478-531 4.25e-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: 53.13  E-value: 4.25e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 113865981   478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGCRAC 531
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-528 4.32e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 4.32e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 113865981    478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGC 528
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
428-475 4.95e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 4.95e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 113865981    428 CDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKlASGLGC 475
Cdd:smart00180    1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
249-301 1.45e-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: 51.97  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 113865981  249 SCFCHGHADRcapnpggSTTAVQVNNVCVCQHNTAGPNCDRCAPFYNNRPWRP 301
Cdd:cd00055     1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
477-529 4.14e-08

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 50.43  E-value: 4.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 113865981  477 PCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGH--VATGCR 529
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
250-304 2.17e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.81  E-value: 2.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981   250 CFCHGHA---DRCAPNPGgsttavqvnnVCVCQHNTAGPNCDRCAPFYNNRPWRPAEG 304
Cdd:pfam00053    1 CDCNPHGslsDTCDPETG----------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
842-1111 1.16e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSR---LLMEEDVQRTRLLIQQVRGFLTDPDTDaatIQQVSEAVLALWLP 918
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVD 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  919 TDSATVLRKM--KEIQAIAARLPNVDSVLSQTKQDIARARRLQA-----EAEQARSRAHAVEGQVDD--VVGNLRQGTVA 989
Cdd:PRK02224  407 LGNAEDFLEElrEERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEEDreRVEELEAELED 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  990 LQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWA---RMKELRRQAQEEQAQAMQARQLAEGASQQ 1066
Cdd:PRK02224  487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEE 566
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 113865981 1067 AMNAQEGFKRLKQKYTELKDRLgqspvlgEQGNRILSIKMEAEEL 1111
Cdd:PRK02224  567 AEEAREEVAELNSKLAELKERI-------ESLERIRTLLAAIADA 604
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
313-367 1.99e-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: 42.73  E-value: 1.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981   313 CDCNGH---SETCHFdpavfaasqgtNGGVCDnCRDHTEGKNCERCQLHYFRNRRPSA 367
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
829-1088 2.13e-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: 48.35  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTD----------- 897
Cdd:pfam07888   34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----LESRVAELKEELRQSREKHEEleekykelsas 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   898 -----PDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARRLQAEAEQARSRAHA 971
Cdd:pfam07888  110 seelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   972 VEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGE----------VQQVLVPAERLVKGMKEQMSGfwarMKE 1041
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSS----MAA 265
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 113865981  1042 LRRQAQEEQAQA-MQARQLAEGASQQAMNAQEGFKRLKQKYTEL-------KDRL 1088
Cdd:pfam07888  266 QRDRTQAELHQArLQAAQLTLQLADASLALREGRARWAQERETLqqsaeadKDRI 320
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
259-299 3.37e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 42.30  E-value: 3.37e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 113865981    259 CAPNPGGSTTAV--QVNNVCVCQHNTAGPNCDRCAPFYNNRPW 299
Cdd:smart00180    1 CDCDPGGSASGTcdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
312-362 5.96e-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: 41.57  E-value: 5.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 113865981  312 RCDCNGH---SETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRN 362
Cdd:cd00055     1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
growth_prot_Scy NF041483
polarized growth protein Scy;
844-1114 1.10e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 46.74  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  844 QTRQMIRAAEEAASRVQADAQR--LETQVSTSRLLME--------------EDVQRTRLLIQQVrgfltdpDTDAATIQ- 906
Cdd:NF041483   73 QAEQLLRNAQIQADQLRADAERelRDARAQTQRILQEhaehqarlqaelhtEAVQRRQQLDQEL-------AERRQTVEs 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  907 QVSEAVLalWlptdsATVLRKMKEIQAiaARLpnVDSVLSQTKQDIARAR------------RLQAEAEQARSRAHAVEG 974
Cdd:NF041483  146 HVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEAEAILR 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  975 QV-DDVVGNLRQGTVALQEAqdtmqgTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE--EQA 1051
Cdd:NF041483  215 RArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEA 288
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981 1052 QAMQARQL--AEGASQQAM-NAQEGFKRLKQKYTElkdrlgQSPVLGEQGNRILS-IKMEAEELFGE 1114
Cdd:NF041483  289 KEAAAKQLasAESANEQRTrTAKEEIARLVGEATK------EAEALKAEAEQALAdARAEAEKLVAE 349
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
828-1078 2.33e-04

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: 44.20  E-value: 2.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRtrllIQQVRGfltdpdtdaaTIQQ 907
Cdd:smart00283   13 AEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITA----MDQIRE----------VVEE 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    908 VSEAVLALwlptdsatvLRKMKEIQAIAArlpNVDSVLSQTkqDI---------ARA--------------RRL----QA 960
Cdd:smart00283   79 AVSAVEEL---------EESSDEIGEIVS---VIDDIADQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAE 144
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    961 EAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaERLVKGMKEQMSG---FWA 1037
Cdd:smart00283  145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQAAGseeVNA 221
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 113865981   1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:smart00283  222 AIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
313-366 8.92e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 8.92e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981    313 CDCNG---HSETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRNRRPS 366
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
growth_prot_Scy NF041483
polarized growth protein Scy;
832-1065 1.44e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  832 AEQLRNFNT-QLQQTR-----------QMIRAAEEAASRVQADAQRLETQVSTS---RLLMEEDV--QRTRLLIQQVRGF 894
Cdd:NF041483  238 AEQLRSSTAaESDQARrqaaelsraaeQRMQEAEEALREARAEAEKVVAEAKEAaakQLASAESAneQRTRTAKEEIARL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  895 LTDPDTDAATIQQVSEAVLA------------------LWLPTDSATVLRKmkeiqaiAARlpNVDSVLSQTKQDiARAR 956
Cdd:NF041483  318 VGEATKEAEALKAEAEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKAT 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  957 -----------RLQAEAEQARSRAHAVE------GQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliQERVGE------ 1013
Cdd:NF041483  388 traaaeeaeriRREAEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirg 465
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981 1014 ------VQQV---LVPAERLVKGMK----EQMSGFWA-----------RMKELRRQAQE--EQAQAMQARQLAEGASQ 1065
Cdd:NF041483  466 earreaVQQIeeaARTAEELLTKAKadadELRSTATAeservrteaieRATTLRRQAEEtlERTRAEAERLRAEAEEQ 543
growth_prot_Scy NF041483
polarized growth protein Scy;
828-1088 4.48e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  828 AGRVAEQLRNFNTQLQ-QTRQMI----RAAEEAASRVQADAQ----RLETQVSTSRLLMEEDVQRTRLLIQQvrgfltdp 898
Cdd:NF041483  773 AEQTAQQVRDSVAGLQeQAEEEIaglrSAAEHAAERTRTEAQeeadRVRSDAYAERERASEDANRLRREAQE-------- 844
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  899 DTDAATI---QQVSEAVlalwlptDSATVLRKMKEIQAIAARLPNVDSvLSQTKQDIARARrlqAEA-EQARSRAHAVEG 974
Cdd:NF041483  845 ETEAAKAlaeRTVSEAI-------AEAERLRSDASEYAQRVRTEASDT-LASAEQDAARTR---ADArEDANRIRSDAAA 913
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  975 QVDDVVGNLRQGTVALQEAqdtmqGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARmkeLRRQAQEEQAQAM 1054
Cdd:NF041483  914 QADRLIGEATSEAERLTAE-----ARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER---LRAEAAETVGSAQ 985
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 113865981 1055 QA--RQLAEGASQQAMNAQEGfKRLKQKYTELKDRL 1088
Cdd:NF041483  986 QHaeRIRTEAERVKAEAAAEA-ERLRTEAREEADRT 1020
growth_prot_Scy NF041483
polarized growth protein Scy;
827-1110 6.07e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRL--ETQVSTSRLLMEEdVQRTRLLIQQVRG----FLTDPDT 900
Cdd:NF041483  566 IAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIrrEAAEETERLRTEA-AERIRTLQAQAEQeaerLRTEAAA 644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  901 DAATIQQVSEAVlALWLPTDSATVLRKMK------------EIQAIAARLPN-VDSVLSQTKQDIARARR--------LQ 959
Cdd:NF041483  645 DASAARAEGENV-AVRLRSEAAAEAERLKseaqesadrvraEAAAAAERVGTeAAEALAAAQEEAARRRReaeetlgsAR 723
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  960 AEAEQARSRAHAvegQVDDVVGNLRQgtvALQEAQDTMQgtgrslRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwarm 1039
Cdd:NF041483  724 AEADQERERARE---QSEELLASARK---RVEEAQAEAQ------RLVEEADRRATELVSAAEQTAQQVRDSVAG----- 786
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113865981 1040 keLRRQAQEEQAqamQARQLAEGASQQA-MNAQEGFKRLKQKYTELKDRlgqspvLGEQGNRILSIKMEAEE 1110
Cdd:NF041483  787 --LQEQAEEEIA---GLRSAAEHAAERTrTEAQEEADRVRSDAYAERER------ASEDANRLRREAQEETE 847
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
20-248 7.35e-70

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: 233.79  E-value: 7.35e-70
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981     20 ACSRGACYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ--YGQWQMKCCKCDSRLPrnYNSHRVENVASSSGP--MRWW 95
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDARNP--RRSHPAENLTDGNNPnnPTWW 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981     96 QSQNDVSP---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSsDFGKTWRVYQYLATDCASTFPQVHQG--QPKNWQD 170
Cdd:smart00136   77 QSEPLSNGpqnVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpiTKGNEDE 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    171 VRCRPLSQRPNGhLTGGKVQLNLMDL-ASAIPASQSKKIQELGDITNLRVNFTKLAPVPQRG-----SYPPSAYFAVSQL 244
Cdd:smart00136  156 VICTSEYSDIVP-LEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELmddrpEVTRRYYYAISDI 234

                    ....
gi 113865981    245 RLQG 248
Cdd:smart00136  235 AVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
26-248 1.16e-56

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 195.88  E-value: 1.16e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    26 CYPPVGDLLIGRTqlLRASSTCGLTKPETYCTQ-YGQWQMKCCKCDSRLPrnYNSHRVENVASSSG--PMRWWQSQNDVS 102
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILsGLEGGKKCFICDSRDP--HNSHPPSNLTDSNNgtNETWWQSETGVI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   103 P---VSLQLDLDKRMQLQDIMMDFKGLTPAGMLIERSSDFGKTWRVYQYLATDCASTFPQVHQGQPKNW-QDVRCrplSQ 178
Cdd:pfam00055   77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKdDEVIC---TS 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981   179 RPNG--HLTGGKVQLNLMDLASAIP-ASQSKKIQELGDITNLRVNFTKLA-PVPQRGSYP---PSAYFAVSQLRLQG 248
Cdd:pfam00055  154 EYSDisPLTGGEVIFSTLEGRPSANiFDYSPELQDWLTATNIRIRLLRLHtLGDELLDDPsvlRKYYYAISDISVGG 230
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
1098-1168 1.14e-23

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: 95.59  E-value: 1.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 113865981 1098 GNRILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATCK 1168
Cdd:cd22303     1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
376-425 1.24e-13

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 66.22  E-value: 1.24e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 113865981   376 CECDPDGAVqGAPCDRLTGQCVCKEYVQGERCDLCKPGFTGLTFANPKGC 425
Cdd:pfam00053    1 CDCNPHGSL-SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1100-1167 2.59e-12

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: 63.07  E-value: 2.59e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981 1100 RILSIKMEAEELFGETMEMMDKMKDMESELLRGSQAIMLRSADLSGLEKRVEQIRSYINGRVLYYATC 1167
Cdd:cd22295     3 RAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
530-579 5.80e-12

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: 61.60  E-value: 5.80e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 113865981  530 ACDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGHCDRYPVCVACH 579
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
531-568 8.43e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 8.43e-12
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 113865981    531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
531-568 1.71e-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: 1.71e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 113865981   531 CDCDFRGTEGPGCDKASGRCLCRPGFTGPRCDQCQRGH 568
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
375-426 3.61e-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: 59.29  E-value: 3.61e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 113865981  375 PCECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGLTfANPKGCH 426
Cdd:cd00055     1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
376-425 9.06e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.09  E-value: 9.06e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 113865981    376 CECDPDGAVQGApCDRLTGQCVCKEYVQGERCDLCKPGFTGltfANPKGC 425
Cdd:smart00180    1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
830-1161 4.79e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 4.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVStsrlLMEEDVQRTRLLIQQVRGFLTDPDtDAATIQQVS 909
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS----ALRKDLARLEAEVEQLEERIAQLS-KELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   910 EAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDI----ARARRLQAEAEQARSRAHAVEGQVDDvvgnlrq 985
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLERRIAA------- 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   986 gtvalqeaqdtmqgTGRSLRLIQERVGEVQQVLVPAErlvkgmkEQMSGFWARMKELRRQ---AQEEQAQAMQARQLAEG 1062
Cdd:TIGR02168  836 --------------TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESEleaLLNERASLEEALALLRS 894
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  1063 ASQQAM----NAQEGFKRLKQKYTELKDRLGQSpvlgeqGNRILSIKMEAEELFgetmemmdkmkdmesELLRGSQAIML 1138
Cdd:TIGR02168  895 ELEELSeelrELESKRSELRRELEELREKLAQL------ELRLEGLEVRIDNLQ---------------ERLSEEYSLTL 953
                          330       340       350
                   ....*....|....*....|....*....|....
gi 113865981  1139 ---------RSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:TIGR02168  954 eeaealenkIEDDEEEARRRLKRLENKIKelGPV 987
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
428-475 1.08e-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: 1.08e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 113865981   428 CDCSILGARKDmPCEEETGRCLCLPNVVGPKCDQCAPSHWKLASGLGC 475
Cdd:pfam00053    1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
427-476 1.10e-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: 55.05  E-value: 1.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 113865981  427 ACDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKLAS-GLGCE 476
Cdd:cd00055     1 PCDCNGHGSL-SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
834-1088 2.70e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  834 QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLlmeeDVQRTRLLIQQVRgfltdpdtdaATIQQVSEAVL 913
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQ----------AEEYELLAELA 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  914 ALwlptdSATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEA 993
Cdd:COG1196   299 RL-----EQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  994 QDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEG 1073
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                         250
                  ....*....|....*
gi 113865981 1074 FKRLKQKYTELKDRL 1088
Cdd:COG1196   451 EAELEEEEEALLELL 465
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
478-531 4.25e-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: 53.13  E-value: 4.25e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 113865981   478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGCRAC 531
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-528 4.32e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 4.32e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 113865981    478 CACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGHVATGC 528
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCD-----RCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
428-475 4.95e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.08  E-value: 4.95e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 113865981    428 CDCSILGARkDMPCEEETGRCLCLPNVVGPKCDQCAPSHWKlASGLGC 475
Cdd:smart00180    1 CDCDPGGSA-SGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
249-301 1.45e-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: 51.97  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 113865981  249 SCFCHGHADRcapnpggSTTAVQVNNVCVCQHNTAGPNCDRCAPFYNNRPWRP 301
Cdd:cd00055     1 PCDCNGHGSL-------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
477-529 4.14e-08

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 50.43  E-value: 4.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 113865981  477 PCACDPRNSLSSQCNQFTGQCPCREGFGGLTCSsaairQCPDQTYGH--VATGCR 529
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCD-----RCAPGYYGLpsQGGGCQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
830-1090 4.15e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVS 909
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----LEQDIARLEERRRELEERLEELEEELAELEEEL 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  910 EAvlalwlptDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVA 989
Cdd:COG1196   333 EE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  990 LQEAQDTMQgtGRSLRLIQERvGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMN 1069
Cdd:COG1196   405 LEEAEEALL--ERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                         250       260
                  ....*....|....*....|.
gi 113865981 1070 AQEGFKRLKQKYTELKDRLGQ 1090
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEAD 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
828-1081 3.45e-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: 54.00  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrlLMEEDVQRTRLLIQQVRgfltdpdtdAATIQQ 907
Cdd:COG4942    50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELAELLR---------ALYRLG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  908 VSEAVLALWLPTDSATVLRKMKEIQAIAarlPNVDSVLSQTKQDIARARRLQAEAEQARSRahavegqvddvvgnLRQGT 987
Cdd:COG4942   118 RQPPLALLLSPEDFLDAVRRLQYLKYLA---PARREQAEELRADLAELAALRAELEAERAE--------------LEALL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  988 VALQEAQDTMQgtgrslRLIQERvgevqqvlvpaERLVKGMKEQMSGFWARMKELRRQAQEEQAQAmqARQLAEGASQQA 1067
Cdd:COG4942   181 AELEEERAALE------ALKAER-----------QKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAE 241
                         250
                  ....*....|....
gi 113865981 1068 MNAQEGFKRLKQKY 1081
Cdd:COG4942   242 RTPAAGFAALKGKL 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
846-1087 9.66e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 9.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  846 RQMI---RAAEEAASRVQADAQRLETqvstsrllMEEDVQRTRlliQQVRgFLTDpdtdaatIQQVSEAVLALWlptDSA 922
Cdd:COG4913   214 REYMleePDTFEAADALVEHFDDLER--------AHEALEDAR---EQIE-LLEP-------IRELAERYAAAR---ERL 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  923 TVLRKMKE---IQAIAARLPNVDSVLSQTKQDIARarrLQAEAEQARSRAHAVEGQVDDVVGNLRQ-GTVALQEAQDTMQ 998
Cdd:COG4913   272 AELEYLRAalrLWFAQRRLELLEAELEELRAELAR---LEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  999 GTGRSLRLIQERVGEVQQVL------VPAERlvkgmkeqmSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQE 1072
Cdd:COG4913   349 RLERELEERERRRARLEALLaalglpLPASA---------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
                         250
                  ....*....|....*
gi 113865981 1073 GFKRLKQKYTELKDR 1087
Cdd:COG4913   420 ELRELEAEIASLERR 434
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
831-1071 9.67e-07

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: 9.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  831 VAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRllmEEDVQRTRLLIQQVRGfltdpdtdaatiQQVSE 910
Cdd:COG3883    35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERARA------------LYRSG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  911 AVLALWlptdsaTVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSrahavegQVDDVVGNLRQGTVAL 990
Cdd:COG3883   100 GSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  991 QEAQDTMQgtgrslRLIQErvgevqqvlvpAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNA 1070
Cdd:COG3883   167 EAAKAELE------AQQAE-----------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229

                  .
gi 113865981 1071 Q 1071
Cdd:COG3883   230 A 230
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
250-304 2.17e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.81  E-value: 2.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981   250 CFCHGHA---DRCAPNPGgsttavqvnnVCVCQHNTAGPNCDRCAPFYNNRPWRPAEG 304
Cdd:pfam00053    1 CDCNPHGslsDTCDPETG----------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
827-1104 3.69e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 51.17  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATIQ 906
Cdd:COG0840    80 VLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAA 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  907 QVSEAVLALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQ--TKQDIARARRLQAEAEQARSR--AHAVEGQVDDVVGN 982
Cdd:COG0840   160 AAALAALLEAAALALAAAALALALLAAALLALVALAIILALllSRSITRPLRELLEVLERIAEGdlTVRIDVDSKDEIGQ 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  983 LRQgtvALQEAQDTMQGTGRSLRLIQERVGE-VQQVLVPAERLVKGMKEQMSGF---WARMKELRRQAQEEQAQAMQARQ 1058
Cdd:COG0840   240 LAD---AFNRMIENLRELVGQVRESAEQVASaSEELAASAEELAAGAEEQAASLeetAAAMEELSATVQEVAENAQQAAE 316
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 113865981 1059 LAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPV----LGEQGNRILSI 1104
Cdd:COG0840   317 LAEEASELAEEGGEVVEEAVEGIEEIRESVEETAEtieeLGESSQEIGEI 366
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
829-1078 3.76e-06

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


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 51.17  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  829 GRVAEQLRNFNTQLQQTRQMIR---------------AAEEAASRVQADAQRLEtQVSTSrllMEE---DVQRTRLLIQQ 890
Cdd:COG0840   238 GQLADAFNRMIENLRELVGQVResaeqvasaseelaaSAEELAAGAEEQAASLE-ETAAA---MEElsaTVQEVAENAQQ 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  891 VRGFLTDPDTDAATIQQVSEAVLALW--LPTDSATVLRKMKEIQAIAArlpNVDSVLSqTKQDI---------------A 953
Cdd:COG0840   314 AAELAEEASELAEEGGEVVEEAVEGIeeIRESVEETAETIEELGESSQ---EIGEIVD-VIDDIaeqtnllalnaaieaA 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  954 RA--------------RRLqAE-----AEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEV 1014
Cdd:COG0840   390 RAgeagrgfavvadevRKL-AErsaeaTKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEV 468
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981 1015 ----QQVLVPAERLVKGMkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:COG0840   469 sdliQEIAAASEEQSAGT-EEVN---QAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFK 532
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
929-1111 4.79e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  929 KEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQ 1008
Cdd:COG4372    21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1009 ERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE-EQAQAMQARQLAEgASQQAMNAQEGFKRLKQKYTELKDR 1087
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAElQSEIAEREEELKE-LEEQLESLQEELAALEQELQALSEA 179
                         170       180
                  ....*....|....*....|....*.
gi 113865981 1088 LGQSPV--LGEQGNRILSIKMEAEEL 1111
Cdd:COG4372   180 EAEQALdeLLKEANRNAEKEEELAEA 205
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
834-1066 7.37e-06

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


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 49.65  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  834 QLRNFNTQLQQTRQMIRAAEEAASRVQadaQRLETQVSTsrllmEEDVQRTRLLIQQVRGFLTDpdtdAATIQQVSEAVL 913
Cdd:COG1538    84 DLLAAQEQLALAEENLALAEELLELAR---ARYEAGLAS-----RLDVLQAEAQLAQARAQLAQ----AEAQLAQARNAL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  914 ALWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQ---DIARARrlqAEAEQARSRAHAVEGQ----VDDVVGNLRQG 986
Cdd:COG1538   152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALErrpDLRAAE---AQLEAAEAEIGVARAAflpsLSLSASYGYSS 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  987 TVALQEAQDTMQGTGRSLRL-----------IQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQ 1055
Cdd:COG1538   229 SDDLFSGGSDTWSVGLSLSLplfdggrnrarVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEA 308
                         250
                  ....*....|.
gi 113865981 1056 ARQLAEGASQQ 1066
Cdd:COG1538   309 AEEALELARAR 319
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
936-1104 9.90e-06

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 48.89  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  936 ARLpnvDSVLSQTKQDIARARRLQAEAEQARSRA-HAVEGQVDDVVGNLRQGTVALQEAQDTMQgtgRSLRLIQERVgev 1014
Cdd:COG1566    74 ARL---DPTDLQAALAQAEAQLAAAEAQLARLEAeLGAEAEIAAAEAQLAAAQAQLDLAQRELE---RYQALYKKGA--- 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1015 qqvlVPAERLvkgmkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAmNAQEGFKRLKQKYTELKDRLGQ---- 1090
Cdd:COG1566   145 ----VSQQEL-----DEAR---AALDAAQAQLEAAQAQLAQAQAGLREEEELA-AAQAQVAQAEAALAQAELNLARttir 211
                         170
                  ....*....|....
gi 113865981 1091 SPVLGEQGNRILSI 1104
Cdd:COG1566   212 APVDGVVTNLNVEP 225
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
842-1111 1.16e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSR---LLMEEDVQRTRLLIQQVRGFLTDPDTDaatIQQVSEAVLALWLP 918
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVD 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  919 TDSATVLRKM--KEIQAIAARLPNVDSVLSQTKQDIARARRLQA-----EAEQARSRAHAVEGQVDD--VVGNLRQGTVA 989
Cdd:PRK02224  407 LGNAEDFLEElrEERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEEDreRVEELEAELED 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  990 LQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWA---RMKELRRQAQEEQAQAMQARQLAEGASQQ 1066
Cdd:PRK02224  487 LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEkreRAEELRERAAELEAEAEEKREAAAEAEEE 566
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 113865981 1067 AMNAQEGFKRLKQKYTELKDRLgqspvlgEQGNRILSIKMEAEEL 1111
Cdd:PRK02224  567 AEEAREEVAELNSKLAELKERI-------ESLERIRTLLAAIADA 604
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
830-1161 1.23e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLEtqvstSRLLMEEDVQRTRLLIQQ--VRGFLTDPDTDAATIQQ 907
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA-----DYEGFLEGVKAALLLAGLrgLAGAVAVLIGVEAAYEA 538
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  908 VSEAVLALWLPTDSATVLRKMKE-IQAIAARLPNVDSVLSQTKqdiARARRLQAEAEQARSRAHAVEGQVDD-------- 978
Cdd:COG1196   539 ALEAALAAALQNIVVEDDEVAAAaIEYLKAAKAGRATFLPLDK---IRARAALAAALARGAIGAAVDLVASDlreadary 615
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  979 -VVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQmsgfwARMKELRRQAQEEQAQAMQAR 1057
Cdd:COG1196   616 yVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE-----LLAALLEAEAELEELAERLAE 690
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1058 QLAEGASQQAMNAQEGfKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAEELFGEtmemmdkmkdmesELLRGSQAIM 1137
Cdd:COG1196   691 EELELEEALLAEEEEE-RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE-------------LLEEEALEEL 756
                         330       340
                  ....*....|....*....|....*.
gi 113865981 1138 LRSADLSGLEKRVEQIRSYIN--GRV 1161
Cdd:COG1196   757 PEPPDLEELERELERLEREIEalGPV 782
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
827-1097 1.28e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQAdaqrletqvstsrllmeEDVQRTRLLIQQVRGflTDPDTDAATIQ 906
Cdd:COG3206    95 VLERVVDKLNLDEDPLGEEASREAAIERLRKNLTV-----------------EPVKGSNVIEISYTS--PDPELAAAVAN 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  907 QVSEAVLAlwlptdsATVLRKMKEIQAIAARLpnvDSVLSQTKQDIARARRlQAEAEQARSRAHAVEGQVDDVVGNLRQG 986
Cdd:COG3206   156 ALAEAYLE-------QNLELRREEARKALEFL---EEQLPELRKELEEAEA-ALEEFRQKNGLVDLSEEAKLLLQQLSEL 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  987 TVALQEAQDTMQGTGRSLRLIQERVGEVQQVL--VPAERLVKGMKEQMSGFWARMKELR----------RQAQEEQAQAM 1054
Cdd:COG3206   225 ESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALR 304
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 113865981 1055 Q-----ARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQ 1097
Cdd:COG3206   305 AqlqqeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
313-367 1.99e-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: 42.73  E-value: 1.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981   313 CDCNGH---SETCHFdpavfaasqgtNGGVCDnCRDHTEGKNCERCQLHYFRNRRPSA 367
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPP 46
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
929-1091 2.06e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  929 KEIQAIAARLpnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDdvvgNLRQgtvALQEAQDTMQGTGRSLRLIQ 1008
Cdd:COG1196   225 LEAELLLLKL---RELEAELEELEAELEELEAELEELEAELAELEAELE----ELRL---ELEELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1009 ERVGEVQQVLVPAErlvkgmkeqmsgfwARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRL 1088
Cdd:COG1196   295 AELARLEQDIARLE--------------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                  ...
gi 113865981 1089 GQS 1091
Cdd:COG1196   361 AEA 363
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
829-1088 2.13e-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: 48.35  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   829 GRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllMEEDVQRTRLLIQQVRGFLTD----------- 897
Cdd:pfam07888   34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----LESRVAELKEELRQSREKHEEleekykelsas 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   898 -----PDTDAATIQQVSEAVLALWLPTDSATVLRKMKEIQAIAARLPN-VDSVLSQTKQDIARARRLQAEAEQARSRAHA 971
Cdd:pfam07888  110 seelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   972 VEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGE----------VQQVLVPAERLVKGMKEQMSGfwarMKE 1041
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEnealleelrsLQERLNASERKVEGLGEELSS----MAA 265
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 113865981  1042 LRRQAQEEQAQA-MQARQLAEGASQQAMNAQEGFKRLKQKYTEL-------KDRL 1088
Cdd:pfam07888  266 QRDRTQAELHQArLQAAQLTLQLADASLALREGRARWAQERETLqqsaeadKDRI 320
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
259-299 3.37e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 42.30  E-value: 3.37e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 113865981    259 CAPNPGGSTTAV--QVNNVCVCQHNTAGPNCDRCAPFYNNRPW 299
Cdd:smart00180    1 CDCDPGGSASGTcdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
312-362 5.96e-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: 41.57  E-value: 5.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 113865981  312 RCDCNGH---SETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRN 362
Cdd:cd00055     1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
830-1090 9.60e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVS--TSRLLMEEDVQRTR------------LLIQQVRGFL 895
Cdd:COG4717   189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKearlllliaaalLALLGLGGSL 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  896 TDPDTDAATIQQVSEAVLAL---WLPTDSATVLRKMKEIQAIAAR-------------------------LPNVDSVLSQ 947
Cdd:COG4717   269 LSLILTIAGVLFLVLGLLALlflLLAREKASLGKEAEELQALPALeeleeeeleellaalglppdlspeeLLELLDRIEE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  948 TKQDIARARRLQAEAEQARSRAHAVE----GQVDDvVGNLRQGTVALQEAQDTMQgtgrSLRLIQERVGEvqQVLVPAER 1023
Cdd:COG4717   349 LQELLREAEELEEELQLEELEQEIAAllaeAGVED-EEELRAALEQAEEYQELKE----ELEELEEQLEE--LLGELEEL 421
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981 1024 LVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEgFKRLKQKYTELKDRLGQ 1090
Cdd:COG4717   422 LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-LAELLQELEELKAELRE 487
growth_prot_Scy NF041483
polarized growth protein Scy;
844-1114 1.10e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 46.74  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  844 QTRQMIRAAEEAASRVQADAQR--LETQVSTSRLLME--------------EDVQRTRLLIQQVrgfltdpDTDAATIQ- 906
Cdd:NF041483   73 QAEQLLRNAQIQADQLRADAERelRDARAQTQRILQEhaehqarlqaelhtEAVQRRQQLDQEL-------AERRQTVEs 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  907 QVSEAVLalWlptdsATVLRKMKEIQAiaARLpnVDSVLSQTKQDIARAR------------RLQAEAEQARSRAHAVEG 974
Cdd:NF041483  146 HVNENVA--W-----AEQLRARTESQA--RRL--LDESRAEAEQALAAARaeaerlaeearqRLGSEAESARAEAEAILR 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  975 QV-DDVVGNLRQGTVALQEAqdtmqgTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQE--EQA 1051
Cdd:NF041483  215 RArKDAERLLNAASTQAQEA------TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvAEA 288
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981 1052 QAMQARQL--AEGASQQAM-NAQEGFKRLKQKYTElkdrlgQSPVLGEQGNRILS-IKMEAEELFGE 1114
Cdd:NF041483  289 KEAAAKQLasAESANEQRTrTAKEEIARLVGEATK------EAEALKAEAEQALAdARAEAEKLVAE 349
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
942-1095 1.15e-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: 45.49  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   942 DSVLSQTKQDIARARRLQAEAEQAR-----SRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERV----- 1011
Cdd:pfam00529   52 DPTDYQAALDSAEAQLAKAQAQVARlqaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrv 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  1012 -----GEVQQVLVPAERLVKGMKEQMSGFWARMKELrrQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKD 1086
Cdd:pfam00529  132 lapigGISRESLVTAGALVAQAQANLLATVAQLDQI--YVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209

                   ....*....
gi 113865981  1087 RLGQSPVLG 1095
Cdd:pfam00529  210 TEIRAPVDG 218
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
832-1076 1.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  832 AEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQvstsrllmeedvqrtRLLIQQVRGFLtdpdtdaatiqqvsea 911
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER---------------REALQRLAEYS---------------- 657
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  912 vlalWLPTDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQ 991
Cdd:COG4913   658 ----WDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  992 EAQDTMQGTGRSLR--LIQERVGEVQQvlvpaerlvkgmkeqmsgfWARMKELRRQAQEEQAqamQARQLAEGASQQAMN 1069
Cdd:COG4913   734 DRLEAAEDLARLELraLLEERFAAALG-------------------DAVERELRENLEERID---ALRARLNRAEEELER 791

                  ....*..
gi 113865981 1070 AQEGFKR 1076
Cdd:COG4913   792 AMRAFNR 798
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
843-1072 1.95e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.71  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  843 QQTR-----QMIRAAEEAASRVQAD---AQRLETQVSTSRllMEEDVQRTRLLIQQVRgfLTDPDTDAATIQQVSEAVLA 914
Cdd:COG3096   408 QQTRaiqyqQAVQALEKARALCGLPdltPENAEDYLAAFR--AKEQQATEEVLELEQK--LSVADAARRQFEKAYELVCK 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  915 LWLPTDSAT-------VLRKMKEIQAIAARLPNVDSVLSQTKQDIAR---ARRLQAEAEQARSRAHAVEGQVDDVvgnlr 984
Cdd:COG3096   484 IAGEVERSQawqtareLLRRYRSQQALAQRLQQLRAQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEEL----- 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  985 qgtvaLQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaerlvkgmkEQMSgfwARMKELRRQAQEEQAQAMQARQLAEGAS 1064
Cdd:COG3096   559 -----LAELEAQLEELEEQAAEAVEQRSELRQQL-----------EQLR---ARIKELAARAPAWLAAQDALERLREQSG 619

                  ....*...
gi 113865981 1065 QQAMNAQE 1072
Cdd:COG3096   620 EALADSQE 627
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
828-1078 2.33e-04

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: 44.20  E-value: 2.33e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    828 AGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRtrllIQQVRGfltdpdtdaaTIQQ 907
Cdd:smart00283   13 AEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITA----MDQIRE----------VVEE 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    908 VSEAVLALwlptdsatvLRKMKEIQAIAArlpNVDSVLSQTkqDI---------ARA--------------RRL----QA 960
Cdd:smart00283   79 AVSAVEEL---------EESSDEIGEIVS---VIDDIADQT--NLlalnaaieaARAgeagrgfavvadevRKLaersAE 144
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981    961 EAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLvpaERLVKGMKEQMSG---FWA 1037
Cdd:smart00283  145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLV---QEIAAATDEQAAGseeVNA 221
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 113865981   1038 RMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLK 1078
Cdd:smart00283  222 AIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
929-1111 3.01e-04

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: 44.37  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  929 KEIQAIAARLPNVDSVLSQTKQDIaraRRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGR----SL 1004
Cdd:COG4942    48 KEEKALLKQLAALERRIAALARRI---RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1005 RLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQamnaQEGFKRLKQKYTEL 1084
Cdd:COG4942   125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE----RAALEALKAERQKL 200
                         170       180
                  ....*....|....*....|....*..
gi 113865981 1085 KDRLGQSpvLGEQGNRILSIKMEAEEL 1111
Cdd:COG4942   201 LARLEKE--LAELAAELAELQQEAEEL 225
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
830-1090 3.93e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   830 RVAE-QLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVstSRLLMEEDVQ---RTRLLIQQVRGFLTDPDTDAati 905
Cdd:pfam01576  688 RALEqQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF--ERDLQARDEQgeeKRRQLVKQVRELEAELEDER--- 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   906 QQVSEAVLA----------LWLPTDSAT--------VLRK----MKEIQ-----AIAARlpnvDSVLSQTKQDIARARRL 958
Cdd:pfam01576  763 KQRAQAVAAkkkleldlkeLEAQIDAANkgreeavkQLKKlqaqMKDLQreleeARASR----DEILAQSKESEKKLKNL 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   959 QAE----------AEQARSRAHAVEGQVDDVVGNLRQGTVALQ------------------EAQDTMQGTGRSLRLIQER 1010
Cdd:pfam01576  839 EAEllqlqedlaaSERARRQAQQERDELADEIASGASGKSALQdekrrleariaqleeeleEEQSNTELLNDRLRKSTLQ 918
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  1011 VGEVQQVLVpAERL----VKGMKEQMSgfwARMKELRRQAQEEQAQ----------AMQAR--QLAEGASQQAMNAQEGF 1074
Cdd:pfam01576  919 VEQLTTELA-AERStsqkSESARQQLE---RQNKELKAKLQEMEGTvkskfkssiaALEAKiaQLEEQLEQESRERQAAN 994
                          330
                   ....*....|....*.
gi 113865981  1075 KRLKQKYTELKDRLGQ 1090
Cdd:pfam01576  995 KLVRRTEKKLKEVLLQ 1010
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
952-1155 7.20e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  952 IARARRLQAEAEQARSRAHAVEGQVDdvvgnlrqgtvALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERL--VKGMK 1029
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLE-----------ALEAELDALQERREALQRLAEYSWDEIDVASAEREIaeLEAEL 677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1030 EQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRIlsikmEAE 1109
Cdd:COG4913   678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-----LLE 752
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 113865981 1110 ELFGEtmemmDKMKDMESELLRG-SQAIMLRSADLSGLEKRVEQIRS 1155
Cdd:COG4913   753 ERFAA-----ALGDAVERELRENlEERIDALRARLNRAEEELERAMR 794
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
313-366 8.92e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 8.92e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981    313 CDCNG---HSETCHFDpavfaasqgtnGGVCDnCRDHTEGKNCERCQLHYFRNRRPS 366
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
842-1090 9.67e-04

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: 43.52  E-value: 9.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFltdpdtdaatIQQVSEAVLAlwlptds 921
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----------LSSLEQEIEN------- 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   922 atvlrKMKEIQAIAARLPNVDSVLSQTKQDIA---------RARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQE 992
Cdd:TIGR02169  756 -----VKSELKELEARIEELEEDLHKLEEALNdlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   993 AQDTMQGTGRSLRLIQERVGEVQQvlvpAERLVKGMKEQMSG-----------FWARMKELRRQAQEEQAQAMQARQLAE 1061
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEK----EIENLNGKKEELEEeleeleaalrdLESRLGDLKKERDELEAQLRELERKIE 906
                          250       260
                   ....*....|....*....|....*....
gi 113865981  1062 GASQQAMNAQEGFKRLKQKYTELKDRLGQ 1090
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEEELSE 935
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
830-1112 1.12e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSrllmEEDVQRTRLLIQQVRgfltdpdtdaATIQQVS 909
Cdd:COG4372    42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL----NEQLQAAQAELAQAQ----------EELESLQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  910 EAvlalwlptdsATVLRkmKEIQAIAARLPNVDSVLSQTKQDIArarRLQAEAEQARSRAHAVEGQVDdvvgNLRQGTVA 989
Cdd:COG4372   108 EE----------AEELQ--EELEELQKERQDLEQQRKQLEAQIA---ELQSEIAEREEELKELEEQLE----SLQEELAA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  990 LQEAQDTMqgtgrslrLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAM-------QARQLAEG 1062
Cdd:COG4372   169 LEQELQAL--------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsleaklgLALSALLD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 113865981 1063 ASQQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAEELF 1112
Cdd:COG4372   241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
817-1112 1.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  817 ALPRAKGAFHMAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTsrllmEEDVQRTRLLIQQVRGFLT 896
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  897 DPDTDAATIQQVSEAVLAlwLPTDSATVLRKMKEIQAIAARLPNVDSV-LSQTKQDI----ARARRLQAEAEQARSRAHA 971
Cdd:COG4717   147 RLEELEERLEELRELEEE--LEELEAELAELQEELEELLEQLSLATEEeLQDLAEELeelqQRLAELEEELEEAQEELEE 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  972 VEGQVDDVVGNLRQGTVA--LQEAQDT---------MQGTGRSLRLIQERVGEVQQVLVPA----------ERLVKGMKE 1030
Cdd:COG4717   225 LEEELEQLENELEAAALEerLKEARLLlliaaallaLLGLGGSLLSLILTIAGVLFLVLGLlallflllarEKASLGKEA 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1031 QMSGFWARMKELRRQAQEEQAQAMQARQLAEGAS-QQAMNAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIKMEAE 1109
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384

                  ...
gi 113865981 1110 ELF 1112
Cdd:COG4717   385 EEL 387
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
840-1063 1.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  840 TQLQQTRQMIRAAEEAASRVQADAQRLETqvstsrllMEEDVQRTRLLIQQVRgfltdpdTDAATIQQVSEAvLALWlpt 919
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELR-------EELEKLEKLLQL-LPLY--- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  920 dsatvlrkmKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDdvvgnlRQGTVALQEAQDTMQG 999
Cdd:COG4717   132 ---------QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQD 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113865981 1000 TGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWarmKELRRQAQEEQAQAMQARQLAEGA 1063
Cdd:COG4717   197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLE---NELEAAALEERLKEARLLLLIAAA 257
growth_prot_Scy NF041483
polarized growth protein Scy;
832-1065 1.44e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  832 AEQLRNFNT-QLQQTR-----------QMIRAAEEAASRVQADAQRLETQVSTS---RLLMEEDV--QRTRLLIQQVRGF 894
Cdd:NF041483  238 AEQLRSSTAaESDQARrqaaelsraaeQRMQEAEEALREARAEAEKVVAEAKEAaakQLASAESAneQRTRTAKEEIARL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  895 LTDPDTDAATIQQVSEAVLA------------------LWLPTDSATVLRKmkeiqaiAARlpNVDSVLSQTKQDiARAR 956
Cdd:NF041483  318 VGEATKEAEALKAEAEQALAdaraeaeklvaeaaekarTVAAEDTAAQLAK-------AAR--TAEEVLTKASED-AKAT 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  957 -----------RLQAEAEQARSRAHAVE------GQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRliQERVGE------ 1013
Cdd:NF041483  388 traaaeeaeriRREAEAEADRLRGEAADqaeqlkGAAKDDTKEYRAKTVELQEEARRLRGEAEQLR--AEAVAEgerirg 465
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113865981 1014 ------VQQV---LVPAERLVKGMK----EQMSGFWA-----------RMKELRRQAQE--EQAQAMQARQLAEGASQ 1065
Cdd:NF041483  466 earreaVQQIeeaARTAEELLTKAKadadELRSTATAeservrteaieRATTLRRQAEEtlERTRAEAERLRAEAEEQ 543
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
831-1069 1.52e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   831 VAEQLRNfntQLQQTRQMIraAEEAA------SRVQADAQRLETQVSTsrllMEEDVQ-----------RTRLLIQQVRG 893
Cdd:pfam01576  851 ASERARR---QAQQERDEL--ADEIAsgasgkSALQDEKRRLEARIAQ----LEEELEeeqsntellndRLRKSTLQVEQ 921
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   894 FLTDPDTDAATIQQVSEAvlalwlptdSATVLRKMKEIQAiaaRLPNVDS-VLSQTKQDIARarrLQAEAEQArsrahav 972
Cdd:pfam01576  922 LTTELAAERSTSQKSESA---------RQQLERQNKELKA---KLQEMEGtVKSKFKSSIAA---LEAKIAQL------- 979
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   973 EGQVDdvvgnlrqgtvalQEAQDTmQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQ--EEQ 1050
Cdd:pfam01576  980 EEQLE-------------QESRER-QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEeaEEE 1045
                          250       260
                   ....*....|....*....|....*.
gi 113865981  1051 AQAMQA------RQLAEGA-SQQAMN 1069
Cdd:pfam01576 1046 ASRANAarrklqRELDDATeSNESMN 1071
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
929-1111 1.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  929 KEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVGNLRQGTVALQEAQDTMQGTGRSLRLIQ 1008
Cdd:PRK03918  200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1009 ERVGEVQQVLVPAERLVKgMKEQMSGFWARMKELRRQAQ--EEQAQAMQaRQLAEGASQqamnaQEGFKRLKQKYTELKD 1086
Cdd:PRK03918  280 EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSrlEEEINGIE-ERIKELEEK-----EERLEELKKKLKELEK 352
                         170       180
                  ....*....|....*....|....*
gi 113865981 1087 RLGQSPVLGEQGNRILSIKMEAEEL 1111
Cdd:PRK03918  353 RLEELEERHELYEEAKAKKEELERL 377
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
852-1090 1.70e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  852 AEEAASRVQADAQRLETQVStsrllmeeDVQRTrLLIQQVRgfltdpdtdAATIQQVSEAvlalwlptdsatvLRKMKEI 931
Cdd:COG3096   380 AEARLEAAEEEVDSLKSQLA--------DYQQA-LDVQQTR---------AIQYQQAVQA-------------LEKARAL 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  932 QAIAARLP-NVDSVL--SQTKQDIARARRLQAE-----AEQARSRAHAVEGQVDDVVGNLRQGTvALQEAQDTMQgTGRS 1003
Cdd:COG3096   429 CGLPDLTPeNAEDYLaaFRAKEQQATEEVLELEqklsvADAARRQFEKAYELVCKIAGEVERSQ-AWQTARELLR-RYRS 506
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981 1004 LRLIQERVGEVQQVLVPAERLV---KGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQK 1080
Cdd:COG3096   507 QQALAQRLQQLRAQLAELEQRLrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
                         250
                  ....*....|
gi 113865981 1081 YTELKDRLGQ 1090
Cdd:COG3096   587 LEQLRARIKE 596
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
966-1086 2.48e-03

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: 40.82  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981   966 RSRAHAVEGQVDDVVGNLRQgtvALQEAQDTMQGTGRSL-------RLIQERVGEVQQVlvpAERLVKGMKEQMSG---- 1034
Cdd:pfam04012   10 RANIHEGLDKAEDPEKMLEQ---AIRDMQSELVKARQALaqtiarqKQLERRLEQQTEQ---AKKLEEKAQAALTKgnee 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 113865981  1035 ----FWARMKELRRQAQEEQAQAMQARQLAEgasqqamNAQEGFKRLKQKYTELKD 1086
Cdd:pfam04012   84 lareALAEKKSLEKQAEALETQLAQQRSAVE-------QLRKQLAALETKIQQLKA 132
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
842-1084 2.96e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRllmeEDVQRTRLLIQQVRgfLTDPDTDAATIQQVSEAVLALwlptDS 921
Cdd:COG3096   838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLK----EQLQLLNKLLPQAN--LLADETLADRLEELREELDAA----QE 907
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  922 AtvlrkMKEIQAIAARLPNVDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQV---DDVVGNLRQgtVALQEAQDtMQ 998
Cdd:COG3096   908 A-----QAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPH--FSYEDAVG-LL 979
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  999 GTGRSLrliqerVGEVQQVLVPAERLVKGMKEQMsgfwarmkelrRQAQEEQAQAMQARQLAEGASQqamNAQEGFKRLK 1078
Cdd:COG3096   980 GENSDL------NEKLRARLEQAEEARREAREQL-----------RQAQAQYSQYNQVLASLKSSRD---AKQQTLQELE 1039

                  ....*.
gi 113865981 1079 QKYTEL 1084
Cdd:COG3096  1040 QELEEL 1045
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
830-1105 2.96e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  830 RVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQVRGFLTDPDTDAATIQQVS 909
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  910 EAVLALWlptDSATVLRKMKEIQAIAARLPNVDSVLSQTKQDIARARRLQ-AEAEQARSRAHAVEGQVDDVVGNLRQGTV 988
Cdd:COG4372   157 EQLESLQ---EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAeAEKLIESLPRELAEELLEAKDSLEAKLGL 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  989 ALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAM 1068
Cdd:COG4372   234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 113865981 1069 NAQEGFKRLKQKYTELKDRLGQSPVLGEQGNRILSIK 1105
Cdd:COG4372   314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
growth_prot_Scy NF041483
polarized growth protein Scy;
828-1088 4.48e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  828 AGRVAEQLRNFNTQLQ-QTRQMI----RAAEEAASRVQADAQ----RLETQVSTSRLLMEEDVQRTRLLIQQvrgfltdp 898
Cdd:NF041483  773 AEQTAQQVRDSVAGLQeQAEEEIaglrSAAEHAAERTRTEAQeeadRVRSDAYAERERASEDANRLRREAQE-------- 844
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  899 DTDAATI---QQVSEAVlalwlptDSATVLRKMKEIQAIAARLPNVDSvLSQTKQDIARARrlqAEA-EQARSRAHAVEG 974
Cdd:NF041483  845 ETEAAKAlaeRTVSEAI-------AEAERLRSDASEYAQRVRTEASDT-LASAEQDAARTR---ADArEDANRIRSDAAA 913
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  975 QVDDVVGNLRQGTVALQEAqdtmqGTGRSLRLIQERVGEVQQVLVPAERLVKGMKEQMSGFWARmkeLRRQAQEEQAQAM 1054
Cdd:NF041483  914 QADRLIGEATSEAERLTAE-----ARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER---LRAEAAETVGSAQ 985
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 113865981 1055 QA--RQLAEGASQQAMNAQEGfKRLKQKYTELKDRL 1088
Cdd:NF041483  986 QHaeRIRTEAERVKAEAAAEA-ERLRTEAREEADRT 1020
growth_prot_Scy NF041483
polarized growth protein Scy;
827-1110 6.07e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  827 MAGRVAEQLRNFNTQLQQTRQMIRAAEEAASRVQADAQRL--ETQVSTSRLLMEEdVQRTRLLIQQVRG----FLTDPDT 900
Cdd:NF041483  566 IAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIrrEAAEETERLRTEA-AERIRTLQAQAEQeaerLRTEAAA 644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  901 DAATIQQVSEAVlALWLPTDSATVLRKMK------------EIQAIAARLPN-VDSVLSQTKQDIARARR--------LQ 959
Cdd:NF041483  645 DASAARAEGENV-AVRLRSEAAAEAERLKseaqesadrvraEAAAAAERVGTeAAEALAAAQEEAARRRReaeetlgsAR 723
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  960 AEAEQARSRAHAvegQVDDVVGNLRQgtvALQEAQDTMQgtgrslRLIQERVGEVQQVLVPAERLVKGMKEQMSGfwarm 1039
Cdd:NF041483  724 AEADQERERARE---QSEELLASARK---RVEEAQAEAQ------RLVEEADRRATELVSAAEQTAQQVRDSVAG----- 786
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113865981 1040 keLRRQAQEEQAqamQARQLAEGASQQA-MNAQEGFKRLKQKYTELKDRlgqspvLGEQGNRILSIKMEAEE 1110
Cdd:NF041483  787 --LQEQAEEEIA---GLRSAAEHAAERTrTEAQEEADRVRSDAYAERER------ASEDANRLRREAQEETE 847
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
945-1090 7.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  945 LSQTKQDIARAR-----------RLQAEAEQARsRAHAVEGQVDdvvgnLRQGTVALQEaqdtmqgtgrsLRLIQERVGE 1013
Cdd:COG1196   181 LEATEENLERLEdilgelerqlePLERQAEKAE-RYRELKEELK-----ELEAELLLLK-----------LRELEAELEE 243
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113865981 1014 VQQVLVPAERLVKGMKEQMSGFWARMKELRRQAQEEQAQAMQARQLAEGASQQAMNAQEGFKRLKQKYTELKDRLGQ 1090
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
842-998 8.80e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.04  E-value: 8.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  842 LQQTRQMIRAAEEAASRVQADAQRLETQVSTSRLLMEEDVQRTRLLIQQ-----VRGFLTDpdtdAATIQQVSEAVLALW 916
Cdd:COG1842    32 IRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALER----KAELEAQAEALEAQL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  917 lpTDSATVLRKMKE-IQAIAARLPNVdsvlsQTKQDIARARRLQAEAEQARSRAHAvEGQVDDVVGNLRQgtvaLQEAQD 995
Cdd:COG1842   108 --AQLEEQVEKLKEaLRQLESKLEEL-----KAKKDTLKARAKAAKAQEKVNEALS-GIDSDDATSALER----MEEKIE 175

                  ...
gi 113865981  996 TMQ 998
Cdd:COG1842   176 EME 178
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
829-1100 9.14e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 40.17  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  829 GRVAEQLRNFNTQLQQT----RQMIRAAEEAASRVQADAQRLetqvstSRLLMEEDvqRTRLLIQQV---RGFLTDPDTD 901
Cdd:PRK10246  307 AHTRQQIEEVNTRLQSTmalrARIRHHAAKQSAELQAQQQSL------NTWLAEHD--RFRQWNNELagwRAQFSQQTSD 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  902 AATIQQVSEAVLALwlptdsatvlrkmkeIQAIAArLPnvDSVLSQTKQDIARARRLQAEAEQARSRAHAVEGQVDDVVG 981
Cdd:PRK10246  379 REQLRQWQQQLTHA---------------EQKLNA-LP--AITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQK 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113865981  982 NLRQGTVALQEAQDTMQGTGRSLRLIQERVGEVQQVLVPaerlVKGMKEQMsgfwARMKELRRQ-AQEEQAQ-------- 1052
Cdd:PRK10246  441 RLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD----VKTICEQE----ARIKDLEAQrAQLQAGQpcplcgst 512
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 113865981 1053 ---AMQARQ-LAEGASQQAMNAQEgfKRLKQKYTELKDRLGQSPVLGEQGNR 1100
Cdd:PRK10246  513 shpAVEAYQaLEPGVNQSRLDALE--KEVKKLGEEGAALRGQLDALTKQLQR 562
 
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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