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Conserved domains on  [gi|24582614|ref|NP_723319|]
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LanB1, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
54-286 2.00e-100

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 321.84  E-value: 2.00e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     54 CYPATGNLLIGREnrLTASSTCGLHSPERFCILSHLQD-KKCFLCDTReetkhDPYKNHRIGQIIYkTKPGTNiPTWWQS 132
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILSGLEGgKKCFICDSR-----DPHNSHPPSNLTD-SNNGTN-ETWWQS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    133 ENGK---ENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENI--TDVMC 207
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkdDEVIC 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    208 TSRYSNVEPSRNGEVIFRVL--PPNINVTDpYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENeEKYYYGISNMVVR 285
Cdd:pfam00055  152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVL-RKYYYAISDISVG 229


                   .
gi 24582614    286 G 286
Cdd:pfam00055  230 G 230
cc_DmLAMB1-like_C cd22302
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ...
 1717-1786 3.80e-26

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


:

Pssm-ID: 411973 [Multi-domain]  Cd Length: 70  Bit Score: 103.08  E-value: 3.80e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1717 RERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQC 1786
Cdd:cd22302    1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1228-1771 5.44e-19

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


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 93.55  E-value: 5.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1228 SEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSlrdQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLV- 1306
Cdd:TIGR04523   33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE---KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIn 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1307 -------QQLSK---ELKENGIQLQESNIEGALNLTRhayervsnLSTLKDEANELASNTDRNCKRVENLSNKIQAEADD 1376
Cdd:TIGR04523  110 seikndkEQKNKlevELNKLEKQKKENKKNIDKFLTE--------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1377 LANNNKLIEDYRAELT-----------------SLTSQIPELNNQVcgkpgdpcdslcggagcghcggflscehgakths 1439
Cdd:TIGR04523  182 KLNIQKNIDKIKNKLLklelllsnlkkkiqknkSLESQISELKKQN---------------------------------- 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1440 eealkvaKDAETAITSKKDQADQTIRAL--TQAKLN-ASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQE-- 1514
Cdd:TIGR04523  228 -------NQLKDNIEKKQQEINEKTTEIsnTQTQLNqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdl 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1515 NKTASPSESKELAQKTLDLDLKLEpeEIETLGDQINRAVSSLKNVEAIIYRTKPDLDrvNNLQSIANATKEKADKIldsa 1594
Cdd:TIGR04523  301 NNQKEQDWNKELKSELKNQEKKLE--EIQNQISQNNKIISQLNEQISQLKKELTNSE--SENSEKQRELEEKQNEI---- 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1595 nsvvESLAaaDESQGKaKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEI 1674
Cdd:TIGR04523  373 ----EKLK--KENQSY-KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1675 TKEAGSVKLEAmrargeaNNLQSATSATNQTLtDRASRS-----ENARERAKQLLQRASKL------TVDTNAKLKDLND 1743
Cdd:TIGR04523  446 TNQDSVKELII-------KNLDNTRESLETQL-KVLSRSinkikQNLEQKQKELKSKEKELkklneeKKELEEKVKDLTK 517

                          570       580       590
                   ....*....|....*....|....*....|..
gi 24582614   1744 LQTVYLNKNQQL----LRLQAEIGPLNKELNE 1771
Cdd:TIGR04523  518 KISSLKEKIEKLesekKEKESKISDLEDELNK 549
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1094-1142 1.09e-14

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 69.69  E-value: 1.09e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614   1094 CNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQPC 1142
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
789-834 2.69e-14

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.49  E-value: 2.69e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614     789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGC 834
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 837-885 3.59e-14

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 68.15  E-value: 3.59e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614    837 CDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRVCQC 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 418-475 7.35e-12

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 7.35e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582614    418 CDCDPQGSSDDGiCDSlneleegaVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGC 475
Cdd:pfam00053    1 CDCNPHGSLSDT-CDP--------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1043-1091 5.56e-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: 59.29  E-value: 5.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614   1043 CECDFLGTNNtiAHCDRFTGQCPCLPNVQGVRCDQCAENHW--KIASGEGC 1091
Cdd:pfam00053    1 CDCNPHGSLS--DTCDPETGQCLCKPGVTGRHCDRCKPGYYglPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
529-567 1.70e-09

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.01  E-value: 1.70e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 24582614     529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 477-526 2.51e-09

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


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 54.67  E-value: 2.51e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24582614  477 PCTCNPLGTLNNSgCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGC 526
Cdd:cd00055    1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1142-1190 1.72e-08

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.97  E-value: 1.72e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614   1142 CECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGqFPHCSPCG 1190
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQG 48
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 883-930 4.62e-08

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 50.81  E-value: 4.62e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614    883 CQCNGHAA---TCDPIQGTCiDCQDSTTGYSCDSCLDGYYGNPlFGSEIGC 930
Cdd:pfam00053    1 CDCNPHGSlsdTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 991-1035 4.03e-07

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 4.03e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 24582614    991 CECSNNVDLYDTgnCDRQTGACLkCLYQTTGDHCELCKDGFFGDA 1035
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 287-343 2.62e-05

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


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 43.11  E-value: 2.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614  287 SCSCYGHASQCLPLDPafsqadnedgmVHGRCECTHNTKGMNCEECEDFFNDLPWKP 343
Cdd:cd00055    1 PCDCNGHGSLSGQCDP-----------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 933-988 5.46e-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: 42.34  E-value: 5.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614    933 CRCPETVASGlahaDGCSLDTrnnnMLCHCQEGYSGSRCEICADNFFGNP-DNGGTC 988
Cdd:pfam00053    1 CDCNPHGSLS----DTCDPET----GQCLCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 355-415 9.84e-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: 41.57  E-value: 9.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582614    355 CECNDHAV---SCHFdeavftasgfvSGGVCDnCLHNTRGQHCEECMPYFYRDPeqdITSERVC 415
Cdd:pfam00053    1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
54-286 2.00e-100

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 321.84  E-value: 2.00e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     54 CYPATGNLLIGREnrLTASSTCGLHSPERFCILSHLQD-KKCFLCDTReetkhDPYKNHRIGQIIYkTKPGTNiPTWWQS 132
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILSGLEGgKKCFICDSR-----DPHNSHPPSNLTD-SNNGTN-ETWWQS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    133 ENGK---ENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENI--TDVMC 207
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkdDEVIC 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    208 TSRYSNVEPSRNGEVIFRVL--PPNINVTDpYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENeEKYYYGISNMVVR 285
Cdd:pfam00055  152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVL-RKYYYAISDISVG 229


                   .
gi 24582614    286 G 286
Cdd:pfam00055  230 G 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 48-286 1.20e-96

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: 311.60  E-value: 1.20e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614      48 PCERSSCYPATGNLLIGREnrLTASSTCGLHSPERFCIL--SHLQDKKCFLCDTReetkhDPYKNHRIGQIIYKTKPgtN 125
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDAR-----NPRRSHPAENLTDGNNP--N 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     126 IPTWWQSEN---GKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSfDFGQTWHIYRYFAYDCKESFPGVPTVLE-- 200
Cdd:smart00136   72 NPTWWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPItk 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     201 -NITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTD-PYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYG 278
Cdd:smart00136  151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230


                    ....*...
gi 24582614     279 ISNMVVRG 286
Cdd:smart00136  231 ISDIAVGG 238
cc_DmLAMB1-like_C cd22302
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ...
 1717-1786 3.80e-26

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


Pssm-ID: 411973 [Multi-domain]  Cd Length: 70  Bit Score: 103.08  E-value: 3.80e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1717 RERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQC 1786
Cdd:cd22302    1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1228-1771 5.44e-19

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 93.55  E-value: 5.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1228 SEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSlrdQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLV- 1306
Cdd:TIGR04523   33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE---KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIn 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1307 -------QQLSK---ELKENGIQLQESNIEGALNLTRhayervsnLSTLKDEANELASNTDRNCKRVENLSNKIQAEADD 1376
Cdd:TIGR04523  110 seikndkEQKNKlevELNKLEKQKKENKKNIDKFLTE--------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1377 LANNNKLIEDYRAELT-----------------SLTSQIPELNNQVcgkpgdpcdslcggagcghcggflscehgakths 1439
Cdd:TIGR04523  182 KLNIQKNIDKIKNKLLklelllsnlkkkiqknkSLESQISELKKQN---------------------------------- 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1440 eealkvaKDAETAITSKKDQADQTIRAL--TQAKLN-ASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQE-- 1514
Cdd:TIGR04523  228 -------NQLKDNIEKKQQEINEKTTEIsnTQTQLNqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdl 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1515 NKTASPSESKELAQKTLDLDLKLEpeEIETLGDQINRAVSSLKNVEAIIYRTKPDLDrvNNLQSIANATKEKADKIldsa 1594
Cdd:TIGR04523  301 NNQKEQDWNKELKSELKNQEKKLE--EIQNQISQNNKIISQLNEQISQLKKELTNSE--SENSEKQRELEEKQNEI---- 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1595 nsvvESLAaaDESQGKaKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEI 1674
Cdd:TIGR04523  373 ----EKLK--KENQSY-KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1675 TKEAGSVKLEAmrargeaNNLQSATSATNQTLtDRASRS-----ENARERAKQLLQRASKL------TVDTNAKLKDLND 1743
Cdd:TIGR04523  446 TNQDSVKELII-------KNLDNTRESLETQL-KVLSRSinkikQNLEQKQKELKSKEKELkklneeKKELEEKVKDLTK 517

                          570       580       590
                   ....*....|....*....|....*....|..
gi 24582614   1744 LQTVYLNKNQQL----LRLQAEIGPLNKELNE 1771
Cdd:TIGR04523  518 KISSLKEKIEKLesekKEKESKISDLEDELNK 549
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1094-1142 1.09e-14

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 69.69  E-value: 1.09e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614   1094 CNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQPC 1142
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
789-834 2.69e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.49  E-value: 2.69e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614     789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGC 834
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 837-885 3.59e-14

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 68.15  E-value: 3.59e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614    837 CDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRVCQC 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 789-837 1.66e-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: 1.66e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614    789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGCKAC 837
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 789-835 5.55e-13

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 64.68  E-value: 5.55e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24582614  789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGF--GPEGCK 835
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1093-1135 7.37e-13

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 64.68  E-value: 7.37e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 24582614 1093 SCNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNP 1135
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1094-1139 1.12e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 63.87  E-value: 1.12e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614    1094 CNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKC 1139
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 836-879 1.14e-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: 63.91  E-value: 1.14e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 24582614  836 ACDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPE 879
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
837-880 2.65e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.71  E-value: 2.65e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614     837 CDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYW--NFPEC 880
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 418-475 7.35e-12

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 7.35e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582614    418 CDCDPQGSSDDGiCDSlneleegaVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGC 475
Cdd:pfam00053    1 CDCNPHGSLSDT-CDP--------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1043-1091 5.56e-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: 59.29  E-value: 5.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614   1043 CECDFLGTNNtiAHCDRFTGQCPCLPNVQGVRCDQCAENHW--KIASGEGC 1091
Cdd:pfam00053    1 CDCNPHGSLS--DTCDPETGQCLCKPGVTGRHCDRCKPGYYglPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1043-1091 6.44e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.17  E-value: 6.44e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24582614    1043 CECDFLGTNNTiaHCDRFTGQCPCLPNVQGVRCDQCAENHWKiASGEGC 1091
Cdd:smart00180    1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1043-1092 1.24e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.44  E-value: 1.24e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24582614 1043 CECDFLGTNNTiaHCDRFTGQCPCLPNVQGVRCDQCAENHWKIAS-GEGCE 1092
Cdd:cd00055    2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
529-567 1.70e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.01  E-value: 1.70e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 24582614     529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1526-1763 1.85e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1526 LAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDL----DRVNNLQSIANATKEKADKILDSANSVVESL 1601
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELeeleLELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1602 AAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAgsv 1681
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--- 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1682 kLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAE 1761
Cdd:COG1196  389 -LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                 ..
gi 24582614 1762 IG 1763
Cdd:COG1196  468 LL 469
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 477-526 2.51e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 54.67  E-value: 2.51e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24582614  477 PCTCNPLGTLNNSgCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGC 526
Cdd:cd00055    1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 529-567 3.79e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.90  E-value: 3.79e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 24582614  529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 417-476 3.86e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.90  E-value: 3.86e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  417 PCDCDPQGSSDdGICDSLNeleegavaGACHCKAFVTGRRCNQCKDGYWNLQSdNPEGCE 476
Cdd:cd00055    1 PCDCNGHGSLS-GQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 478-526 6.15e-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: 53.51  E-value: 6.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 24582614    478 CTCNPLGTLNnSGCVMRTGECKCKKYVTGKDCNQCMPETYGL-SESPEGC 526
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
418-475 1.31e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.31e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582614     418 CDCDPQGSSDDGiCDSLNeleegavaGACHCKAFVTGRRCNQCKDGYWNlqsDNPEGC 475
Cdd:smart00180    1 CDCDPGGSASGT-CDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1142-1190 1.72e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.97  E-value: 1.72e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614   1142 CECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGqFPHCSPCG 1190
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQG 48
growth_prot_Scy NF041483
polarized growth protein Scy;
1434-1727 1.82e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 59.84  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1434 GAKTHSEEALKVA-KDAETAITSKKDQADQT------IRALT-----QAKLNASEAYEKAKRGFEQSERYLNQTNANikl 1501
Cdd:NF041483  204 SARAEAEAILRRArKDAERLLNAASTQAQEAtdhaeqLRSSTaaesdQARRQAAELSRAAEQRMQEAEEALREARAE--- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1502 AENLFialnnfqenktaspSESKELAQKTLDLDLKLEPEEIETLGDQINRAVS-SLKNVEAiiyrTKPDLDrvnnlQSIA 1580
Cdd:NF041483  281 AEKVV--------------AEAKEAAAKQLASAESANEQRTRTAKEEIARLVGeATKEAEA----LKAEAE-----QALA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1581 NATKEkADKILDSANSVVESLAAADESQGKAK----------DAIQQANSNIELAGQDLEKIDEEtysAEAPANNTAQQV 1650
Cdd:NF041483  338 DARAE-AEKLVAEAAEKARTVAAEDTAAQLAKaartaeevltKASEDAKATTRAAAEEAERIRRE---AEAEADRLRGEA 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1651 EKLAKKVQKlqnnimkndrDAKEITKE--AGSVKL--EAMRARGEANNLQSATSATNQTLTDRASRS-----ENARERAK 1721
Cdd:NF041483  414 ADQAEQLKG----------AAKDDTKEyrAKTVELqeEARRLRGEAEQLRAEAVAEGERIRGEARREavqqiEEAARTAE 483


                  ....*.
gi 24582614  1722 QLLQRA 1727
Cdd:NF041483  484 ELLTKA 489
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1141-1189 3.33e-08

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 51.20  E-value: 3.33e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24582614 1141 PCECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGQFPHCSPC 1189
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 883-930 4.62e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 50.81  E-value: 4.62e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614    883 CQCNGHAA---TCDPIQGTCiDCQDSTTGYSCDSCLDGYYGNPlFGSEIGC 930
Cdd:pfam00053    1 CDCNPHGSlsdTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1528-1756 5.41e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.13  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1528 QKTLDLDLKLEPEEIET--LGDQINRAVSSLKNVEAIIyrtkpdlDRVNNLQSIANATKEKADKILDSANSVVESL---- 1601
Cdd:PRK02224  185 QRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLEEHEERREELetle 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1602 AAADESQGK----------AKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDA 1671
Cdd:PRK02224  258 AEIEDLRETiaeterereeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1672 KEITKEAGSV-----KLE--AMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVD----------- 1733
Cdd:PRK02224  338 QAHNEEAESLredadDLEerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgnaedfleel 417

                         250       260       270
                  ....*....|....*....|....*....|..
gi 24582614  1734 ------TNAKLKDLN-DLQTV--YLNKNQQLL 1756
Cdd:PRK02224  418 reerdeLREREAELEaTLRTAreRVEEAEALL 449
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 883-931 1.73e-07

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.27  E-value: 1.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24582614  883 CQCNGHAA---TCDPIQGTCIdCQDSTTGYSCDSCLDGYYGNPLFGSeiGCR 931
Cdd:cd00055    2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1142-1186 3.64e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.08  E-value: 3.64e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614    1142 CECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIG-QFPHC 1186
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-526 3.74e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.08  E-value: 3.74e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24582614     478 CTCNPLGTLNNSgCVMRTGECKCKKYVTGKDCNQCMPETYGlsESPEGC 526
Cdd:smart00180    1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG--DGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 991-1035 4.03e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 4.03e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 24582614    991 CECSNNVDLYDTgnCDRQTGACLkCLYQTTGDHCELCKDGFFGDA 1035
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1599-1769 6.65e-07

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 52.30  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1599 ESLAAADESQGKAKDAIQqansNIELAGQDLEKIDEetysAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEA 1678
Cdd:pfam12795    3 DELEKAKLDEAAKKKLLQ----DLQQALSLLDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1679 -GSVKLEAMRAR-----GEANNLQSATSATNQTLTDRASRSENARER---AKQLLQRASKLTVDTNAKLKDLNDLQTVYL 1749
Cdd:pfam12795   75 lASLSLEELEQRllqtsAQLQELQNQLAQLNSQLIELQTRPERAQQQlseARQRLQQIRNRLNGPAPPGEPLSEAQRWAL 154

                          170       180
                   ....*....|....*....|
gi 24582614   1750 NKNQQLLRLQAEIgpLNKEL 1769
Cdd:pfam12795  155 QAELAALKAQIDM--LEQEL 172
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 991-1041 4.71e-06

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 45.42  E-value: 4.71e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24582614  991 CECSNNVDLydTGNCDRQTGACLkCLYQTTGDHCELCKDGFFGDALQ-QNCQ 1041
Cdd:cd00055    2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 529-567 5.54e-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: 45.04  E-value: 5.54e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24582614    529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
 1545-1702 1.34e-05

Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.


Pssm-ID: 259842 [Multi-domain]  Cd Length: 158  Bit Score: 46.93  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1545 LGDQINRAVSSLKNVEAIIYRTKPDldrvNNLQSIANATKEKADKILDSANSVVESLA-AADESQGKAKDAIQQANSNIE 1623
Cdd:cd13769    3 LSELIQKAQEAINNLAQQVQKQLGL----QNPEEVVNTLKEQSDNFANNLQEVSSSLKeEAKKKQGEVEEAWNEFKTKLS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1624 LAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKE----ITKEAGSVKLEAmrargeANNLQ-SA 1698
Cdd:cd13769   79 ETVPELRKSLPVEEKAQELQAKLQSGLQTLVTESQKLAKAISENSQKAQEelqkATKQAYDIAVEA------AQNLQnQL 152


                 ....
gi 24582614 1699 TSAT 1702
Cdd:cd13769  153 QTAT 156
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 287-343 2.62e-05

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 43.11  E-value: 2.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614  287 SCSCYGHASQCLPLDPafsqadnedgmVHGRCECTHNTKGMNCEECEDFFNDLPWKP 343
Cdd:cd00055    1 PCDCNGHGSLSGQCDP-----------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 933-988 5.46e-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: 42.34  E-value: 5.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614    933 CRCPETVASGlahaDGCSLDTrnnnMLCHCQEGYSGSRCEICADNFFGNP-DNGGTC 988
Cdd:pfam00053    1 CDCNPHGSLS----DTCDPET----GQCLCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1438-1662 7.54e-05

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


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 46.51  E-value: 7.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1438 HSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERyLNQTNANIK-LAE--NLfIALNnfqe 1514
Cdd:smart00283   40 NADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDE-IGEIVSVIDdIADqtNL-LALN---- 113

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1515 nktAS----------------PSESKELAQKTLDldlklEPEEIETLgdqINRAVSSLKNVEAIIYRTKpdlDRVNNLQS 1578
Cdd:smart00283  114 ---AAieaarageagrgfavvADEVRKLAERSAE-----SAKEIESL---IKEIQEETNEAVAAMEESS---SEVEEGVE 179

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1579 IANATKEKADKILDSANSV---VESLAAADESQgkaKDAIQQANSNIElagqDLEKIDEETysaEAPANNTAQQVEKLAK 1655
Cdd:smart00283  180 LVEETGDALEEIVDSVEEIadlVQEIAAATDEQ---AAGSEEVNAAID----EIAQVTQET---AAMSEEISAAAEELSG 249


                    ....*..
gi 24582614    1656 KVQKLQN 1662
Cdd:smart00283  250 LAEELDE 256
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 355-415 9.84e-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: 41.57  E-value: 9.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582614    355 CECNDHAV---SCHFdeavftasgfvSGGVCDnCLHNTRGQHCEECMPYFYRDPeqdITSERVC 415
Cdd:pfam00053    1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 932-988 1.44e-04

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: 41.19  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614  932 PCRCPETVASGlahaDGCSLDTrnnnMLCHCQEGYSGSRCEICADNFFGNPDNGGTC 988
Cdd:cd00055    1 PCDCNGHGSLS----GQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
991-1034 2.21e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.37  E-value: 2.21e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24582614     991 CECsnNVDLYDTGNCDRQTGACLkCLYQTTGDHCELCKDGFFGD 1034
Cdd:smart00180    1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 355-407 6.73e-04

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: 39.26  E-value: 6.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24582614  355 CECNDHA---VSCHFDeavftasgfvsGGVCDnCLHNTRGQHCEECMPYFYRDPEQ 407
Cdd:cd00055    2 CDCNGHGslsGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 288-346 7.42e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.18  E-value: 7.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24582614    288 CSCYGHASQCLPLDPafsqadnedgmVHGRCECTHNTKGMNCEECEDFFNDLPWKPAFG 346
Cdd:pfam00053    1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
54-286 2.00e-100

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 321.84  E-value: 2.00e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     54 CYPATGNLLIGREnrLTASSTCGLHSPERFCILSHLQD-KKCFLCDTReetkhDPYKNHRIGQIIYkTKPGTNiPTWWQS 132
Cdd:pfam00055    1 CYPAFGNLAFGRE--VSATSTCGLNGPERYCILSGLEGgKKCFICDSR-----DPHNSHPPSNLTD-SNNGTN-ETWWQS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    133 ENGK---ENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSFDFGQTWHIYRYFAYDCKESFPGVPTVLENI--TDVMC 207
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkdDEVIC 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    208 TSRYSNVEPSRNGEVIFRVL--PPNINVTDpYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENeEKYYYGISNMVVR 285
Cdd:pfam00055  152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVL-RKYYYAISDISVG 229


                   .
gi 24582614    286 G 286
Cdd:pfam00055  230 G 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 48-286 1.20e-96

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: 311.60  E-value: 1.20e-96
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614      48 PCERSSCYPATGNLLIGREnrLTASSTCGLHSPERFCIL--SHLQDKKCFLCDTReetkhDPYKNHRIGQIIYKTKPgtN 125
Cdd:smart00136    1 AGRPRSCYPPFVNLAFGRE--VTATSTCGEPGPERYCKLvgHTEQGKKCDYCDAR-----NPRRSHPAENLTDGNNP--N 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     126 IPTWWQSEN---GKENATIQLDLEAEFHFTHLIITFTTFRPAAMYIERSfDFGQTWHIYRYFAYDCKESFPGVPTVLE-- 200
Cdd:smart00136   72 NPTWWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPItk 150

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614     201 -NITDVMCTSRYSNVEPSRNGEVIFRVLPPNINVTD-PYAEHVQNQLKMTNLRIQMTKLHKLGDNLLDSRLENEEKYYYG 278
Cdd:smart00136  151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230


                    ....*...
gi 24582614     279 ISNMVVRG 286
Cdd:smart00136  231 ISDIAVGG 238
cc_DmLAMB1-like_C cd22302
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ...
 1717-1786 3.80e-26

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


Pssm-ID: 411973 [Multi-domain]  Cd Length: 70  Bit Score: 103.08  E-value: 3.80e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1717 RERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQC 1786
Cdd:cd22302    1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
 1717-1786 8.79e-22

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: 90.42  E-value: 8.79e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1717 RERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKERGSHYRQC 1786
Cdd:cd22295    1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1228-1771 5.44e-19

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 93.55  E-value: 5.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1228 SEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSlrdQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLV- 1306
Cdd:TIGR04523   33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE---KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIn 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1307 -------QQLSK---ELKENGIQLQESNIEGALNLTRhayervsnLSTLKDEANELASNTDRNCKRVENLSNKIQAEADD 1376
Cdd:TIGR04523  110 seikndkEQKNKlevELNKLEKQKKENKKNIDKFLTE--------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1377 LANNNKLIEDYRAELT-----------------SLTSQIPELNNQVcgkpgdpcdslcggagcghcggflscehgakths 1439
Cdd:TIGR04523  182 KLNIQKNIDKIKNKLLklelllsnlkkkiqknkSLESQISELKKQN---------------------------------- 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1440 eealkvaKDAETAITSKKDQADQTIRAL--TQAKLN-ASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQE-- 1514
Cdd:TIGR04523  228 -------NQLKDNIEKKQQEINEKTTEIsnTQTQLNqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdl 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1515 NKTASPSESKELAQKTLDLDLKLEpeEIETLGDQINRAVSSLKNVEAIIYRTKPDLDrvNNLQSIANATKEKADKIldsa 1594
Cdd:TIGR04523  301 NNQKEQDWNKELKSELKNQEKKLE--EIQNQISQNNKIISQLNEQISQLKKELTNSE--SENSEKQRELEEKQNEI---- 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1595 nsvvESLAaaDESQGKaKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEI 1674
Cdd:TIGR04523  373 ----EKLK--KENQSY-KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1675 TKEAGSVKLEAmrargeaNNLQSATSATNQTLtDRASRS-----ENARERAKQLLQRASKL------TVDTNAKLKDLND 1743
Cdd:TIGR04523  446 TNQDSVKELII-------KNLDNTRESLETQL-KVLSRSinkikQNLEQKQKELKSKEKELkklneeKKELEEKVKDLTK 517

                          570       580       590
                   ....*....|....*....|....*....|..
gi 24582614   1744 LQTVYLNKNQQL----LRLQAEIGPLNKELNE 1771
Cdd:TIGR04523  518 KISSLKEKIEKLesekKEKESKISDLEDELNK 549
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1228-1778 1.56e-16

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: 86.26  E-value: 1.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1228 SEFSELDKKLQHIRNLLQNTSVSL----VDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQ-NH 1302
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEIsrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeEL 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1303 SRLVQQLSKELK-----ENGIQLQESNIE---GALNLTRHAYERVSN-LSTLKDEANELASNTDRNCKRVENL-----SN 1368
Cdd:TIGR02168  354 ESLEAELEELEAeleelESRLEELEEQLEtlrSKVAQLELQIASLNNeIERLEARLERLEDRRERLQQEIEELlkkleEA 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1369 KIQAEADDLANNNKLIED-------YRAELTSLTSQIPELNNQVCGKPGD------PCDSLcggagCGHCGGFLSCEHGA 1435
Cdd:TIGR02168  434 ELKELQAELEELEEELEElqeelerLEEALEELREELEEAEQALDAAERElaqlqaRLDSL-----ERLQENLEGFSEGV 508

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1436 KT---HSE----------EALKVAKDAETAI------------TSKKDQADQTIRALTQ----------------AKLNA 1474
Cdd:TIGR02168  509 KAllkNQSglsgilgvlsELISVDEGYEAAIeaalggrlqavvVENLNAAKKAIAFLKQnelgrvtflpldsikgTEIQG 588

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1475 SEAYEKA-KRGFEQSERYLNQTN-----------ANIKLAENLFIALN-----NFQEN------KTASPS-----ESKEL 1526
Cdd:TIGR02168  589 NDREILKnIEGFLGVAKDLVKFDpklrkalsyllGGVLVVDDLDNALElakklRPGYRivtldgDLVRPGgvitgGSAKT 668

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1527 AQKTLDLDlklepEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKILDSANsvvESLAAADE 1606
Cdd:TIGR02168  669 NSSILERR-----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR---KDLARLEA 740

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1607 SQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAM 1686
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1687 RARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLN 1766
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          650
                   ....*....|..
gi 24582614   1767 KELNEHLIHIKE 1778
Cdd:TIGR02168  901 EELRELESKRSE 912
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1094-1142 1.09e-14

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 69.69  E-value: 1.09e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614   1094 CNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKCQPC 1142
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
789-834 2.69e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 68.49  E-value: 2.69e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614     789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGC 834
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 837-885 3.59e-14

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 68.15  E-value: 3.59e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614    837 CDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPECRVCQC 885
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 789-837 1.66e-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: 1.66e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614    789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGFGPEGCKAC 837
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 789-835 5.55e-13

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 64.68  E-value: 5.55e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24582614  789 CNCNPTGSLSKVCESNGGYCQCKPNVVGRQCDQCAPGTYGF--GPEGCK 835
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1093-1135 7.37e-13

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 64.68  E-value: 7.37e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 24582614 1093 SCNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNP 1135
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1094-1139 1.12e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 63.87  E-value: 1.12e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614    1094 CNCDPIGALHEQCNSYTGQCQCKPGFGGRACNQCQAHYWGNPNEKC 1139
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 836-879 1.14e-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: 63.91  E-value: 1.14e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 24582614  836 ACDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYWNFPE 879
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
837-880 2.65e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 62.71  E-value: 2.65e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614     837 CDCNSIGSKDKYCDLITGQCQCVPNTYGRECNQCQPGYW--NFPEC 880
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1228-1778 3.14e-12

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 71.59  E-value: 3.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1228 SEFSELDKKLQH-----------IRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVEL 1296
Cdd:TIGR04523  124 VELNKLEKQKKEnkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1297 ESL----QNHSRLVQQLSkELKENGIQLQESNIEgalnLTRHAYERVSNLSTLKDEANELASNTDRNCKRvenLSNKIQa 1372
Cdd:TIGR04523  204 SNLkkkiQKNKSLESQIS-ELKKQNNQLKDNIEK----KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---LSEKQK- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1373 eadDLANNNKLIEDYRAELTSLTSQIPELNNQvcgkpgdpcdslcggagcghcggflscehgaktHSEEALKVAKDaetA 1452
Cdd:TIGR04523  275 ---ELEQNNKKIKELEKQLNQLKSEISDLNNQ---------------------------------KEQDWNKELKS---E 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1453 ITSKKDQADQTIRALTQAKLNASEayekakrgfeqseryLNQTNANIKlaenlfialnnfqenKTASPSES------KEL 1526
Cdd:TIGR04523  316 LKNQEKKLEEIQNQISQNNKIISQ---------------LNEQISQLK---------------KELTNSESensekqREL 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1527 AQKTldldlklepEEIETLGDQINRAVSSLKNVEAiiyrTKPDLDrvNNLQSIANATKEKADKI--LDSANSVVEslaaa 1604
Cdd:TIGR04523  366 EEKQ---------NEIEKLKKENQSYKQEIKNLES----QINDLE--SKIQNQEKLNQQKDEQIkkLQQEKELLE----- 425

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1605 dESQGKAKDAIQQANSNIElagqDLEkidEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEagsvkLE 1684
Cdd:TIGR04523  426 -KEIERLKETIIKNNSEIK----DLT---NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE-----LK 492

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1685 amRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLtvdtNAKLKDLND-------------LQTVYLNK 1751
Cdd:TIGR04523  493 --SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK----ESKISDLEDelnkddfelkkenLEKEIDEK 566

                          570       580       590
                   ....*....|....*....|....*....|
gi 24582614   1752 NQQLLRLQAEIGPL---NKELNEhLIHIKE 1778
Cdd:TIGR04523  567 NKEIEELKQTQKSLkkkQEEKQE-LIDQKE 595
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 418-475 7.35e-12

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 7.35e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582614    418 CDCDPQGSSDDGiCDSlneleegaVAGACHCKAFVTGRRCNQCKDGYWNLQSDNPEGC 475
Cdd:pfam00053    1 CDCNPHGSLSDT-CDP--------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1440-1778 2.90e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.93  E-value: 2.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1440 EEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENlfialnnfQENKTAS 1519
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--------EIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1520 PSESKELAQKTLDldlklepEEIETLGDQINRAVSSLKNVEAIIYRTKpdlDRVNNLQSIANATKEKADKILDSANSVVE 1599
Cdd:TIGR02168  769 RLEEAEEELAEAE-------AEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1600 SLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEET------YSAEAPANNTAQ-QVEKLAKKVQKLQNNIMKNDRDAK 1672
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallneRASLEEALALLRsELEELSEELRELESKRSELRRELE 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1673 EITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRaskltvdtnaKLKDLndlqtvylnkN 1752
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR----------RLKRL----------E 978

                          330       340       350
                   ....*....|....*....|....*....|...
gi 24582614   1753 QQLlrlqAEIGPLN-------KELNEHLIHIKE 1778
Cdd:TIGR02168  979 NKI----KELGPVNlaaieeyEELKERYDFLTA 1007
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1227-1778 3.62e-11

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 68.12  E-value: 3.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1227 TSEFSELDKKLQHIRNLLQNTSVSLVDIEKldyetqslrdQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSrlV 1306
Cdd:TIGR04523  238 QQEINEKTTEISNTQTQLNQLKDEQNKIKK----------QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK--E 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1307 QQLSKELKEN--GIQLQESNIEGALNltrhayERVSNLSTLKDEANELasNTDRNCKRVENLSNKIQAEA--DDLANNNK 1382
Cdd:TIGR04523  306 QDWNKELKSElkNQEKKLEEIQNQIS------QNNKIISQLNEQISQL--KKELTNSESENSEKQRELEEkqNEIEKLKK 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1383 LIEDYRAELTSLTSQIPELNNQVcgkpgdpcdslcggagcgHCGGFLSCEHGAKTHSEEALKVAKDAE-TAITSKKDQAD 1461
Cdd:TIGR04523  378 ENQSYKQEIKNLESQINDLESKI------------------QNQEKLNQQKDEQIKKLQQEKELLEKEiERLKETIIKNN 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1462 QTIRALTqaklnaSEAYEKaKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTaspsesKELAQKTLDLD-LKLEPE 1540
Cdd:TIGR04523  440 SEIKDLT------NQDSVK-ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ------KELKSKEKELKkLNEEKK 506

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1541 EIETLGDQINRAVSSLKNveaiiyrtkpdldRVNNLqsiaNATKEKADKILDSANSVVESLAAaDESQGKAKDAIQQANS 1620
Cdd:TIGR04523  507 ELEEKVKDLTKKISSLKE-------------KIEKL----ESEKKEKESKISDLEDELNKDDF-ELKKENLEKEIDEKNK 568

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1621 NIELAGQDLEKIDeetysaeapANNTAQQ--VEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSA 1698
Cdd:TIGR04523  569 EIEELKQTQKSLK---------KKQEEKQelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1699 TSATNQTLtdrasrsENARERAKQLlqRASKLTVDTNAK-LKDLNDLQTVYLNK--NQQLLRLQAEIGPLNK-----ELN 1770
Cdd:TIGR04523  640 KNKLKQEV-------KQIKETIKEI--RNKWPEIIKKIKeSKTKIDDIIELMKDwlKELSLHYKKYITRMIRikdlpKLE 710


                   ....*...
gi 24582614   1771 EHLIHIKE 1778
Cdd:TIGR04523  711 EKYKEIEK 718
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1043-1091 5.56e-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: 59.29  E-value: 5.56e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614   1043 CECDFLGTNNtiAHCDRFTGQCPCLPNVQGVRCDQCAENHW--KIASGEGC 1091
Cdd:pfam00053    1 CDCNPHGSLS--DTCDPETGQCLCKPGVTGRHCDRCKPGYYglPSDPPQGC 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1226-1695 1.12e-10

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 66.58  E-value: 1.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1226 YTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQashgRLSETEQNLDDIYNSLSLSGVELES-LQNHSR 1304
Cdd:TIGR04523  178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS----ELKKQNNQLKDNIEKKQQEINEKTTeISNTQT 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1305 LVQQLSKELKENGIQLQESNIEgaLNLTRHAYERVSN-LSTLKDEANEL----ASNTDRNCK-RVENLSNKIQAEADDLA 1378
Cdd:TIGR04523  254 QLNQLKDEQNKIKKQLSEKQKE--LEQNNKKIKELEKqLNQLKSEISDLnnqkEQDWNKELKsELKNQEKKLEEIQNQIS 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1379 NNNKLI-------EDYRAELTSLTSQIPELNNQVCGKpgdpcdslcggagcGHCGGFLSCEHGAKTHSEEALKVAK-DAE 1450
Cdd:TIGR04523  332 QNNKIIsqlneqiSQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQInDLE 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1451 TAITSKKDQA---DQTIRALTQAKLNASEAYE--KAKRGFEQSE-RYLNQTNANIKLA------------ENLFIALNNF 1512
Cdd:TIGR04523  398 SKIQNQEKLNqqkDEQIKKLQQEKELLEKEIErlKETIIKNNSEiKDLTNQDSVKELIiknldntresleTQLKVLSRSI 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1513 QENKTASPSESKELAQKTLDLD-LKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDR--------VNNLQSiaNAT 1583
Cdd:TIGR04523  478 NKIKQNLEQKQKELKSKEKELKkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdledeLNKDDF--ELK 555

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1584 KEKADKILDSANSVVESL----AAADESQGKAKDAIQQANSNIelagQDL-EKIDEETYSAEapanNTAQQVEKLAKKVQ 1658
Cdd:TIGR04523  556 KENLEKEIDEKNKEIEELkqtqKSLKKKQEEKQELIDQKEKEK----KDLiKEIEEKEKKIS----SLEKELEKAKKENE 627

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 24582614   1659 KLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNL 1695
Cdd:TIGR04523  628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1043-1091 6.44e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.17  E-value: 6.44e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24582614    1043 CECDFLGTNNTiaHCDRFTGQCPCLPNVQGVRCDQCAENHWKiASGEGC 1091
Cdd:smart00180    1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1043-1092 1.24e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.44  E-value: 1.24e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24582614 1043 CECDFLGTNNTiaHCDRFTGQCPCLPNVQGVRCDQCAENHWKIAS-GEGCE 1092
Cdd:cd00055    2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
529-567 1.70e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.01  E-value: 1.70e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 24582614     529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1526-1763 1.85e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1526 LAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDL----DRVNNLQSIANATKEKADKILDSANSVVESL 1601
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELeeleLELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1602 AAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAgsv 1681
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--- 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1682 kLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAE 1761
Cdd:COG1196  389 -LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                 ..
gi 24582614 1762 IG 1763
Cdd:COG1196  468 LL 469
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1232-1677 2.22e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 62.35  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1232 ELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQashgRLSETEQNLDDiynslslsgvELESLQNHSRLVQQLSK 1311
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ----NQEKLNQQKDE----------QIKKLQQEKELLEKEIE 429

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1312 ELKENGIQlQESNIEgalNLTRHAYErvsnlstLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAEL 1391
Cdd:TIGR04523  430 RLKETIIK-NNSEIK---DLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1392 TSLTSQIPELNNQVcgkpgdpcdslcggagcghcgGFLSCEHGAKTHSEEALKVAK-DAETAITSKKDQADQTIRALTQA 1470
Cdd:TIGR04523  499 KKLNEEKKELEEKV---------------------KDLTKKISSLKEKIEKLESEKkEKESKISDLEDELNKDDFELKKE 557

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1471 KLnaseayEKAKRGFEQSERYLNQTNANIKlaenlfiaLNNFQENKTAspsesKELAQKTLDLDLKLEPEE--IETLGDQ 1548
Cdd:TIGR04523  558 NL------EKEIDEKNKEIEELKQTQKSLK--------KKQEEKQELI-----DQKEKEKKDLIKEIEEKEkkISSLEKE 618

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1549 INRAVSSLKNVEAIIyrtkpdldrvNNLQSIANATKEKADKILDSANSVVESLAAADEsqgKAKDAIQQANSNIELAGQD 1628
Cdd:TIGR04523  619 LEKAKKENEKLSSII----------KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK---KIKESKTKIDDIIELMKDW 685

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614   1629 LEK--IDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKE 1677
Cdd:TIGR04523  686 LKElsLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKN 736
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 477-526 2.51e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 54.67  E-value: 2.51e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24582614  477 PCTCNPLGTLNNSgCVMRTGECKCKKYVTGKDCNQCMPETYGLSESPEGC 526
Cdd:cd00055    1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1205-1678 2.68e-09

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: 62.38  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1205 DATTATIL-RAKEIKQVGAT-GAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNL 1282
Cdd:TIGR02168  666 AKTNSSILeRRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1283 DDIYNSLSLSGVEL--ESLQNHSRL--VQQLSKELKENGIQLQES--NIEGALNLTRHAYERVSN-LSTLKDEANELAS- 1354
Cdd:TIGR02168  746 EERIAQLSKELTELeaEIEELEERLeeAEEELAEAEAEIEELEAQieQLKEELKALREALDELRAeLTLLNEEAANLREr 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1355 ------NTDRNCKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQvcgkpgdpcdslcggagcghcggf 1428
Cdd:TIGR02168  826 leslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE------------------------ 881

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1429 lscehgaKTHSEEALKVAKDAetaitskKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIklaenlfia 1508
Cdd:TIGR02168  882 -------RASLEEALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI--------- 938

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1509 lNNFQENKTaspseskELAQKTLDLDLKLEPEeIETLGDQINRAVSSLKNveAIIYrtkpdLDRVNnlqsianatkekad 1588
Cdd:TIGR02168  939 -DNLQERLS-------EEYSLTLEEAEALENK-IEDDEEEARRRLKRLEN--KIKE-----LGPVN-------------- 988

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1589 kildsansvvesLAAADEsqgkakdaiqqansnielagqdLEKIdEETYsaeapaNNTAQQVEKLAKKVQKLQNNIMKND 1668
Cdd:TIGR02168  989 ------------LAAIEE----------------------YEEL-KERY------DFLTAQKEDLTEAKETLEEAIEEID 1027

                          490
                   ....*....|
gi 24582614   1669 RDAKEITKEA 1678
Cdd:TIGR02168 1028 REARERFKDT 1037
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1570-1779 2.73e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 61.07  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1570 LDRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQ 1649
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1650 VEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLtdRASRSENARERAKQLLQRASK 1729
Cdd:COG4372  117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEANR 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24582614 1730 lTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIKER 1779
Cdd:COG4372  195 -NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 529-567 3.79e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.90  E-value: 3.79e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 24582614  529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 417-476 3.86e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.90  E-value: 3.86e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  417 PCDCDPQGSSDdGICDSLNeleegavaGACHCKAFVTGRRCNQCKDGYWNLQSdNPEGCE 476
Cdd:cd00055    1 PCDCNGHGSLS-GQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1200-1773 6.04e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 6.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1200 LSALE-DATTAtiLRAKEIKQvgatgaytsEFSELDKKLQ--HIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLS 1276
Cdd:COG1196  202 LEPLErQAEKA--ERYRELKE---------ELKELEAELLllKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1277 ETEQNLDDI-------YNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLSTLKDEA 1349
Cdd:COG1196  271 ELRLELEELeleleeaQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1350 NELASNTDRNCKRVENLSNKIQAEADDLAnnnKLIEDYRAELTSLTSQIPELNNQvcgkpgdpcdslcggagcghcggfl 1429
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEE---ELEELAEELLEALRAAAELAAQL------------------------- 402

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1430 scehgakTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRgfEQSERYLNQTNANIKLAENLFIAL 1509
Cdd:COG1196  403 -------EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE--EEAELEEEEEALLELLAELLEEAA 473

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1510 NNFQENKTASPSESKELAQKTLDLDLKLEPE---------EIETLGDQINRAVSSLKNVEAiIYRTKPDLDRVNNLQSIA 1580
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkaaLLLAGLRGLAGAVAVLIGVEA-AYEAALEAALAAALQNIV 552

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1581 NATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAP---ANNTAQQVEKLAKKV 1657
Cdd:COG1196  553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvLGDTLLGRTLVAARL 632

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1658 QKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAK 1737
Cdd:COG1196  633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712

                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 24582614 1738 LKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHL 1773
Cdd:COG1196  713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1228-1623 6.15e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 59.92  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1228 SEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNslslsgvELESLQNhsrLVQ 1307
Cdd:COG4372   14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-------ELEQLEE---ELE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1308 QLSKELKENGIQLQESNiegalnltrhayervSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDY 1387
Cdd:COG4372   84 ELNEQLQAAQAELAQAQ---------------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1388 RAELTSLTSQIPELNNQVcgkpgdpcDSLCGGAGCGhcggflscehgAKTHSEEALK-VAKDAETAITSKKDQADQtIRA 1466
Cdd:COG4372  149 EEELKELEEQLESLQEEL--------AALEQELQAL-----------SEAEAEQALDeLLKEANRNAEKEEELAEA-EKL 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1467 LTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAqktlDLDLKLEPEEIETLG 1546
Cdd:COG4372  209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV----EKDTEEEELEIAALE 284

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614 1547 DQINRAVSSLKNVEAIIYRTKPdLDRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIE 1623
Cdd:COG4372  285 LEALEEAALELKLLALLLNLAA-LSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 478-526 6.15e-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: 53.51  E-value: 6.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 24582614    478 CTCNPLGTLNnSGCVMRTGECKCKKYVTGKDCNQCMPETYGL-SESPEGC 526
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
418-475 1.31e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.31e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 24582614     418 CDCDPQGSSDDGiCDSLNeleegavaGACHCKAFVTGRRCNQCKDGYWNlqsDNPEGC 475
Cdd:smart00180    1 CDCDPGGSASGT-CDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1142-1190 1.72e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.97  E-value: 1.72e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24582614   1142 CECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGqFPHCSPCG 1190
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQG 48
growth_prot_Scy NF041483
polarized growth protein Scy;
1434-1727 1.82e-08

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 59.84  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1434 GAKTHSEEALKVA-KDAETAITSKKDQADQT------IRALT-----QAKLNASEAYEKAKRGFEQSERYLNQTNANikl 1501
Cdd:NF041483  204 SARAEAEAILRRArKDAERLLNAASTQAQEAtdhaeqLRSSTaaesdQARRQAAELSRAAEQRMQEAEEALREARAE--- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1502 AENLFialnnfqenktaspSESKELAQKTLDLDLKLEPEEIETLGDQINRAVS-SLKNVEAiiyrTKPDLDrvnnlQSIA 1580
Cdd:NF041483  281 AEKVV--------------AEAKEAAAKQLASAESANEQRTRTAKEEIARLVGeATKEAEA----LKAEAE-----QALA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1581 NATKEkADKILDSANSVVESLAAADESQGKAK----------DAIQQANSNIELAGQDLEKIDEEtysAEAPANNTAQQV 1650
Cdd:NF041483  338 DARAE-AEKLVAEAAEKARTVAAEDTAAQLAKaartaeevltKASEDAKATTRAAAEEAERIRRE---AEAEADRLRGEA 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1651 EKLAKKVQKlqnnimkndrDAKEITKE--AGSVKL--EAMRARGEANNLQSATSATNQTLTDRASRS-----ENARERAK 1721
Cdd:NF041483  414 ADQAEQLKG----------AAKDDTKEyrAKTVELqeEARRLRGEAEQLRAEAVAEGERIRGEARREavqqiEEAARTAE 483


                  ....*.
gi 24582614  1722 QLLQRA 1727
Cdd:NF041483  484 ELLTKA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1274-1720 2.32e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1274 RLSETEQNL---DDI--------------------YNSLS---------LSGVELESLQNHSRLVQQLSKELKE--NGIQ 1319
Cdd:COG1196  180 KLEATEENLerlEDIlgelerqleplerqaekaerYRELKeelkeleaeLLLLKLRELEAELEELEAELEELEAelEELE 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1320 LQESNIEGALNLTRHAYERVSNLSTLKDEANELASntdrncKRVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIP 1399
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELL------AELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1400 ELNNQvcgkpgdpcdslcggagcghcggflscEHGAKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYE 1479
Cdd:COG1196  334 ELEEE---------------------------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1480 KAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQKTLDLDLKLEpEEIETLGDQINRAVSSLKNV 1559
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELL 465

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1560 EAIIYRTKpdldRVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQAnsNIELAGQDLEKiDEETYSA 1639
Cdd:COG1196  466 AELLEEAA----LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIG-VEAAYEA 538

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1640 EAPANNTAQqveklakkvqkLQNNIMKNDRDAKEItkeagsVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARER 1719
Cdd:COG1196  539 ALEAALAAA-----------LQNIVVEDDEVAAAA------IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601


                 .
gi 24582614 1720 A 1720
Cdd:COG1196  602 D 602
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1141-1189 3.33e-08

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 51.20  E-value: 3.33e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24582614 1141 PCECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIGQFPHCSPC 1189
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1438-1713 3.58e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 57.53  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1438 HSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAEnlfialnnfqenkt 1517
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE-------------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1518 aspsesKELAQKTldldlklepeeiETLGDQIN---RAVSSLKNVEAIIYRTKPD--LDRVNNLQSIANATKEkadkILD 1592
Cdd:COG3883   79 ------AEIEERR------------EELGERARalyRSGGSVSYLDVLLGSESFSdfLDRLSALSKIADADAD----LLE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1593 SANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEEtysAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAK 1672
Cdd:COG3883  137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE---QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 24582614 1673 EITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRS 1713
Cdd:COG3883  214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 883-930 4.62e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 50.81  E-value: 4.62e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24582614    883 CQCNGHAA---TCDPIQGTCiDCQDSTTGYSCDSCLDGYYGNPlFGSEIGC 930
Cdd:pfam00053    1 CDCNPHGSlsdTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1528-1756 5.41e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.13  E-value: 5.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1528 QKTLDLDLKLEPEEIET--LGDQINRAVSSLKNVEAIIyrtkpdlDRVNNLQSIANATKEKADKILDSANSVVESL---- 1601
Cdd:PRK02224  185 QRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLEEHEERREELetle 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1602 AAADESQGK----------AKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDA 1671
Cdd:PRK02224  258 AEIEDLRETiaeterereeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1672 KEITKEAGSV-----KLE--AMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVD----------- 1733
Cdd:PRK02224  338 QAHNEEAESLredadDLEerAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgnaedfleel 417

                         250       260       270
                  ....*....|....*....|....*....|..
gi 24582614  1734 ------TNAKLKDLN-DLQTV--YLNKNQQLL 1756
Cdd:PRK02224  418 reerdeLREREAELEaTLRTAreRVEEAEALL 449
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1228-1484 7.07e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 56.07  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1228 SEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQashgrlseTEqnlddiynSLSLsgvELESlqnhsRLVQ 1307
Cdd:COG1340   85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ--------TE--------VLSP---EEEK-----ELVE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1308 QLsKELKEngiQLQEsnIEGALNLTRHAYERVSNLSTLKDEANELAsntdrncKRVENLSNKIQAEADDLANNNKLIEDY 1387
Cdd:COG1340  141 KI-KELEK---ELEK--AKKALEKNEKLKELRAELKELRKEAEEIH-------KKIKELAEEAQELHEEMIELYKEADEL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1388 RAELTSLTSQIPELNNQvcgkpgdpcdslcggagcghcggflscehgAKTHSEEALKVAK---DAETAITSKKDQADQTI 1464
Cdd:COG1340  208 RKEADELHKEIVEAQEK------------------------------ADELHEEIIELQKelrELRKELKKLRKKQRALK 257

                        250       260
                 ....*....|....*....|..
gi 24582614 1465 RALTQAKLN--ASEAYEKAKRG 1484
Cdd:COG1340  258 REKEKEELEekAEEIFEKLKKG 279
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1602-1771 7.61e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 56.45  E-value: 7.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1602 AAADESQGKAKDAIQQANSNIELAGQDLEKIDEEtysaeapANNTAQQVEKLAKKVQKLQNNImkndrdaKEITKEAGSV 1681
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREE-------LEQLEEELEQARSELEQLEEEL-------EELNEQLQAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1682 KLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQtvylnknQQLLRLQAE 1761
Cdd:COG4372   93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE-------EQLESLQEE 165

                        170
                 ....*....|
gi 24582614 1762 IGPLNKELNE 1771
Cdd:COG4372  166 LAALEQELQA 175
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1240-1779 1.07e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.97  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1240 IRNLLQNTSVSLVDIEKL--DYETQSLRDQLQASHGRLSETEQNLDDiYNSLSLSGVEL-----ESLQNHSRLVQQLSkE 1312
Cdd:PRK02224  178 VERVLSDQRGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIER-YEEQREQARETrdeadEVLEEHEERREELE-T 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1313 LKENGIQLQESnIEGAL----NLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEDYR 1388
Cdd:PRK02224  256 LEAEIEDLRET-IAETErereELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1389 AELTSLTSQIPELNNQVcgkpgdpcDSLcggagcghcggflscEHGAKTHSEEALKVAKDAETAITSKKDQADQtIRALT 1468
Cdd:PRK02224  335 VAAQAHNEEAESLREDA--------DDL---------------EERAEELREEAAELESELEEAREAVEDRREE-IEELE 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1469 QAKLNASEAYEKAKRGFEQSERYL-----NQTNANIKLAE---NLFIALNNFQENKT-------------------ASPS 1521
Cdd:PRK02224  391 EEIEELRERFGDAPVDLGNAEDFLeelreERDELREREAEleaTLRTARERVEEAEAlleagkcpecgqpvegsphVETI 470

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1522 ESKELAQKTLDLDLKLEPEEIETLGDQINRAvSSLKNVEAIIYRTKPDLDRVNNLQSIANAT-KEKADKILDSANSVVES 1600
Cdd:PRK02224  471 EEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETiEEKRERAEELRERAAEL 549

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1601 LAAADESQGKAKDAIQQANSNIELAG---QDLEKIDEETYSAE------APANNTAQQVEKLAKKVQKLQNnimKND--R 1669
Cdd:PRK02224  550 EAEAEEKREAAAEAEEEAEEAREEVAelnSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAE---LNDerR 626

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1670 DakeitkeagsvKLEAMRARgeannlqsatsatNQTLtdRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTvyl 1749
Cdd:PRK02224  627 E-----------RLAEKRER-------------KREL--EAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERD--- 677

                         570       580       590
                  ....*....|....*....|....*....|
gi 24582614  1750 nknqqllRLQAEIGPLNKELNEhLIHIKER 1779
Cdd:PRK02224  678 -------DLQAEIGAVENELEE-LEELRER 699
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1600-1762 1.49e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.61  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1600 SLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAG 1679
Cdd:COG3883   10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1680 SVKLEAMRARGEANNLQSATSATN-QTLTDRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQLLRL 1758
Cdd:COG3883   90 ERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169


                 ....
gi 24582614 1759 QAEI 1762
Cdd:COG3883  170 KAEL 173
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 883-931 1.73e-07

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 49.27  E-value: 1.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24582614  883 CQCNGHAA---TCDPIQGTCIdCQDSTTGYSCDSCLDGYYGNPLFGSeiGCR 931
Cdd:cd00055    2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG--GCQ 50
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1227-1781 2.28e-07

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.21  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1227 TSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSE-TEQNLDDIYNSLSLSG-----------V 1294
Cdd:TIGR00606  247 LDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDLYHNHQRTVrekerelvdcqR 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1295 ELESLQNHSRLVQQLSKEL--KENGIQLQESNIEgaLNLTRHAYERVSNLSTLKDEANELASNTDRNCKRVENLsnKIQA 1372
Cdd:TIGR00606  327 ELEKLNKERRLLNQEKTELlvEQGRLQLQADRHQ--EHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL--VIER 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1373 EADDLANNNKLIEDYRAELTSLTSQIPELNNQVCGKpgdpcdslcggagcghcggflscehgAKTHSEEALKVAKdaeta 1452
Cdd:TIGR00606  403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGL--------------------------GRTIELKKEILEK----- 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1453 itsKKDQADQTIRALTQAKLNASEAYEKakrgfeqsERYLNQTNANIKLAENlfialNNFQENKTAspsESKELAQKTLD 1532
Cdd:TIGR00606  452 ---KQEELKFVIKELQQLEGSSDRILEL--------DQELRKAERELSKAEK-----NSLTETLKK---EVKSLQNEKAD 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1533 LDLKLEPEEIETlgDQINRAVSSLKNVEAIIyRTKPDLDrvnnlqsianatkEKADKILDSANSVVESLAAADESQGKAK 1612
Cdd:TIGR00606  513 LDRKLRKLDQEM--EQLNHHTTTRTQMEMLT-KDKMDKD-------------EQIRKIKSRHSDELTSLLGYFPNKKQLE 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1613 DAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMkndrdaKEITKEAGSVKLEAMRARGEA 1692
Cdd:TIGR00606  577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF------DVCGSQDEESDLERLKEEIEK 650

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1693 NNLQSATSATNQTLTDR-ASRSENARERAKQLLQRASKltvdTNAKLKDL-NDLQTVYLNKNQQLLRLQAEIGPLNKELN 1770
Cdd:TIGR00606  651 SSKQRAMLAGATAVYSQfITQLTDENQSCCPVCQRVFQ----TEAELQEFiSDLQSKLRLAPDKLKSTESELKKKEKRRD 726

                          570
                   ....*....|.
gi 24582614   1771 EHLIHIKERGS 1781
Cdd:TIGR00606  727 EMLGLAPGRQS 737
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1142-1186 3.64e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.08  E-value: 3.64e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 24582614    1142 CECDQFGAADFQCDRETGNCVCHEGIGGYKCNECARGYIG-QFPHC 1186
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
478-526 3.74e-07

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 48.08  E-value: 3.74e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 24582614     478 CTCNPLGTLNNSgCVMRTGECKCKKYVTGKDCNQCMPETYGlsESPEGC 526
Cdd:smart00180    1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGYYG--DGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 991-1035 4.03e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 4.03e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 24582614    991 CECSNNVDLYDTgnCDRQTGACLkCLYQTTGDHCELCKDGFFGDA 1035
Cdd:pfam00053    1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1599-1769 6.65e-07

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 52.30  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1599 ESLAAADESQGKAKDAIQqansNIELAGQDLEKIDEetysAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEA 1678
Cdd:pfam12795    3 DELEKAKLDEAAKKKLLQ----DLQQALSLLDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1679 -GSVKLEAMRAR-----GEANNLQSATSATNQTLTDRASRSENARER---AKQLLQRASKLTVDTNAKLKDLNDLQTVYL 1749
Cdd:pfam12795   75 lASLSLEELEQRllqtsAQLQELQNQLAQLNSQLIELQTRPERAQQQlseARQRLQQIRNRLNGPAPPGEPLSEAQRWAL 154

                          170       180
                   ....*....|....*....|
gi 24582614   1750 NKNQQLLRLQAEIgpLNKEL 1769
Cdd:pfam12795  155 QAELAALKAQIDM--LEQEL 172
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1599-1778 6.98e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 6.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1599 ESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEA 1678
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1679 GSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLtvdtnakLKDLNDLQTVYLNKNQQllRL 1758
Cdd:COG4372  111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL-------QEELAALEQELQALSEA--EA 181

                        170       180
                 ....*....|....*....|
gi 24582614 1759 QAEIGPLNKELNEHLIHIKE 1778
Cdd:COG4372  182 EQALDELLKEANRNAEKEEE 201
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1254-1730 7.89e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 7.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1254 IEKLDYEtqslRDQLQASHGRLSE-TEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKEngIQLQESNIEGALNLT 1332
Cdd:COG4717   48 LERLEKE----ADELFKPQGRKPElNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE--LEAELEELREELEKL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1333 RHAYERVSNLSTLKDEANELASNTDRnckrVENLSNKIQAeaddlannnklIEDYRAELTSLTSQIPELNNQvcgkpgdp 1412
Cdd:COG4717  122 EKLLQLLPLYQELEALEAELAELPER----LEELEERLEE-----------LRELEEELEELEAELAELQEE-------- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1413 CDSLCGGAGCGHCGGFLSCehgAKTHSE--EALKVAKDAETAITSKKDQADQTIRALtQAKLNASEAYEKAKR------- 1483
Cdd:COG4717  179 LEELLEQLSLATEEELQDL---AEELEElqQRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEarlllli 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1484 ----------GFEQSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQ----------------KTLDLDLKL 1537
Cdd:COG4717  255 aaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAlpaleeleeeeleellAALGLPPDL 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1538 EPEEIETLGDQINRAVSSLKNVEAII--YRTKPDLDRVNNLQSIANATKEKA-DKILDSANSVVESLAAADEsqgkAKDA 1614
Cdd:COG4717  335 SPEELLELLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEE----LEEQ 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1615 IQQANSNIE--LAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNI--MKNDRDAKEITKEAGSVKLEAMRARG 1690
Cdd:COG4717  411 LEELLGELEelLEALDEEELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAE 490

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 24582614 1691 EANNLQSATSATNQTLtDRASRsenarERAKQLLQRASKL 1730
Cdd:COG4717  491 EWAALKLALELLEEAR-EEYRE-----ERLPPVLERASEY 524
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1198-1541 1.02e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1198 LILSALEDATTATILRAKEIKQVGAtgaytSEFSELDKKLQHIRNLLQNTSVSLVDIEKldyETQSLRDQLQASHGRLSE 1277
Cdd:COG4372   13 LSLFGLRPKTGILIAALSEQLRKAL-----FELDKLQEELEQLREELEQAREELEQLEE---ELEQARSELEQLEEELEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1278 TEQNLDDIYNSLSLSGVELESLQNH-SRL---VQQLSKELKEngIQLQESNIEGALN-LTRHAYERVSNLSTLKDEANEL 1352
Cdd:COG4372   85 LNEQLQAAQAELAQAQEELESLQEEaEELqeeLEELQKERQD--LEQQRKQLEAQIAeLQSEIAEREEELKELEEQLESL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1353 ASNTDRNCKRVENLSN-KIQAEADDL---ANNNK-----LIEDYRAELTSLTSQIPELNNQVCGKPGDPCDSLCGGAGCG 1423
Cdd:COG4372  163 QEELAALEQELQALSEaEAEQALDELlkeANRNAekeeeLAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1424 HCGGFLSCEHGAKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAE 1503
Cdd:COG4372  243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 24582614 1504 NLFIALNNFQENKTASPSESKELAQKTLDLDLKLEPEE 1541
Cdd:COG4372  323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1440-1771 1.05e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1440 EEALKVAKDAETAITSKKDQADQtiraLTQAKLNASE--AYEKAKRGFEQSERyLNQTNANIKLAENLfialnnfqENKT 1517
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLER----LRREREKAERyqALLKEKREYEGYEL-LKEKEALERQKEAI--------ERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1518 ASPSESKELAQKTLDlDLKLEPEEIETLGDQINRAVSSLKNVEAIiyRTKPDLDRVN-NLQSIANATKEKADKILDSAns 1596
Cdd:TIGR02169  247 ASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGELEaEIASLERSIAEKERELEDAE-- 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1597 vvESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITK 1676
Cdd:TIGR02169  322 --ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1677 EAGSVKLEAMRARGEANNLQSATSATNQTLTDR-------ASRSENARERAKQLLQRASKLTvdtnaklKDLNDLQTVYL 1749
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEELADLNAAIAGIeakinelEEEKEDKALEIKKQEWKLEQLA-------ADLSKYEQELY 472

                          330       340
                   ....*....|....*....|..
gi 24582614   1750 NKNQQLLRLQAEIGPLNKELNE 1771
Cdd:TIGR02169  473 DLKEEYDRVEKELSKLQRELAE 494
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1228-1606 1.14e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1228 SEFSELDKKLQHIRNLLQNTSVslvDIEKLDYETQSLRDQLQASHGRLSETEqnlddiynslslsgVELESLQNHSRLVQ 1307
Cdd:PRK02224  384 EEIEELEEEIEELRERFGDAPV---DLGNAEDFLEELREERDELREREAELE--------------ATLRTARERVEEAE 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1308 QLSKELK--ENGIQLQESNIEGALNLTRhayERVSNLSTLKDEANELASNTDRNCKRVENLSnKIQAEADDLANN----N 1381
Cdd:PRK02224  447 ALLEAGKcpECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERredlE 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1382 KLIEDYRAELTSLTSQIPELNNQVcgkpgdpcDSLcggagcghcggflscEHGAKTHSEEALKVAKDAETA------ITS 1455
Cdd:PRK02224  523 ELIAERRETIEEKRERAEELRERA--------AEL---------------EAEAEEKREAAAEAEEEAEEAreevaeLNS 579

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1456 KKDQADQTIRALT--QAKLNASEAYEkakrgfEQSERyLNQTNANikLAEnlfiaLNNFQENKTASPSESKElaqktlDL 1533
Cdd:PRK02224  580 KLAELKERIESLEriRTLLAAIADAE------DEIER-LREKREA--LAE-----LNDERRERLAEKRERKR------EL 639

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582614  1534 DLKLEPEEIETLGDQINRAVSSLKNVEaiiyrtkPDLDrvnnlqsianATKEKADKILDSANSVVESLAAADE 1606
Cdd:PRK02224  640 EAEFDEARIEEAREDKERAEEYLEQVE-------EKLD----------ELREERDDLQAEIGAVENELEELEE 695
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1227-1770 1.39e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 53.54  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1227 TSEFSELDKKLQHIRNLLQNTSVSLVDIEKL-DYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVEL-ESLQNHSR 1304
Cdd:COG5022  917 SDLIENLEFKTELIARLKKLLNNIDLEEGPSiEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGnKANSELKN 996

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1305 LVQQLSKELKENGIqLQESniegalnltrhayerVSNLSTLKDEANELASNTDRNCKRVENLSnkIQAEADDLANNNKLi 1384
Cdd:COG5022  997 FKKELAELSKQYGA-LQES---------------TKQLKELPVEVAELQSASKIISSESTELS--ILKPLQKLKGLLLL- 1057

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1385 edyraELTSLTSQIPELNNQvcgKPGDPCDSLCggagcghcggflscehgakthsEEALKVAKDAETAITSKKDQADQTI 1464
Cdd:COG5022 1058 -----ENNQLQARYKALKLR---RENSLLDDKQ----------------------LYQLESTENLLKTINVKDLEVTNRN 1107

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1465 RALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIK-----------LAENLFIALNNFQENKTASP---SESKELAQKT 1530
Cdd:COG5022 1108 LVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEpvfqklsvlqlELDGLFWEANLEALPSPPPFaalSEKRLYQSAL 1187

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1531 LDLDLKLEPEEIETLGDQInravsslknvEAIIYRTKPDLdrvnnlqsianatkEKADKILDSAnsvVESLAAADESQgK 1610
Cdd:COG5022 1188 YDEKSKLSSSEVNDLKNEL----------IALFSKIFSGW--------------PRGDKLKKLI---SEGWVPTEYST-S 1239

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1611 AKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNImkNDRDAKEITKEAGSVKLEamraRG 1690
Cdd:COG5022 1240 LKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI--NVGLFNALRTKASSLRWK----SA 1313

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1691 EANNLqsatsatNQTLTD---RASRSENARERAKQLLQRASKLTVDtnakLKDLNDLQTV----YLNKNQQLLRLQAEIG 1763
Cdd:COG5022 1314 TEVNY-------NSEELDdwcREFEISDVDEELEELIQAVKVLQLL----KDDLNKLDELldacYSLNPAEIQNLKSRYD 1382


                 ....*..
gi 24582614 1764 PLNKELN 1770
Cdd:COG5022 1383 PADKENN 1389
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1485-1774 1.87e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 53.10  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1485 FEQSERYLNQTNANIKLAE----NLFIALNNFQENKTASPSESKELAQKTLDLDLKLEPEEietlgDQINRAVSSLKNVE 1560
Cdd:TIGR04523   35 EKQLEKKLKTIKNELKNKEkelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK-----DKINKLNSDLSKIN 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1561 AIIyrtKPDLDRVNNLQS-IANATKEK--ADKILDSANSVVESLAA-ADESQGKAKDAIQQansnIELAGQDLEKIDEET 1636
Cdd:TIGR04523  110 SEI---KNDKEQKNKLEVeLNKLEKQKkeNKKNIDKFLTEIKKKEKeLEKLNNKYNDLKKQ----KEELENELNLLEKEK 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1637 YSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEIT---KEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRS 1713
Cdd:TIGR04523  183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24582614   1714 ENAReraKQLLQRASKLTvDTNAKLKDLNDlqtvylnknqQLLRLQAEIGPLNKELNEHLI 1774
Cdd:TIGR04523  263 NKIK---KQLSEKQKELE-QNNKKIKELEK----------QLNQLKSEISDLNNQKEQDWN 309
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 1231-1405 1.98e-06

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 51.15  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1231 SELDKKLQhirNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLD-----------DIYNSLSLSgvELEsl 1299
Cdd:pfam12795   12 EAAKKKLL---QDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAalqakaeaapkEILASLSLE--ELE-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1300 qnhSRLVQQLSkELKENGIQLQESNIEgaLNLTRHAYERVSN-LSTLKDEANELASNTDRNCKRVENLS----NKIQAEA 1374
Cdd:pfam12795   85 ---QRLLQTSA-QLQELQNQLAQLNSQ--LIELQTRPERAQQqLSEARQRLQQIRNRLNGPAPPGEPLSeaqrWALQAEL 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 24582614   1375 D-----------DLANNNKLIEDYRAELTSLTSQIPELNNQV 1405
Cdd:pfam12795  159 AalkaqidmleqELLSNNNRQDLLKARRDLLTLRIQRLEQQL 200
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1545-1762 2.18e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.59  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1545 LGDQINRAVSSLKNVEAIIYRTKPDLDRVNnlQSIAN--ATKEKADKILDSANSVVESLaaadesQGKAKDAIQQANSNi 1622
Cdd:COG1842   14 INALLDKAEDPEKMLDQAIRDMEEDLVEAR--QALAQviANQKRLERQLEELEAEAEKW------EEKARLALEKGRED- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1623 eLAGQDLEKI---DEETYSAEAPANNTAQQVEKLAKKVQKLQNNImkndRDAKEitkeagsvKLEAMRARGEAnnlQSAT 1699
Cdd:COG1842   85 -LAREALERKaelEAQAEALEAQLAQLEEQVEKLKEALRQLESKL----EELKA--------KKDTLKARAKA---AKAQ 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582614 1700 SATNQTLTDRASRS-----ENARERAKQLLQRA-------SKLTVDtnAKLKDLNDLQTVylnkNQQLLRLQAEI 1762
Cdd:COG1842  149 EKVNEALSGIDSDDatsalERMEEKIEEMEARAeaaaelaAGDSLD--DELAELEADSEV----EDELAALKAKM 217
PTZ00121 PTZ00121
MAEBL; Provisional
 1435-1761 2.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1435 AKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAEnlfialnnfqE 1514
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE----------D 1403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1515 NKTASPSESKELAQKTLDlDLKLEPEEIETLGDQINRAVSSLKNVEAiiYRTKPDLDRVNNLQSIANaTKEKADKILDSA 1594
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEA--KKKAEEAKKAEEAKKKAE-EAKKADEAKKKA 1479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1595 nsvvESLAAADESQGKAKDAIQQANSnIELAGQDLEKIDEETYSAEAPANNTAQQVEKlAKKVQKLqnnimkndRDAKEI 1674
Cdd:PTZ00121 1480 ----EEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEA--------KKAEEK 1545

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1675 TKEAGSVKLEAMRARGEANNLQSATsatnqtltdRASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNKNQQ 1754
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAK---------KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616


                  ....*..
gi 24582614  1755 LLRLQAE 1761
Cdd:PTZ00121 1617 EAKIKAE 1623
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1212-1773 3.64e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1212 LRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDI------ 1285
Cdd:PRK03918  212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkek 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1286 ---YNSLS---------LSGVE--LESLQNHSRLVQQLSKELKENGIQLQEsnIEGALNLTRHAYERVSNLSTLKDEANE 1351
Cdd:PRK03918  292 aeeYIKLSefyeeyldeLREIEkrLSRLEEEINGIEERIKELEEKEERLEE--LKKKLKELEKRLEELEERHELYEEAKA 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1352 LASNTDRNCKRVENLS-NKIQAEADDLANNNKLIEDYRAELT----SLTSQIPELNNQ------------VCGKPgdpcd 1414
Cdd:PRK03918  370 KKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITarigELKKEIKELKKAieelkkakgkcpVCGRE----- 444

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1415 slcggagcghcggfLSCEHGAKTHSEEALKVAKdaetaITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYlnq 1494
Cdd:PRK03918  445 --------------LTEEHRKELLEEYTAELKR-----IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA--- 502

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1495 tnaniKLAENLFIALNNFQENKTaspSESKELAQKTLDLDLKLEpEEIETLGDQINRAvSSLKNVEAIIYRTKPDLDRvn 1574
Cdd:PRK03918  503 -----EQLKELEEKLKKYNLEEL---EKKAEEYEKLKEKLIKLK-GEIKSLKKELEKL-EELKKKLAELEKKLDELEE-- 570

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1575 NLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQansnIELAGQDLEKIDEETYSAEAPANNTAQQVEKLA 1654
Cdd:PRK03918  571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE----LEREEKELKKLEEELDKAFEELAETEKRLEELR 646

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1655 KKVQKLQNNImkNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDRASRSENARERAKQL--LQRASKLTV 1732
Cdd:PRK03918  647 KELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekLEKALERVE 724

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 24582614  1733 DTNAKLKDLndlqtvylnKNQQLLRLQAEIGPLNKELNEHL 1773
Cdd:PRK03918  725 ELREKVKKY---------KALLKERALSKVGEIASEIFEEL 756
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1212-1689 4.05e-06

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 51.50  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1212 LRAKEIKQVGATGAYTSEFSELDKKLQHIR----------NLLQNTSVSLVDI----EKLDYETQSLRDQlqashgRLSE 1277
Cdd:COG5185   84 KARKFLKEKKLDTKILQEYVNSLIKLPNYEwsadilisllYLYKSEIVALKDElikvEKLDEIADIEASY------GEVE 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1278 TEQNLDDIY---NSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGALnltrhayERVSNLSTLKDEANELAS 1354
Cdd:COG5185  158 TGIIKDIFGkltQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESET-------GNLGSESTLLEKAKEIIN 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1355 --NTDRNCKRVENLSNKIQAEADDLANNNKLIEDYR----AELTSLTSQIPELNNQVCGKPGDPCDSLCGGAGCGHCGgf 1428
Cdd:COG5185  231 ieEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRleklGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIK-- 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1429 lscehgAKTHSEEALKVAKDAETAITSKKDQADQTIRALT----QAKLNASEAYEKAK---------RGFEQSERYLNQT 1495
Cdd:COG5185  309 ------KATESLEEQLAAAEAEQELEESKRETETGIQNLTaeieQGQESLTENLEAIKeeienivgeVELSKSSEELDSF 382

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1496 NANIklaENLFIALnnfqENKTASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSL-----KNVEAIIYRTKPDL 1570
Cdd:COG5185  383 KDTI---ESTKESL----DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNeevskLLNELISELNKVMR 455

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1571 DRVNNLQS--------IANATKEKADKILDSANSVVESLAAADESQGKAKDAI-QQANSNIELAGQDLEKIDE---ETYS 1638
Cdd:COG5185  456 EADEESQSrleeaydeINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLeRQLEGVRSKLDQVAESLKDfmrARGY 535

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24582614 1639 AEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAGSVKLEAMRAR 1689
Cdd:COG5185  536 AHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAR 586
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1546-1777 4.57e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 4.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1546 GDQINRAVSSlKNVEAIIYRTKPDLDrVNNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELA 1625
Cdd:COG4372    1 GDRLGEKVGK-ARLSLFGLRPKTGIL-IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1626 GQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNImkndrdaKEITKEAGSVKLEAMRARGEANNLQSATSATNQT 1705
Cdd:COG4372   79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582614 1706 LTDRASRSENARERAKQLLQRASKLTVD-TNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLIHIK 1777
Cdd:COG4372  152 LKELEEQLESLQEELAALEQELQALSEAeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 991-1041 4.71e-06

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 45.42  E-value: 4.71e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24582614  991 CECSNNVDLydTGNCDRQTGACLkCLYQTTGDHCELCKDGFFGDALQ-QNCQ 1041
Cdd:cd00055    2 CDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 529-567 5.54e-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: 45.04  E-value: 5.54e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24582614    529 CNCDAGGSYDNYCDVISGQCRCRPHMTGRSCSQPKQNYF 567
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1550-1783 5.70e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1550 NRAVS--SLKNVEAIIY-------RTKPDLDRV-------NNLQSIANATKEKADkILDSANSVVESLAAADESQGKAKD 1613
Cdd:COG4913  198 HKTQSfkPIGDLDDFVReymleepDTFEAADALvehfddlERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEY 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1614 AIQQANS-----NIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKE-ITKEAGSVKLEAMR 1687
Cdd:COG4913  277 LRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEE 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1688 ARGEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASkltvdtnAKLKDLNDLQTvylNKNQQLLRLQAEIGPLNK 1767
Cdd:COG4913  357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE-------EELEALEEALA---EAEAALRDLRRELRELEA 426

                        250
                 ....*....|....*.
gi 24582614 1768 ELNEhlihIKERGSHY 1783
Cdd:COG4913  427 EIAS----LERRKSNI 438
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1600-1771 7.26e-06

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: 50.53  E-value: 7.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1600 SLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKEAG 1679
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1680 SV--KLEAMRAR-----------GEANNLQSATSATNqtltdrASRSENARERAKQLLQRASKLTVDTNAKLKDLNDLQT 1746
Cdd:COG4942   94 ELraELEAQKEElaellralyrlGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167

                        170       180
                 ....*....|....*....|....*
gi 24582614 1747 VYLNKNQQLLRLQAEIGPLNKELNE 1771
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEA 192
ApoLp-III_like cd13769
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ...
 1545-1702 1.34e-05

Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.


Pssm-ID: 259842 [Multi-domain]  Cd Length: 158  Bit Score: 46.93  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1545 LGDQINRAVSSLKNVEAIIYRTKPDldrvNNLQSIANATKEKADKILDSANSVVESLA-AADESQGKAKDAIQQANSNIE 1623
Cdd:cd13769    3 LSELIQKAQEAINNLAQQVQKQLGL----QNPEEVVNTLKEQSDNFANNLQEVSSSLKeEAKKKQGEVEEAWNEFKTKLS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1624 LAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKE----ITKEAGSVKLEAmrargeANNLQ-SA 1698
Cdd:cd13769   79 ETVPELRKSLPVEEKAQELQAKLQSGLQTLVTESQKLAKAISENSQKAQEelqkATKQAYDIAVEA------AQNLQnQL 152


                 ....
gi 24582614 1699 TSAT 1702
Cdd:cd13769  153 QTAT 156
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 287-343 2.62e-05

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 43.11  E-value: 2.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614  287 SCSCYGHASQCLPLDPafsqadnedgmVHGRCECTHNTKGMNCEECEDFFNDLPWKP 343
Cdd:cd00055    1 PCDCNGHGSLSGQCDP-----------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1212-1402 4.63e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.36  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1212 LRAKEIKQVGATGAYTS-EFSELDKKLQHIRNLlqNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDI--YNS 1288
Cdd:PRK01156  541 LKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNA--LAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDksYID 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1289 LSLSGVEleslqNHSRLVQQLSKELKENGIQLQEsnIEGALnltRHAYERVSNLSTLKDEANELASNTDRNCKRVENLSN 1368
Cdd:PRK01156  619 KSIREIE-----NEANNLNNKYNEIQENKILIEK--LRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRK 688

                         170       180       190
                  ....*....|....*....|....*....|....
gi 24582614  1369 KIQAEADDLANNNKLIEDYRAELTSLTSQIPELN 1402
Cdd:PRK01156  689 ALDDAKANRARLESTIEILRTRINELSDRINDIN 722
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1198-1721 5.08e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 48.30  E-value: 5.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1198 LILSALEDATTATILRAKEIKQVGATG--AYTSEFSELDKKLQHIRNLL-QNTSVSLVDIEKLDYETQSLRDQ----LQA 1270
Cdd:pfam12128  258 LRLSHLHFGYKSDETLIASRQEERQETsaELNQLLRTLDDQWKEKRDELnGELSAADAAVAKDRSELEALEDQhgafLDA 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1271 SHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENGIQLQESNIEGaLNltrhayERVSNLSTLKDEAN 1350
Cdd:pfam12128  338 DIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAG-IK------DKLAKIREARDRQL 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1351 ELASNTdrnckrVENLSNKIQAEADDlANNNKLIEDYRaeltsLTSQIPELNNQVcgkpgdpcdslcggagcghcggfls 1430
Cdd:pfam12128  411 AVAEDD------LQALESELREQLEA-GKLEFNEEEYR-----LKSRLGELKLRL------------------------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1431 cehGAKTHSEEAL--KVAKDAET-AITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQ-TNANIKLAENLF 1506
Cdd:pfam12128  454 ---NQATATPELLlqLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEErQSALDELELQLF 530

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1507 IA---LNNFQENKTASPSES-KELAQKTLDLDLKLEPEEIETLGDQinravsslknvEAIIYRTKPDLDRVNNLQSIA-- 1580
Cdd:pfam12128  531 PQagtLLHFLRKEAPDWEQSiGKVISPELLHRTDLDPEVWDGSVGG-----------ELNLYGVKLDLKRIDVPEWAAse 599

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1581 NATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLE------------------KIDEETYSAEAP 1642
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKnarldlrrlfdekqsekdKKNKALAERKDS 679

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1643 ANNTAQQVEKLAKKV-QKLQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQSATSATNQTLTDR---ASRSENARE 1718
Cdd:pfam12128  680 ANERLNSLEAQLKQLdKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAelkALETWYKRD 759


                   ...
gi 24582614   1719 RAK 1721
Cdd:pfam12128  760 LAS 762
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 933-988 5.46e-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: 42.34  E-value: 5.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614    933 CRCPETVASGlahaDGCSLDTrnnnMLCHCQEGYSGSRCEICADNFFGNP-DNGGTC 988
Cdd:pfam00053    1 CDCNPHGSLS----DTCDPET----GQCLCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 1446-1663 5.96e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 46.98  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1446 AKDAETAITSKKDQADQTIRALTQAklNASEAYEKAKRGF-EQSERYLNQTNANIKLAENLFIALNNFqENKTASPSESK 1524
Cdd:cd22656   82 AQNAGGTIDSYYAEILELIDDLADA--TDDEELEEAKKTIkALLDDLLKEAKKYQDKAAKVVDKLTDF-ENQTEKDQTAL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1525 ELAQKTLDLDL-----KLEPEEIETLGDQINravsslKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKILDSANSVVE 1599
Cdd:cd22656  159 ETLEKALKDLLtdeggAIARKEIKDLQKELE------KLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADT 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24582614 1600 SLAAADESQGKAKDAIQqansNIELA----GQDLEKI------DEETYSAEAPANNTAQQVE----KLAKKVQKLQNN 1663
Cdd:cd22656  233 DLDNLLALIGPAIPALE----KLQGAwqaiATDLDSLkdlledDISKIPAAILAKLELEKAIekwnELAEKADKFRQN 306
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 1438-1662 7.54e-05

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


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 46.51  E-value: 7.54e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1438 HSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERyLNQTNANIK-LAE--NLfIALNnfqe 1514
Cdd:smart00283   40 NADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEELEESSDE-IGEIVSVIDdIADqtNL-LALN---- 113

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1515 nktAS----------------PSESKELAQKTLDldlklEPEEIETLgdqINRAVSSLKNVEAIIYRTKpdlDRVNNLQS 1578
Cdd:smart00283  114 ---AAieaarageagrgfavvADEVRKLAERSAE-----SAKEIESL---IKEIQEETNEAVAAMEESS---SEVEEGVE 179

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1579 IANATKEKADKILDSANSV---VESLAAADESQgkaKDAIQQANSNIElagqDLEKIDEETysaEAPANNTAQQVEKLAK 1655
Cdd:smart00283  180 LVEETGDALEEIVDSVEEIadlVQEIAAATDEQ---AAGSEEVNAAID----EIAQVTQET---AAMSEEISAAAEELSG 249


                    ....*..
gi 24582614    1656 KVQKLQN 1662
Cdd:smart00283  250 LAEELDE 256
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1574-1771 8.14e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 8.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1574 NNLQSIANATKEKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKL 1653
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1654 AKKVQKLQNN----IMKNDRDAKEITKEAGSVK--LEAMRARGEAnnLQsatsATNQTLTDRASRSENARERAKQLLQRA 1727
Cdd:COG4942  110 LRALYRLGRQpplaLLLSPEDFLDAVRRLQYLKylAPARREQAEE--LR----ADLAELAALRAELEAERAELEALLAEL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24582614 1728 S----KLTVDTNAKLKDLNDLQTVYLNKNQQLLRLQAEIGPLNKELNE 1771
Cdd:COG4942  184 EeeraALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
PTZ00121 PTZ00121
MAEBL; Provisional
 1435-1739 9.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1435 AKTHSEEALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAyEKAKRGFEQSErylnqtnanIKLAENLFIAlnnfQE 1514
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEE---------KKKADEAKKA----EE 1300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1515 NKTASPSESKELAQKTLDlDLKLEPEEIETLGDQI-NRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEK---ADKI 1590
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAkKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeAKKK 1379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1591 LDSANSVVESLAAADESQGKAKDAIQQANSnIELAGQDLEKIDEETYSAEapannTAQQVEKLAKKVQKlqnnimknDRD 1670
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEE--------AKK 1445

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582614  1671 AKEITKEAGSVKlEAMRARGEANNLQSATSATNQtlTDRASRSENARERAKQLLQRASKLTVDTNAKLK 1739
Cdd:PTZ00121 1446 ADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 355-415 9.84e-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: 41.57  E-value: 9.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582614    355 CECNDHAV---SCHFdeavftasgfvSGGVCDnCLHNTRGQHCEECMPYFYRDPeqdITSERVC 415
Cdd:pfam00053    1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1362-1777 9.96e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 9.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1362 RVENLSNKIQAEADDLANNNKLIEDYRAELTSLTSQIPELNNQVcgkpgdpcdslcggagcghcggflscehgakthsEE 1441
Cdd:TIGR04523   34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKI----------------------------------KI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1442 ALKVAKDAETAITSKKDQADQTIRALT----------QAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNN 1511
Cdd:TIGR04523   80 LEQQIKDLNDKLKKNKDKINKLNSDLSkinseikndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1512 fQENKTASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIANATKEKADKIL 1591
Cdd:TIGR04523  160 -KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1592 DSANSVVESLaaaDESQGKAKDAIQQANSNIElagQDLEKIDEetysaeapANNTAQQVEKLAKKVQKLQNNI--MKNDR 1669
Cdd:TIGR04523  239 QEINEKTTEI---SNTQTQLNQLKDEQNKIKK---QLSEKQKE--------LEQNNKKIKELEKQLNQLKSEIsdLNNQK 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1670 DAkEITKEagsVKLEAMRARGEANNLQSATSATNQTLTdrasrsenarerakQLLQRASKLTvdtnaklKDLNDLQTVYL 1749
Cdd:TIGR04523  305 EQ-DWNKE---LKSELKNQEKKLEEIQNQISQNNKIIS--------------QLNEQISQLK-------KELTNSESENS 359

                          410       420
                   ....*....|....*....|....*...
gi 24582614   1750 NKNQQLLRLQAEIGPLNKELNEHLIHIK 1777
Cdd:TIGR04523  360 EKQRELEEKQNEIEKLKKENQSYKQEIK 387
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 1233-1394 1.02e-04

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


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 45.87  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1233 LDKKLQHIRNLLQNTSVSLVDIEK----LDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESL-QNHSRLVQ 1307
Cdd:pfam06008   24 LTKQLQEYLSPENAHKIQIEILEKelssLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLiDNIKEINE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1308 QLSKeLKENGIQLQESNIEGALNLTRHAYE--RVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANN-NKLI 1384
Cdd:pfam06008  104 KVAT-LGENDFALPSSDLSRMLAEAQRMLGeiRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANAlRDSL 182

                          170
                   ....*....|
gi 24582614   1385 EDYRAELTSL 1394
Cdd:pfam06008  183 AEYEAKLSDL 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1228-1404 1.25e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1228 SEFSELDKKLQHIRNLLQNTsvsLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNhsrLVQ 1307
Cdd:COG3883   16 PQIQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1308 QLSKELKENGIQ-------LQESNIEGALNltrhayeRVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLANN 1380
Cdd:COG3883   90 ERARALYRSGGSvsyldvlLGSESFSDFLD-------RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162

                        170       180
                 ....*....|....*....|....
gi 24582614 1381 NKLIEDYRAELTSLTSQIPELNNQ 1404
Cdd:COG3883  163 KAELEAAKAELEAQQAEQEALLAQ 186
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1228-1405 1.42e-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: 46.30  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1228 SEFSELDKKLQHIRNLLQNTSVSLVDIEKldyETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHsrlVQ 1307
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1308 QLSKELKENGIQLQESNIEGALNL-----------TRHAY------ERVSNLSTLKDEANELASNTDRNCKRVENLSNKI 1370
Cdd:COG4942  101 AQKEELAELLRALYRLGRQPPLALllspedfldavRRLQYlkylapARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 24582614 1371 QAEADDLANNNKLIEDYRAELTSLTSQIPELNNQV 1405
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAEL 215
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 932-988 1.44e-04

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: 41.19  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614  932 PCRCPETVASGlahaDGCSLDTrnnnMLCHCQEGYSGSRCEICADNFFGNPDNGGTC 988
Cdd:cd00055    1 PCDCNGHGSLS----GQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
991-1034 2.21e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.37  E-value: 2.21e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 24582614     991 CECsnNVDLYDTGNCDRQTGACLkCLYQTTGDHCELCKDGFFGD 1034
Cdd:smart00180    1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1204-1405 3.64e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1204 EDATTATILRAKEIKQVGATG----AYTSEFSELDKK-LQHIRNLLQNTSVSLvDIEKLDYETQSLRDQLQASHGRLSET 1278
Cdd:COG3206  116 REAAIERLRKNLTVEPVKGSNvieiSYTSPDPELAAAvANALAEAYLEQNLEL-RREEARKALEFLEEQLPELRKELEEA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1279 EQNLDDI---YNSLSLSGVELESLQNHSRLVQQLSK-ELKENGIQLQESNIEGALNLTRHAYERVSN---LSTLKDEANE 1351
Cdd:COG3206  195 EAALEEFrqkNGLVDLSEEAKLLLQQLSELESQLAEaRAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAE 274

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582614 1352 LASN--------TDRNcKRVENLSNKIQAEADDLANN-NKLIEDYRAELTSLTSQIPELNNQV 1405
Cdd:COG3206  275 LEAElaelsaryTPNH-PDVIALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQL 336
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 355-407 6.73e-04

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: 39.26  E-value: 6.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24582614  355 CECNDHA---VSCHFDeavftasgfvsGGVCDnCLHNTRGQHCEECMPYFYRDPEQ 407
Cdd:cd00055    2 CDCNGHGslsGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
ApoLp-III pfam07464
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ...
 1575-1673 7.85e-04

Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolism. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.


Pssm-ID: 462172 [Multi-domain]  Cd Length: 143  Bit Score: 41.58  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1575 NLQSIANATKEKADKILDSANSVVESLA-AADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAPANNTAQQ-VEK 1652
Cdd:pfam07464   17 SQQEVVETIKENTENLVDQLKQVQKSLQeELKKASGEAEEALKELNTKIVETADKLSEANPEVVQKANELQEKFQSgVQS 96

                           90       100
                   ....*....|....*....|.
gi 24582614   1653 LAKKVQKLQNNIMKNDRDAKE 1673
Cdd:pfam07464   97 LVTESQKLAKSISENSQGATE 117
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1232-1400 7.86e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1232 ELDKKLQHIRNLLqntsvslvdiEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNH--------- 1302
Cdd:COG1579   14 ELDSELDRLEHRL----------KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqlg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1303 ----SRLVQQLSKElkengIQLQESNIEGALNLTRHAYERVSNLSTLKDEANELASntdrncKRVENLSNKIQAEADDLA 1378
Cdd:COG1579   84 nvrnNKEYEALQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELA------ELEAELEEKKAELDEELA 152

                        170       180
                 ....*....|....*....|..
gi 24582614 1379 NNNKLIEDYRAELTSLTSQIPE 1400
Cdd:COG1579  153 ELEAELEELEAEREELAAKIPP 174
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1186-1405 8.53e-04

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 43.96  E-value: 8.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1186 CSPCGECFnnwDLILSALEDATtatilRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQ--- 1262
Cdd:COG5059  313 ISPSSNSF---EETINTLKFAS-----RAKSIKNKIQVNSSSDSSREIEEIKFDLSEDRSEIEILVFREQSQLSQSSlsg 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1263 ----------SLRDQLQASHGRLSETEQNLDDIYNSLSLSGVELESLQNHSRLVQQLSKELKENgIQLQESNIEGALNLT 1332
Cdd:COG5059  385 ifaymqslkkETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREE-ELSKKKTKIHKLNKL 463

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24582614 1333 RHayERVSNLSTLKDEANELASNtDRNCKRVENLSNKIQAEadDLANNNKLiEDYRAELTSLTSQIPElnNQV 1405
Cdd:COG5059  464 RH--DLSSLLSSIPEETSDRVES-EKASKLRSSASTKLNLR--SSRSHSKF-RDHLNGSNSSTKELSL--NQV 528
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1221-1632 8.70e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 8.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1221 GATGAYTSEFSELDKKLQHIRNLLQ---NTSVSLVD-IEKLDYETQSLRDQLQASHGRLSETEQNLDDIY-------NSL 1289
Cdd:TIGR00606  660 GATAVYSQFITQLTDENQSCCPVCQrvfQTEAELQEfISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLglapgrqSII 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1290 SLSGVEL----ESLQNHSRLVQQLSKELKENGIQLQESNIEgaLNLTRHAYERVSNLSTLKDEanelasnTDRNCKRVEN 1365
Cdd:TIGR00606  740 DLKEKEIpelrNKLQKVNRDIQRLKNDIEEQETLLGTIMPE--EESAKVCLTDVTIMERFQME-------LKDVERKIAQ 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1366 LSNKIQAEADDLANN--NKLIEDYRAELTSLTSQIpELNNQVCGKPGDPCDSLCggagcghcggflSCEHGAKTHS---E 1440
Cdd:TIGR00606  811 QAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKI-ELNRKLIQDQQEQIQHLK------------SKTNELKSEKlqiG 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1441 EALKVAKDAETAITSKKDQADQTIRALTQAKLNASEAYEKAKRGFEQSERYLNQTNANIKLAENLFIALNNFQENKTASP 1520
Cdd:TIGR00606  878 TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYM 957

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1521 SESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVEAIIYRTKPDLDRVNNLQSIA--NATKEkadKILDSANSVV 1598
Cdd:TIGR00606  958 KDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLqdNLTLR---KRENELKEVE 1034

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 24582614   1599 ESLAAADESQG-----KAKDAIQQANSNIELAGQDLEKI 1632
Cdd:TIGR00606 1035 EELKQHLKEMGqmqvlQMKQEHQKLEENIDLIKRNHVLA 1073
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1199-1403 9.86e-04

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: 44.28  E-value: 9.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1199 ILSALEDATTATILRAKEIKQV--------GATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQA 1270
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELeaqieqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1271 SHGRLSETEQNLDDIYNSLSLSGVE----LESLQNHSRLVQQLSKELKENGIQLQES--NIEGALNLTRHAYERVSN-LS 1343
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEEleseLEALLNERASLEEALALLRSELEELSEElrELESKRSELRRELEELREkLA 925

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582614   1344 TLKDEANELASNTDRNckrVENLSNKIQAEADDLANNNKLIEDY----RAELTSLTSQIPELNN 1403
Cdd:TIGR02168  926 QLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDeeeaRRRLKRLENKIKELGP 986
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1568-1779 1.04e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1568 PDLDRVNNLQSIANatkeKADKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEEtysaeapanntA 1647
Cdd:COG1579    4 EDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-----------I 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1648 QQVEKLAKKVQKLQNNIMKNdRDAKEITKEagsvkLEAMRARgeannlqsatsatNQTLTDRASRSENARERAKQLLQRA 1727
Cdd:COG1579   69 EEVEARIKKYEEQLGNVRNN-KEYEALQKE-----IESLKRR-------------ISDLEDEILELMERIEELEEELAEL 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614 1728 SKLTVDTNAKLKDL-NDLQTVYLNKNQQLLRLQAEIGPLNKELNEHLI----HIKER 1779
Cdd:COG1579  130 EAELAELEAELEEKkAELDEELAELEAELEELEAEREELAAKIPPELLalyeRIRKR 186
PTZ00121 PTZ00121
MAEBL; Provisional
 1439-1722 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1439 SEEALKvAKDAETAITSKKdqADQTIRALTQAKLNASEAYEKAKRgFEQSERYLNQTNAN-IKLAENlfiALNNFQENKT 1517
Cdd:PTZ00121 1172 AEDAKK-AEAARKAEEVRK--AEELRKAEDARKAEAARKAEEERK-AEEARKAEDAKKAEaVKKAEE---AKKDAEEAKK 1244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1518 ASPSESKELAQKTLDLDLKLEPEEIETLGDQINRAVSSLKNVE----AIIYRTKPDLDRVNNLQSIANAtKEKADKILDS 1593
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekkkADEAKKAEEKKKADEAKKKAEE-AKKADEAKKK 1323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1594 ANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAE---APANNTAQQVEKLAKKVQKLQNNIMKNDRD 1670
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24582614  1671 AK--EITKEAGSVKLEAMRARGEANNLQSATSATNQtlTDRASRSENARERAKQ 1722
Cdd:PTZ00121 1404 KKkaDELKKAAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKKAEE 1455
46 PHA02562
endonuclease subunit; Provisional
 1524-1743 1.11e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1524 KELAQ--KTLDLDLKLEPEEIETLGDQINRAvSSLKNVEAIIYRTKPDlDRVNNLQSIANATKEKADKILDsansVVESL 1601
Cdd:PHA02562  177 RELNQqiQTLDMKIDHIQQQIKTYNKNIEEQ-RKKNGENIARKQNKYD-ELVEEAKTIKAEIEELTDELLN----LVMDI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1602 AAADESQGKAKDAIQQANSNIELAgQDLEKIDEEtySAEAPAnnTAQQVEKLAKKVQKLQN---NIMKNDRDAKEITKEA 1678
Cdd:PHA02562  251 EDPSAALNKLNTAAAKIKSKIEQF-QKVIKMYEK--GGVCPT--CTQQISEGPDRITKIKDklkELQHSLEKLDTAIDEL 325

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24582614  1679 GSVKLEAMRARGEANNLQSATSATNQTLtdraSRSENARERAKQLLQRASKLTVDTNAKLKDLND 1743
Cdd:PHA02562  326 EEIMDEFNEQSKKLLELKNKISTNKQSL----ITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1465-1737 1.44e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1465 RALTQAKLNA-SEAY---------EKAKRGFEQSERYLNQTNANIKLAENlfiALNNF-QENKTASPSESKELAQktldl 1533
Cdd:COG3206  147 PELAAAVANAlAEAYleqnlelrrEEARKALEFLEEQLPELRKELEEAEA---ALEEFrQKNGLVDLSEEAKLLL----- 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1534 dlklepEEIETLGDQINRAVSSLKNVEAiiyrtkpdldRVNNLQSIANATKEKADKILDSAnsvveslaaadesqgkakd 1613
Cdd:COG3206  219 ------QQLSELESQLAEARAELAEAEA----------RLAALRAQLGSGPDALPELLQSP------------------- 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1614 AIQQANSNIELAGQDLEKIdEETYSAEAPanntaqQVEKLAKKVQKLQNNI---MKNDRDAKEITKEAGSVKLEAMRAR- 1689
Cdd:COG3206  264 VIQQLRAQLAELEAELAEL-SARYTPNHP------DVIALRAQIAALRAQLqqeAQRILASLEAELEALQAREASLQAQl 336

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 24582614 1690 GEANNLQSATSATNQTLTDRASRSENARERAKQLLQRASKLTVDTNAK 1737
Cdd:COG3206  337 AQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1200-1401 1.52e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1200 LSALEDATTATILRAKEIKQvgatgaytsEFSELDKKLQHIRNLLQNTSvSLVDIEKLDYETQSLRDQLQ---ASHGRLS 1276
Cdd:COG4913  619 LAELEEELAEAEERLEALEA---------ELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELErldASSDDLA 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1277 ETEQNLDDIYNSLSLSGVELESLQ-NHSRL---VQQLSKELKENGIQLQESNIEGALNLTRHAYERVSNLST---LKDEA 1349
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKgEIGRLekeLEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGdavERELR 768

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24582614 1350 NELASNTDRNCKRVENLSNKI-----------QAEADDLANNNKLIEDYRAELTSLTSQ-IPEL 1401
Cdd:COG4913  769 ENLEERIDALRARLNRAEEELeramrafnrewPAETADLDADLESLPEYLALLDRLEEDgLPEY 832
PRK01156 PRK01156
chromosome segregation protein; Provisional
 1226-1410 2.00e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.97  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1226 YTSEFSELDKKLQHIRNLLQNTSVSLVDIEKL-DYETQSLRDQLQASHGRLSETEQNLDDIYNSLS------LSGVELES 1298
Cdd:PRK01156  474 YNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkEYLESEEINKSINEYNKIESARADLEDIKIKINelkdkhDKYEEIKN 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1299 LQNHSRLVQQLSKELKENGIQLQESNIEGALNLTRHAyERVSNLSTLKDEANELASNTDRNCKRVENLSNKIQAEADDLA 1378
Cdd:PRK01156  554 RYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSN-EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN 632

                         170       180       190
                  ....*....|....*....|....*....|..
gi 24582614  1379 NNNKLIEDYRAELTSLTSQIPELNNQVCGKPG 1410
Cdd:PRK01156  633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDS 664
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1441-1733 2.09e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1441 EALKVAKDAETAITSKKDQADQTIRAL--TQAKLNASEAYEKAKRG--FEQSERYLNQTNANIKLAENLfiaLNNFQENK 1516
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELkeKRDELNEELKELAEKRDelNAQVKELREEAQELREKRDEL---NEKVKELK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1517 taspSESKELAQKTLDLDLKLEpeEIETLGDQINRAVSSLKNVEAIIyrtkpdlDRVNNLQSIANATKEKADKIldsans 1596
Cdd:COG1340   78 ----EERDELNEKLNELREELD--ELRKELAELNKAGGSIDKLRKEI-------ERLEWRQQTEVLSPEEEKEL------ 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1597 vVESLAAADESQGKAKDAIQQANSNIELAGQdLEKIDEEtysaeapANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITK 1676
Cdd:COG1340  139 -VEKIKELEKELEKAKKALEKNEKLKELRAE-LKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRK 209

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582614 1677 EAGSVKLEAMRARGEANNLQSATSATNQTLTD----------------RASRSENARERAKQLLQRAS---KLTVD 1733
Cdd:COG1340  210 EADELHKEIVEAQEKADELHEEIIELQKELRElrkelkklrkkqralkREKEKEELEEKAEEIFEKLKkgeKLTTE 285
COG6 smart01087
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ...
 1212-1398 2.20e-03

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.


Pssm-ID: 215018  Cd Length: 598  Bit Score: 42.69  E-value: 2.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1212 LRAK-EIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEK-----------LDYETQSLRDQLQashgRLSETE 1279
Cdd:smart01087    8 LRSDlEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDqlntaknqtqdLISEASELQEELA----LLELKK 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614    1280 QNLDDIYNSLSLSGVELESLQN-----HSRLVQQLSK--ELKEN-GIQLQESNIEGAL--------NLTrHAYERVSNLS 1343
Cdd:smart01087   84 KLLDAFLSKFTLSQDELDVLTSregpiDDEFFQVLDKvqEIHEDcSVLLQNEYQTAGLeimekmnqLLE-RAYERLYRWL 162

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 24582614    1344 TlkdeaNELASNTDRNCKRVENLSNKIQAEADDLANNNKLIEdyraELTSLTSQI 1398
Cdd:smart01087  163 Q-----SELRNLTTDNPEILSLLRQALRRLSERPVLFKYCLD----EFTTARSKS 208
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 1570-1786 2.32e-03

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


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 42.37  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1570 LDRVNNLQSIANAtkekadkILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEEtysaeapANNTAQQ 1649
Cdd:pfam04108    2 LSSAQDLCRWANE-------LLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNE-------LKKDFKQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1650 VEKLAKKVQKLQNNIMKNdrdakeitkeAGSVKLEAMRARGEANnlqsatsatNQTLTDRASRS--ENARERAKQLLQRA 1727
Cdd:pfam04108   68 LLKDLDAALERLEETLDK----------LRNTPVEPALPPGEEK---------QKTLLDFIDEDsvEILRDALKELIDEL 128

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24582614   1728 S----KLTVDTNAKLKDLNDLQTvYLNKNQQLLRLQAEIGPLNKELNEHL----IHIKERGSHYRQC 1786
Cdd:pfam04108  129 QaaqeSLDSDLKRFDDDLRDLQK-ELESLSSPSESISLIPTLLKELESLEeemaSLLESLTNHYDQC 194
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 1229-1387 2.39e-03

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 42.33  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1229 EFSELDKKLQHIRNLLQNTSVSLVDIEKLDYETQSLRDQLQASHGRLSETEQNLDDIYNSL-----SLSGVeLESLQNHS 1303
Cdd:cd08915   71 GLDNIEQSFKELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPSSDEAAKELyekvtKLRGY-LEQASNSD 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1304 RLVQQLSKELKENGIQLQESNIEGALNLTrhayervSNLSTLKDEANELASNTDRNCKRVENL----SNKIQaEADDLAN 1379
Cdd:cd08915  150 NEVLQCYESIDPNLVLLCGGYKELKAFIP-------SPYPALDPEVSEVVSSLRPLLNEVSELekerERFIS-ELEIKSR 221

                        170
                 ....*....|..
gi 24582614 1380 NN----KLIEDY 1387
Cdd:cd08915  222 NNdilpKLITEY 233
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 1467-1677 3.02e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 42.36  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1467 LTQAKLNASEAYekakrgFeqSERYLNQTNANIKLAENLFIALNNFQENKTASPSESKELAQktldldLKLEPEEIETLG 1546
Cdd:pfam13166  265 LPAERKAALEAH------F--DDEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSA------FELDVEDIESEA 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1547 DQINravSSLKNVEAIIYRTKPDLDRVNNLQSIANATkEKADKILDSANSVV----ESLAAADESQGKAKDA-----IQQ 1617
Cdd:pfam13166  331 EVLN---SQLDGLRRALEAKRKDPFKSIELDSVDAKI-ESINDLVASINELIakhnEITDNFEEEKNKAKKKlrlhlVEE 406

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1618 ANSNIELAGQDLEKIDEETYSAEAPANNTAQQVEKLAKKVQKLQNNIMKNDRDAKEITKE 1677
Cdd:pfam13166  407 FKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKL 466
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
 1337-1405 3.48e-03

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


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 37.72  E-value: 3.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24582614 1337 ERVSNLstlKDEANELASNTDRNCKRVENLSNKIQaeadDLANNNkliEDYRAELTSLTSQIPELNNQV 1405
Cdd:cd22301    2 ERLKNI---KKEAENLAKEIEDKMKRIEDLEKRIQ----DLNKRK---EDKANQLARLEKQVISLRKEI 60
PRK12705 PRK12705
hypothetical protein; Provisional
 1198-1408 5.15e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.62  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1198 LILSALEDATTATILRAKEIKQVGATGAYTSEFSELDKKLQHIRNLLQNTSVSLVDIEKLdyETQSLRDQLQASHGRLSE 1277
Cdd:PRK12705   11 LLLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQ--EARREREELQREEERLVQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614  1278 TEQNLDDIYNSLSLSGVELESLQNH-SRLVQQLSKELKENGIQLQEsniegALNLTRHAYERVSnLSTLKDEANELASnt 1356
Cdd:PRK12705   89 KEEQLDARAEKLDNLENQLEEREKAlSARELELEELEKQLDNELYR-----VAGLTPEQARKLL-LKLLDAELEEEKA-- 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24582614  1357 drncKRVENLSNKIQAEADDLANNN--KLIEDYRAELTSLT--SQIPELNNQVCGK 1408
Cdd:PRK12705  161 ----QRVKKIEEEADLEAERKAQNIlaQAMQRIASETASDLsvSVVPIPSDAMKGR 212
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1660-1771 6.25e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614   1660 LQNNIMKNDRDAKEITKEAGSVKLEAMRARGEANNLQsatsatnQTLTDRASRSENARERAKQLLQRASKLT---VDTNA 1736
Cdd:TIGR04523   24 YKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNdklKKNKD 96

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 24582614   1737 KLKDLN-DLQTVYL---NKNQQLLRLQAEIGPLNKELNE 1771
Cdd:TIGR04523   97 KINKLNsDLSKINSeikNDKEQKNKLEVELNKLEKQKKE 135
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 288-346 7.42e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.18  E-value: 7.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24582614    288 CSCYGHASQCLPLDPafsqadnedgmVHGRCECTHNTKGMNCEECEDFFNDLPWKPAFG 346
Cdd:pfam00053    1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
 1718-1786 7.88e-03

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


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 36.95  E-value: 7.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24582614 1718 ERAKQLLQRASKLTVDTNAKLKDLNDLQT--VYLNKNQ-----QLLRLQAEIGPLNKElnehlihIKERGSHYRQC 1786
Cdd:cd22301    2 ERLKNIKKEAENLAKEIEDKMKRIEDLEKriQDLNKRKedkanQLARLEKQVISLRKE-------IVERVEGYSTC 70
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 1492-1657 8.20e-03

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 39.70  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1492 LNQTNANIKLAENLFIA----LNNFQENKTASPSESKELAQKTLDlDLKlepEEIETLGDQINRAVSSLKNveaiiYRTK 1567
Cdd:cd21116   57 LLSLPNDIIGYNNTFQSyypdLIELADNLIKGDQGAKQQLLQGLE-ALQ---SQVTKKQTSVTSFINELTT-----FKND 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24582614 1568 PDlDRVNNLQSIAN-ATKEKA--DKILDSANSVVESLAAADESQGKAKDAIQQANSNIELAGQDLEKIDEETYSAEAP-- 1642
Cdd:cd21116  128 LD-DDSRNLQTDATkAQAQVAvlNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAFLQad 206

                        170
                 ....*....|....*...
gi 24582614 1643 ---ANNTAQQVEKLAKKV 1657
Cdd:cd21116  207 lkaAKADWNQLYEQAKSL 224
cc_LAMB1_C cd22300
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ...
 1716-1786 9.07e-03

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


Pssm-ID: 411971 [Multi-domain]  Cd Length: 73  Bit Score: 36.68  E-value: 9.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24582614 1716 ARERAKQLLQRASKLTVDTNAKLKDLNDLQTVYLNkNQQLLRLQA-EIGPLNKELNEHLIHIKERGSHYRQC 1786
Cdd:cd22300    2 ARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEE-NQKILEDKAqELVGLEEEVRSLLQEISQKVAVYSTC 72
 
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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