|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
33-252 |
4.79e-62 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 211.29 E-value: 4.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 33 CYPAAGDLLLGRahHLRASSTCGLTKPETYCtpHGEWSMR---CCRCDSRLPHtyNGHRVENV--LSSAGHSRWWQSQSG 107
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYC--ILSGLEGgkkCFICDSRDPH--NSHPPSNLtdSNNGTNETWWQSETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 108 V---KRVSLQLDLDQTFQLSSILLHFRSPLPAAMLIERSTDFGKTWEVYQYLASDCATAFPhVPRGSPESWQDARCQALQ 184
Cdd:pfam00055 75 ViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFG-RPSGPSRGIKDDEVICTS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 185 GH----PLHGGKVKFSVQDlASTITTSYSQTVDKLGQF--TNLRINFTEL--PHIARQGYHSPST--FYAVTEMLVLG 252
Cdd:pfam00055 154 EYsdisPLTGGEVIFSTLE-GRPSANIFDYSPELQDWLtaTNIRIRLLRLhtLGDELLDDPSVLRkyYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
27-252 |
2.57e-58 |
|
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: 201.05 E-value: 2.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 27 ACSQAACYPAAGDLLLGRahHLRASSTCGLTKPETYC--TPHGEWSMRCCRCDSRLPHtyNGHRVENV--LSSAGHSRWW 102
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCklVGHTEQGKKCDYCDARNPR--RSHPAENLtdGNNPNNPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 103 QSQS---GVKRVSLQLDLDQTFQLSSILLHFRSPLPAAMLIERStDFGKTWEVYQYLASDCATAFPHVPRGSPES--WQD 177
Cdd:smart00136 77 QSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITKgnEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 178 ARCQALQG--HPLHGGKVKFSVQDL-ASTITTSYSQTVDKLGQFTNLRINFTELPHIARQGYHS-----PSTFYAVTEML 249
Cdd:smart00136 156 VICTSEYSdiVPLEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrpevtRRYYYAISDIA 235
|
...
gi 1803687377 250 VLG 252
Cdd:smart00136 236 VGG 238
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1109-1179 |
2.38e-30 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 114.46 E-value: 2.38e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 1109 GSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYESCS 1179
Cdd:cd22303 1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
545-589 |
6.45e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.87 E-value: 6.45e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1803687377 545 CDCNFQGTEDVGCDKTTGQCLCRPGVTGPHCDQCQRGHC-STYPGC 589
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
390-439 |
8.77e-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: 63.91 E-value: 8.77e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1803687377 390 CECDPDGTVPGSiCDPLTGRCICKENVQGDRCHLCKPGFTQLANANPMGC 439
Cdd:pfam00053 1 CDCNPHGSLSDT-CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
545-582 |
1.52e-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: 63.14 E-value: 1.52e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1803687377 545 CDCNFQGTEDVGCDKTTGQCLCRPGVTGPHCDQCQRGH 582
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
545-582 |
2.07e-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: 62.76 E-value: 2.07e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1803687377 545 CDCNFQGTEDVGCDKTTGQCLCRPGVTGPHCDQCQRGH 582
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
389-440 |
9.46e-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: 60.83 E-value: 9.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1803687377 389 PCECDPDGTVPGSiCDPLTGRCICKENVQGDRCHLCKPGFTQLAnANPMGCR 440
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1169 |
2.67e-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: 68.16 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 851 ARLRETAQLIKTTETSANQIQSSTRRLADqMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMDPATIQEISESvLSLRLPT 930
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 931 DAAAVLRKMTEIQNLATKLqcpESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRG 1010
Cdd:TIGR02168 752 LSKELTELEAEIEELEERL---EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1011 SDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQnrlrATDAQQTAGEAGEQARSAQQAFEqvkq 1090
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA----LLNERASLEEALALLRSELEELS---- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1091 myAELkRRMEQspalgqqgsRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLL--------------- 1155
Cdd:TIGR02168 901 --EEL-RELES---------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealenkieddee 968
|
330
....*....|....
gi 1803687377 1156 GLEEQVGRIRDAIN 1169
Cdd:TIGR02168 969 EARRRLKRLENKIK 982
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
492-545 |
9.10e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 9.10e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 492 CGCHPHGSRSPHCNQFTGQCPCREGFTGRTCsatqeQVCPDRHFGDTRVGCTEC 545
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHC-----DRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-541 |
2.06e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 2.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 491 PCGCHPHGSRSPHCNQFTGQCPCREGFTGRTCSAtqeqvCPDRHFGDTRVG 541
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDR-----CAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
390-428 |
2.34e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 2.34e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1803687377 390 CECDPDGTVPGSiCDPLTGRCICKENVQGDRCHLCKPGF 428
Cdd:smart00180 1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
844-1162 |
6.68e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLsdkdmdpATIQEISESV 923
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRlptdaAAVLRKMTEIQNLATKLqcpESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLE 1003
Cdd:COG1196 298 ARLE-----QDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1004 ARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEA----GEQAR 1079
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEeealEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1080 SAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQALFEETLAMMLRMETLEMEIQE-SNKALMSKSARLLGLE 1158
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAaLLLAGLRGLAGAVAVL 529
|
....
gi 1803687377 1159 EQVG 1162
Cdd:COG1196 530 IGVE 533
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
442-489 |
1.03e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 1.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1803687377 442 CTCNALGTQQDmPCDDETGRCFCLPNVVGNDCDQCAAEYW--EMGSGRGC 489
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYglPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
492-542 |
1.14e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 492 CGCHPHGSRSPHCNQFTGQCPCREGFTGRTCSAtqeqvCPDRHFGDTRVGC 542
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDR-----CAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
442-489 |
4.80e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 4.80e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1803687377 442 CTCNALGTQQDmPCDDETGRCFCLPNVVGNDCDQCAAEYWeMGSGRGC 489
Cdd:smart00180 1 CDCDPGGSASG-TCDPDTGQCECKPNVTGRRCDRCAPGYY-GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
441-490 |
6.96e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 6.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 441 RCTCNALGTQQDmPCDDETGRCFCLPNVVGNDCDQCAAEYWEMGS-GRGCR 490
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
285-315 |
2.42e-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: 2.42e-06
10 20 30
....*....|....*....|....*....|.
gi 1803687377 285 QVHGHCVCQHNTAGPNCDRCAALYNDRPWAP 315
Cdd:cd00055 16 PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
885-1170 |
2.92e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 885 RTQIEGDLQRIQQFIQQVRNflsdkdmdpatIQE-ISESVLSLrlptdaAAVLRKMTEIqnlatklqcpESILVQTAEDI 963
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTEN-----------IEElIKEKEKEL------EEVLREINEI----------SSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 964 AKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKsLAGQL 1043
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1044 DGLMERLSQLQRGAD--QNRLRATDAQ-QTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQ 1120
Cdd:PRK03918 303 EEYLDELREIEKRLSrlEEEINGIEERiKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 1121 AL-FEETLAMMLRMETLEMEIQESNKALMSKSARllgLEEQVGRIRDAINK 1170
Cdd:PRK03918 383 GLtPEKLEKELEELEKAKEEIEEEISKITARIGE---LKKEIKELKKAIEE 430
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-377 |
5.34e-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: 44.65 E-value: 5.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 327 CNCNGHST---SCHFdpelyrasggaSGGVCDgCQHNTEGNNCERCKTNYFRNH 377
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
957-1170 |
9.54e-06 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.44 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 957 VQTAEDIAK-AKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKN 1035
Cdd:smart00283 3 SEAVEEIAAgAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1036 VKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQ---------------ARSAQQAfEQVKQMYAELKRRME 1100
Cdd:smart00283 83 VEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAgrgfavvadevrklaERSAESA-KEIESLIKEIQEETN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1101 QSPALGQQGSR-----------------------------VQSIDLEAQALF---EETLAMMLRMETLemeIQEsNKALM 1148
Cdd:smart00283 162 EAVAAMEESSSeveegvelveetgdaleeivdsveeiadlVQEIAAATDEQAagsEEVNAAIDEIAQV---TQE-TAAMS 237
|
250 260
....*....|....*....|...
gi 1803687377 1149 SKSAR-LLGLEEQVGRIRDAINK 1170
Cdd:smart00283 238 EEISAaAEELSGLAEELDELVER 260
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-376 |
1.52e-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: 1.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 326 RCNCNGHST---SCHFDpelyrasggasGGVCDgCQHNTEGNNCERCKTNYFRN 376
Cdd:cd00055 1 PCDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
285-318 |
2.35e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.73 E-value: 2.35e-05
10 20 30
....*....|....*....|....*....|....
gi 1803687377 285 QVHGHCVCQHNTAGPNCDRCAALYNDRPWAPAED 318
Cdd:pfam00053 15 PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
845-1170 |
1.34e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLSARLREtaQLIktteTSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFL--------SDKDMDPATI 916
Cdd:pfam12128 280 ERQETSAELNQ--LLR----TLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLdadietaaADQEQLPSWQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 917 QEISESVLSLRLPTDAAAVLRKMTEIQNLATKLQCpesilvqtAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGN-LR 995
Cdd:pfam12128 354 SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN--------NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESeLR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 996 -QANTVLLEARGAIRGSDSSLRFIQERVDEIEAvlgpAEKNVKSLAgQLDGLMERLSQLQRGADQNRLRATDAQQTAGEA 1074
Cdd:pfam12128 426 eQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA----TPELLLQLE-NFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1075 GEQA----RSAQQAFEQVKQMYAELKRRM------------------EQS------PAL--------------GQQGSRV 1112
Cdd:pfam12128 501 RDQAsealRQASRRLEERQSALDELELQLfpqagtllhflrkeapdwEQSigkvisPELlhrtdldpevwdgsVGGELNL 580
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1803687377 1113 QSIDLEAQAL-FEETLAMMlrmETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINK 1170
Cdd:pfam12128 581 YGVKLDLKRIdVPEWAASE---EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
285-313 |
2.20e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 2.20e-04
10 20
....*....|....*....|....*....
gi 1803687377 285 QVHGHCVCQHNTAGPNCDRCAALYNDRPW 313
Cdd:smart00180 15 PDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
327-377 |
8.92e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 8.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 327 CNCNG---HSTSCHFDpelyrasggasGGVCDgCQHNTEGNNCERCKTNYFRNH 377
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
854-1040 |
3.17e-03 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 40.30 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 854 RETAQLIKTTETSANQIQSSTRRLADQMSvtrtQIEGDLQRIQQFIQqvrnflsdkdmdpaTIQEISE--SVLSLRLPTD 931
Cdd:cd11386 29 EKGREAAEDAINQMNQIDESVDEAVSAVE----ELEESSAEIGEIVE--------------VIDDIAEqtNLLALNAAIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 932 AA---------AVLRKmtEIQNLATKLQcpesilvQTAEDIAK-AKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVL 1001
Cdd:cd11386 91 AArageagrgfAVVAD--EVRKLAEESA-------EAAKEIEElIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1803687377 1002 LEARGAIRGSDSSLRFIQERVDEIEAVlgpAEKNVKSLA 1040
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSAS---TQEIAAAVE 197
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
858-1128 |
5.18e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 858 QLIKTTETSANQIQSSTRRladQMSVTRTQIegdlQRIqqfiqqvrnflsdkdmdpatIQEISESVLSLRLPTDAAAVLR 937
Cdd:NF041483 76 QLLRNAQIQADQLRADAER---ELRDARAQT----QRI--------------------LQEHAEHQARLQAELHTEAVQR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 938 KMTEIQNLATKLQCPESilvQTAEDIAKAKQLQQEAE-QARNRANAVEGNVEEVVGNLR-QANTVLLEARGAIRGSDSSL 1015
Cdd:NF041483 129 RQQLDQELAERRQTVES---HVNENVAWAEQLRARTEsQARRLLDESRAEAEQALAAARaEAERLAEEARQRLGSEAESA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1016 RfiqervDEIEAVLGPAEKNVkslagqldglmERLsqlqrgadqnrLRATDAQ-QTAGEAGEQARSAQQA-FEQVKQMYA 1093
Cdd:NF041483 206 R------AEAEAILRRARKDA-----------ERL-----------LNAASTQaQEATDHAEQLRSSTAAeSDQARRQAA 257
|
250 260 270
....*....|....*....|....*....|....*
gi 1803687377 1094 ELKRRMEQSPALGQQGSRvqsidlEAQALFEETLA 1128
Cdd:NF041483 258 ELSRAAEQRMQEAEEALR------EARAEAEKVVA 286
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
33-252 |
4.79e-62 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 211.29 E-value: 4.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 33 CYPAAGDLLLGRahHLRASSTCGLTKPETYCtpHGEWSMR---CCRCDSRLPHtyNGHRVENV--LSSAGHSRWWQSQSG 107
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYC--ILSGLEGgkkCFICDSRDPH--NSHPPSNLtdSNNGTNETWWQSETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 108 V---KRVSLQLDLDQTFQLSSILLHFRSPLPAAMLIERSTDFGKTWEVYQYLASDCATAFPhVPRGSPESWQDARCQALQ 184
Cdd:pfam00055 75 ViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFG-RPSGPSRGIKDDEVICTS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 185 GH----PLHGGKVKFSVQDlASTITTSYSQTVDKLGQF--TNLRINFTEL--PHIARQGYHSPST--FYAVTEMLVLG 252
Cdd:pfam00055 154 EYsdisPLTGGEVIFSTLE-GRPSANIFDYSPELQDWLtaTNIRIRLLRLhtLGDELLDDPSVLRkyYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
27-252 |
2.57e-58 |
|
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: 201.05 E-value: 2.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 27 ACSQAACYPAAGDLLLGRahHLRASSTCGLTKPETYC--TPHGEWSMRCCRCDSRLPHtyNGHRVENV--LSSAGHSRWW 102
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCklVGHTEQGKKCDYCDARNPR--RSHPAENLtdGNNPNNPTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 103 QSQS---GVKRVSLQLDLDQTFQLSSILLHFRSPLPAAMLIERStDFGKTWEVYQYLASDCATAFPHVPRGSPES--WQD 177
Cdd:smart00136 77 QSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITKgnEDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 178 ARCQALQG--HPLHGGKVKFSVQDL-ASTITTSYSQTVDKLGQFTNLRINFTELPHIARQGYHS-----PSTFYAVTEML 249
Cdd:smart00136 156 VICTSEYSdiVPLEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrpevtRRYYYAISDIA 235
|
...
gi 1803687377 250 VLG 252
Cdd:smart00136 236 VGG 238
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1109-1179 |
2.38e-30 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 114.46 E-value: 2.38e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 1109 GSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYESCS 1179
Cdd:cd22303 1 GERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1109-1178 |
2.10e-14 |
|
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: 68.84 E-value: 2.10e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1109 GSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYESC 1178
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
545-589 |
6.45e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.87 E-value: 6.45e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1803687377 545 CDCNFQGTEDVGCDKTTGQCLCRPGVTGPHCDQCQRGHC-STYPGC 589
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYgDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
390-439 |
8.77e-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: 63.91 E-value: 8.77e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1803687377 390 CECDPDGTVPGSiCDPLTGRCICKENVQGDRCHLCKPGFTQLANANPMGC 439
Cdd:pfam00053 1 CDCNPHGSLSDT-CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
545-582 |
1.52e-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: 63.14 E-value: 1.52e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1803687377 545 CDCNFQGTEDVGCDKTTGQCLCRPGVTGPHCDQCQRGH 582
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
545-582 |
2.07e-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: 62.76 E-value: 2.07e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1803687377 545 CDCNFQGTEDVGCDKTTGQCLCRPGVTGPHCDQCQRGH 582
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
389-440 |
9.46e-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: 60.83 E-value: 9.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1803687377 389 PCECDPDGTVPGSiCDPLTGRCICKENVQGDRCHLCKPGFTQLAnANPMGCR 440
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1169 |
2.67e-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: 68.16 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 851 ARLRETAQLIKTTETSANQIQSSTRRLADqMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMDPATIQEISESvLSLRLPT 930
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 931 DAAAVLRKMTEIQNLATKLqcpESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRG 1010
Cdd:TIGR02168 752 LSKELTELEAEIEELEERL---EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1011 SDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQnrlrATDAQQTAGEAGEQARSAQQAFEqvkq 1090
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA----LLNERASLEEALALLRSELEELS---- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1091 myAELkRRMEQspalgqqgsRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLL--------------- 1155
Cdd:TIGR02168 901 --EEL-RELES---------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealenkieddee 968
|
330
....*....|....
gi 1803687377 1156 GLEEQVGRIRDAIN 1169
Cdd:TIGR02168 969 EARRRLKRLENKIK 982
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
492-545 |
9.10e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 9.10e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 492 CGCHPHGSRSPHCNQFTGQCPCREGFTGRTCsatqeQVCPDRHFGDTRVGCTEC 545
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHC-----DRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
491-541 |
2.06e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 2.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 491 PCGCHPHGSRSPHCNQFTGQCPCREGFTGRTCSAtqeqvCPDRHFGDTRVG 541
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDR-----CAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
390-428 |
2.34e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 2.34e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1803687377 390 CECDPDGTVPGSiCDPLTGRCICKENVQGDRCHLCKPGF 428
Cdd:smart00180 1 CDCDPGGSASGT-CDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1083 |
2.63e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLSARLRE-TAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMDPATIQEISESV 923
Cdd:TIGR02169 266 RLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRLPTDAAavlrkMTEIQNLATKLQcpesILVQTAEDIAKA--------KQLQQEAEQARNRANAVEGNVEEVVGNLR 995
Cdd:TIGR02169 346 EEERKRRDKL-----TEEYAELKEELE----DLRAELEEVDKEfaetrdelKDYREKLEKLKREINELKRELDRLQEELQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 996 QANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQL--------------DGLMERLSQLQRgadqnR 1061
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLskyeqelydlkeeyDRVEKELSKLQR-----E 491
|
250 260
....*....|....*....|..
gi 1803687377 1062 LRATDAQQTAGEAGEQARSAQQ 1083
Cdd:TIGR02169 492 LAEAEAQARASEERVRGGRAVE 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
844-1162 |
6.68e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLsdkdmdpATIQEISESV 923
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRlptdaAAVLRKMTEIQNLATKLqcpESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLE 1003
Cdd:COG1196 298 ARLE-----QDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1004 ARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEA----GEQAR 1079
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEeealEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1080 SAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQALFEETLAMMLRMETLEMEIQE-SNKALMSKSARLLGLE 1158
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAaLLLAGLRGLAGAVAVL 529
|
....
gi 1803687377 1159 EQVG 1162
Cdd:COG1196 530 IGVE 533
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
958-1170 |
9.35e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 958 QTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLgpaEKNVK 1037
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1038 SLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPAL-GQQGSRVQSID 1116
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALrAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 1117 LEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINK 1170
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
935-1159 |
9.43e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.84 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 935 VLRKMTEIQNLATKLQCPESILVQTAED-IAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARgairgsdS 1013
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKaLFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-------E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1014 SLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQrgADQNRLRAT----DAQQTAGEAGEQARSAQ--QAFEQ 1087
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ--KERQDLEQQrkqlEAQIAELQSEIAEREEElkELEEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 1088 VKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQA------LFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEE 1159
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEAnrnaekEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
442-489 |
1.03e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 1.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1803687377 442 CTCNALGTQQDmPCDDETGRCFCLPNVVGNDCDQCAAEYW--EMGSGRGC 489
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYglPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
492-542 |
1.14e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 492 CGCHPHGSRSPHCNQFTGQCPCREGFTGRTCSAtqeqvCPDRHFGDTRVGC 542
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDR-----CAPGYYGDGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
960-1168 |
2.56e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 960 AEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSL 1039
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1040 AGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAE-LKRRMEQSPALGQQGSRVQSIDLE 1118
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEaLRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1119 AQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAI 1168
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
957-1176 |
2.70e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.69 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 957 VQTAEDIAK-AKQLQQEAEQARNRANAVEGN-------VEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAV 1028
Cdd:COG4372 37 LFELDKLQEeLEQLREELEQAREELEQLEEEleqarseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1029 LGPAEKNVKSLAGQLDGLMERLSQLQRGAD---------QNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRM 1099
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAereeelkelEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 1100 EQSPALG-QQGSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYE 1176
Cdd:COG4372 197 EKEEELAeAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
963-1168 |
5.97e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 963 IAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQ 1042
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1043 LDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEqspalgQQGSRVQSIDLEAQAL 1122
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL------EAEAELAEAEEELEEL 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1803687377 1123 FEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAI 1168
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
442-489 |
4.80e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 4.80e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1803687377 442 CTCNALGTQQDmPCDDETGRCFCLPNVVGNDCDQCAAEYWeMGSGRGC 489
Cdd:smart00180 1 CDCDPGGSASG-TCDPDTGQCECKPNVTGRRCDRCAPGYY-GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
441-490 |
6.96e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 6.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 441 RCTCNALGTQQDmPCDDETGRCFCLPNVVGNDCDQCAAEYWEMGS-GRGCR 490
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
922-1152 |
7.66e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 922 SVLSLRLPTDAAAVlrkmTEIQNLATKLQCPESILVQTAEDIakaKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVL 1001
Cdd:COG3883 2 LALALAAPTPAFAD----PQIQAKQKELSELQAELEAAQAEL---DALQAELEELNEEYNELQAELEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1002 LEARGAIRGSDSSL----RFIQE---RVDEIEAVLGpaeknvkslAGQLDGLMERLSQLQR--GADQNRLRA-TDAQQTA 1071
Cdd:COG3883 75 AEAEAEIEERREELgeraRALYRsggSVSYLDVLLG---------SESFSDFLDRLSALSKiaDADADLLEElKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1072 GEAGEQARSAQQAFEQVKQMYAELKRRMEQspALGQQGSRVQSIDLEAQALFEEtlammlrMETLEMEIQESNKALMSKS 1151
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEA--QQAEQEALLAQLSAEEAAAEAQ-------LAELEAELAAAEAAAAAAA 216
|
.
gi 1803687377 1152 A 1152
Cdd:COG3883 217 A 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
961-1172 |
8.41e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 961 EDIAKAKQLQQEAEQARNRANAVEGNVEE---VVGNLRQANTVLLEARgairgsDSSLRF--IQERVDEIEA--VLGPAE 1033
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRRER------EKAERYqaLLKEKREYEGyeLLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1034 KNVKSLA---GQLDGLMERLSQLQRGADQNRLRATDAQQTAGEA---------GEQAR------SAQQAFEQVKQMYAEL 1095
Cdd:TIGR02169 234 ALERQKEaieRQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeEEQLRvkekigELEAEIASLERSIAEK 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 1096 KRRMEQSPALGQQG-SRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRV 1172
Cdd:TIGR02169 314 ERELEDAEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1174 |
1.19e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 847 RSLSARLRETAQLIKTTETSANQIQSSTRRLaDQMSVTRT-------QIEGDLQRIQQFIQQVRNFLSD--KDMDPATIQ 917
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDL-SSLEQEIEnvkselkELEARIEELEEDLHKLEEALNDleARLSHSRIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 918 EISESVLSLRlptdaaAVLRKMTE-IQNLATKLQcPESILVQTAEDiaKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQ 996
Cdd:TIGR02169 795 EIQAELSKLE------EEVSRIEArLREIEQKLN-RLTLEKEYLEK--EIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 997 ANTVLLEARGAIRGSDSSL--------------RFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRgadqnrl 1062
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLgdlkkerdeleaqlRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED------- 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1063 ratdaqqtAGEAGEQARSAQQAFEQVKQMYAELKRRMEqspALGqqgsrvqSIDLEAQALFEETLAMMLRMETLEMEIQE 1142
Cdd:TIGR02169 939 --------PKGEDEEIPEEELSLEDVQAELQRVEEEIR---ALE-------PVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
330 340 350
....*....|....*....|....*....|...
gi 1803687377 1143 SNKALMSKSARLLGLEEQV-GRIRDAINKRVAY 1174
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKREVfMEAFEAINENFNE 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
845-1128 |
1.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMdpatiQEISESVL 924
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-----AEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 925 SLRLPTDAAAVLRKMTEIQNLATKLQcpeSILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEA 1004
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELL---EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1005 RGAIRgsdSSLRFIQERVDEIEAvlgpAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQqtageagEQARSAQQA 1084
Cdd:COG1196 441 EEALE---EAAEEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-------EAEADYEGF 506
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1803687377 1085 FEQVKqmyaeLKRRMEQSPALGQQGSRVQSIDLEAQALFEETLA 1128
Cdd:COG1196 507 LEGVK-----AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
847-1097 |
1.90e-07 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 55.03 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 847 RSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIE---GDLQRIQQFIQQVRNFLSdkdmdpaTIQEISE-- 921
Cdd:COG0840 305 QEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEetaETIEELGESSQEIGEIVD-------VIDDIAEqt 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 922 SVLSLrlptDAA-------------AVLrkMTEIQNLATKLQcpesilvQTAEDIAKA-KQLQQEAEQARNRANAVEGNV 987
Cdd:COG0840 378 NLLAL----NAAieaarageagrgfAVV--ADEVRKLAERSA-------EATKEIEELiEEIQSETEEAVEAMEEGSEEV 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 988 EEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVlgpaeknvkslAGQLDGLMERLSQLqrgadqnrlratdA 1067
Cdd:COG0840 445 EEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAG-----------TEEVNQAIEQIAAA-------------A 500
|
250 260 270
....*....|....*....|....*....|
gi 1803687377 1068 QQTAGEAGEQARSAQQAFEQVKQMYAELKR 1097
Cdd:COG0840 501 QENAASVEEVAAAAEELAELAEELQELVSR 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
967-1171 |
2.37e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 967 KQLQQEAEQARnRANAVEGNVEEvvgnlRQANTVLLEargairgsdssLRFIQERVDEIEAVLgpaeknvKSLAGQLDGL 1046
Cdd:COG1196 203 EPLERQAEKAE-RYRELKEELKE-----LEAELLLLK-----------LRELEAELEELEAEL-------EELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1047 MERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQV-KQMYAELKRRMEQSPALGQQGSRVQSIDLEAQALFEE 1125
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1803687377 1126 TLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKR 1171
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
844-1169 |
2.44e-07 |
|
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: 54.96 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLI---KTTETSANQIQSSTRR--LADQMSvtrtQIEGDLQRIQQFIQQVRNFLSDKDmdpATIQE 918
Cdd:COG5185 289 KQFENTKEKIAEYTKSIdikKATESLEEQLAAAEAEqeLEESKR----ETETGIQNLTAEIEQGQESLTENL---EAIKE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 919 ISESVLSLRLPTDAAAVLRKM-TEIQNLatklqcPESILVQTAEdiakAKQLQQEAEQARNRA-NAVEGNVEEVVGNLRQ 996
Cdd:COG5185 362 EIENIVGEVELSKSSEELDSFkDTIEST------KESLDEIPQN----QRGYAQEILATLEDTlKAADRQIEELQRQIEQ 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 997 ANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQ--LDGLMERLSQLQRGAdqnrlrATDAQQTAGEA 1074
Cdd:COG5185 432 ATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRskKEDLNEELTQIESRV------STLKATLEKLR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1075 GEQARSAQQAFEQVKQMYAELKRRM-EQSPALGQQGSrvqsidlEAQALFEETLAMMlrMETLEMEIQESNKALMSKSAR 1153
Cdd:COG5185 506 AKLERQLEGVRSKLDQVAESLKDFMrARGYAHILALE-------NLIPASELIQASN--AKTDGQAANLRTAVIDELTQY 576
|
330
....*....|....*.
gi 1803687377 1154 LLGLEEQVGRIRDAIN 1169
Cdd:COG5185 577 LSTIESQQAREDPIPD 592
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1111-1178 |
3.21e-07 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 48.51 E-value: 3.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 1111 RVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYESC 1178
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
931-1170 |
3.87e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 931 DAAAVLRKMTEIQNLatklqcPESILVQ---TAEDiakakqlqqeAEQARNRANAVegnVEEVVGNLRQANTvllearga 1007
Cdd:COG3206 118 AAIERLRKNLTVEPV------KGSNVIEisyTSPD----------PELAAAVANAL---AEAYLEQNLELRR-------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1008 iRGSDSSLRFIQERVDEIEAVLGPAEKNVK---------SLAGQLDGLMERLSQLqrgadQNRLRATDAQQtageagEQA 1078
Cdd:COG3206 171 -EEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSEL-----ESQLAEARAEL------AEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1079 RSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDL---EAQALFEET----LAMMLRMETLEMEI-QESNKALMSK 1150
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAelaELSARYTPNhpdvIALRAQIAALRAQLqQEAQRILASL 318
|
250 260
....*....|....*....|
gi 1803687377 1151 SARLLGLEEQVGRIRDAINK 1170
Cdd:COG3206 319 EAELEALQAREASLQAQLAQ 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1170 |
5.70e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDmdpATIQEISESV 923
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE---EELEEAQEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRLPTDAaavLRKMTEIQNLATKLQCPESILVQTAEDIAKAKQLQQEAEQARNRANA---VEGNVEEVVGNLRQANTV 1000
Cdd:COG4717 223 EELEEELEQ---LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflVLGLLALLFLLLAREKAS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1001 LLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLA-------GQLDGLMERLSQLQRGADQNRLRATDAQ---QT 1070
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldriEELQELLREAEELEEELQLEELEQEIAAllaEA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1071 AGEAGEQARSAQQAFEQvkqmYAELKRRMEQspaLGQQgsrvqsidLEAQALFEETLAMMLRMETLEMEIQESNKALMSK 1150
Cdd:COG4717 380 GVEDEEELRAALEQAEE----YQELKEELEE---LEEQ--------LEELLGELEELLEALDEEELEEELEELEEELEEL 444
|
330 340
....*....|....*....|
gi 1803687377 1151 SARLLGLEEQVGRIRDAINK 1170
Cdd:COG4717 445 EEELEELREELAELEAELEQ 464
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
877-1116 |
5.88e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 877 LADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDmdpATIQEISESVLSLRLPTDAAAVLRKMTEIQNLATKLQcpesil 956
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE---AALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 957 VQTAEDIAKAKQLQQEAEQARNRANAVEGN--VEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEK 1034
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1035 NVK-SLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAfeqvKQMYAELKRRMEQ-SPALGQQGSRV 1112
Cdd:COG3206 313 RILaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA----RELYESLLQRLEEaRLAEALTVGNV 388
|
....
gi 1803687377 1113 QSID 1116
Cdd:COG3206 389 RVID 392
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
958-1094 |
6.88e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 51.36 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 958 QTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVvgnLRQANTVLleARGAIrgsdSSLRFIQERVDEIEAVLGPAEKNVK 1037
Cdd:COG1842 45 ALAQVIANQKRLERQLEELEAEAEKWEEKARLA---LEKGREDL--AREAL----ERKAELEAQAEALEAQLAQLEEQVE 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1803687377 1038 SLAGQLDGLMERLSQLQRGADQ--NRLRATDAQQTAGEA--GEQARSAQQAFEQVK----QMYAE 1094
Cdd:COG1842 116 KLKEALRQLESKLEELKAKKDTlkARAKAAKAQEKVNEAlsGIDSDDATSALERMEekieEMEAR 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
844-1163 |
8.61e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQ-SSTRRLADQMSVTR--TQIEGDLQRIQQFIQQVRnflsdkdmdpATIQEIS 920
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAelARLEQDIARLEERRRELE----------ERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 921 ESVLSL--RLPTDAAAVLRKMTEIQNLATKLQCPESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQAN 998
Cdd:COG1196 323 EELAELeeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 999 TVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQA 1078
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1079 RSAQQAFEQVKQMYAELKRRMEQSPA-------LGQQGSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKS 1151
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEgvkaallLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
330
....*....|..
gi 1803687377 1152 ARLLgLEEQVGR 1163
Cdd:COG1196 563 IEYL-KAAKAGR 573
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1057 |
1.21e-06 |
|
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: 53.14 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVrNFLSDKdmdpatIQEISESV 923
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL-AELEEK------LEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRLPTDAAAVLRKM---------TEIQNLATKLQCPE----------SILVQTAEDIAKAKQlQQEAEQARNRANAVE 984
Cdd:TIGR02168 354 ESLEAELEELEAELEElesrleeleEQLETLRSKVAQLElqiaslnneiERLEARLERLEDRRE-RLQQEIEELLKKLEE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1803687377 985 GNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGL---MERLSQLQRGA 1057
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerlQENLEGFSEGV 508
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
285-315 |
2.42e-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: 2.42e-06
10 20 30
....*....|....*....|....*....|.
gi 1803687377 285 QVHGHCVCQHNTAGPNCDRCAALYNDRPWAP 315
Cdd:cd00055 16 PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
885-1170 |
2.92e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 885 RTQIEGDLQRIQQFIQQVRNflsdkdmdpatIQE-ISESVLSLrlptdaAAVLRKMTEIqnlatklqcpESILVQTAEDI 963
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTEN-----------IEElIKEKEKEL------EEVLREINEI----------SSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 964 AKAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKsLAGQL 1043
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1044 DGLMERLSQLQRGAD--QNRLRATDAQ-QTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQ 1120
Cdd:PRK03918 303 EEYLDELREIEKRLSrlEEEINGIEERiKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 1121 AL-FEETLAMMLRMETLEMEIQESNKALMSKSARllgLEEQVGRIRDAINK 1170
Cdd:PRK03918 383 GLtPEKLEKELEELEKAKEEIEEEISKITARIGE---LKKEIKELKKAIEE 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
963-1171 |
3.01e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 963 IAKAKQLQQEAEQARNRANAVEGNVEEvvgnlrqantvLLEARGAIRGSDSSLRFIQERVDEieavlgpaEKNVKSLAGQ 1042
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEA-----------LEAELDALQERREALQRLAEYSWD--------EIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1043 LDGLMERLSQLQRG----------ADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRV 1112
Cdd:COG4913 670 IAELEAELERLDASsddlaaleeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1803687377 1113 QSIDLEAQALFEETLAMMLRmetlemEIQESNKALmskSARLLGLEEQVGRIRDAINKR 1171
Cdd:COG4913 750 LLEERFAAALGDAVERELRE------NLEERIDAL---RARLNRAEEELERAMRAFNRE 799
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1089 |
3.50e-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: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 847 RSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQI---EGDLQRIQQFIQQVRNFLSDKDMDpatIQEISESV 923
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKE---IAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRlpTDAAAVLRKMTEIQNlatklQCPESILV--QTAEDIAKAKQLQQEAEQAR-NRANAVEGNVEEvvgnLRQANTV 1000
Cdd:COG4942 100 EAQK--EELAELLRALYRLGR-----QPPLALLLspEDFLDAVRRLQYLKYLAPARrEQAEELRADLAE----LAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1001 LLEARGAIRgsdSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRgaDQNRLRATDAQQTAGEAGEQARS 1080
Cdd:COG4942 169 LEAERAELE---ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--EAEELEALIARLEAEAAAAAERT 243
|
....*....
gi 1803687377 1081 AQQAFEQVK 1089
Cdd:COG4942 244 PAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
942-1171 |
4.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 942 IQNLATKLQCPESILVQTAEDIAKAKQLQQEAEQARNRANAVEG------NVEEVVGNLRQANtvllEARGAIRGSDSSL 1015
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELE----AELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1016 RFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQ---ARSAQQAFEQVkqmY 1092
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAV---E 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1093 AELKRRMEQspalgqqgsRVQSIDLEAQALFEETLAMMLR------METLEMEIQ-ESNKALMSKSARLL--GLEEQVGR 1163
Cdd:COG4913 765 RELRENLEE---------RIDALRARLNRAEEELERAMRAfnrewpAETADLDADlESLPEYLALLDRLEedGLPEYEER 835
|
....*...
gi 1803687377 1164 IRDAINKR 1171
Cdd:COG4913 836 FKELLNEN 843
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
327-377 |
5.34e-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: 44.65 E-value: 5.34e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 327 CNCNGHST---SCHFdpelyrasggaSGGVCDgCQHNTEGNNCERCKTNYFRNH 377
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
848-1087 |
5.36e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 848 SLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMDPATIQEIsESVLSLR 927
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL-DVLLGSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 928 LPTDA---AAVLRKMTEIQNlatklqcpeSILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVvgnLRQANTVLLEA 1004
Cdd:COG3883 113 SFSDFldrLSALSKIADADA---------DLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1005 RGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQA 1084
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
...
gi 1803687377 1085 FEQ 1087
Cdd:COG3883 261 SAG 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1174 |
9.49e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSST-RRLADQMSVT--RTQIEGDLQRIQQFIQQVRnflsdkdmdpATIQEIS 920
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAgLDDADAEAVEarREELEDRDEELRDRLEECR----------VAAQAHN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 921 ESVLSLRlpTDAAAVLRKMTEIQNLATKLqcpESILVQTAEDIAKAK----QLQQEAEQARNRAnaveGNVEEVVGNLRQ 996
Cdd:PRK02224 342 EEAESLR--EDADDLEERAEELREEAAEL---ESELEEAREAVEDRReeieELEEEIEELRERF----GDAPVDLGNAED 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 997 ANTVLLEARGAIRGS----DSSLRFIQERVDEIEAVLG---------PAEKN--VKSLA---GQLDGLMERLSQL--QRG 1056
Cdd:PRK02224 413 FLEELREERDELREReaelEATLRTARERVEEAEALLEagkcpecgqPVEGSphVETIEedrERVEELEAELEDLeeEVE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1057 ADQNRL-RATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQqgsRVQSIDLEAQALFEETLAMMLRMET 1135
Cdd:PRK02224 493 EVEERLeRAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE---RAAELEAEAEEKREAAAEAEEEAEE 569
|
330 340 350
....*....|....*....|....*....|....*....
gi 1803687377 1136 LEMEIQESNKALMSKSARLlgleEQVGRIRDAINKRVAY 1174
Cdd:PRK02224 570 AREEVAELNSKLAELKERI----ESLERIRTLLAAIADA 604
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
957-1170 |
9.54e-06 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.44 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 957 VQTAEDIAK-AKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKN 1035
Cdd:smart00283 3 SEAVEEIAAgAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1036 VKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQ---------------ARSAQQAfEQVKQMYAELKRRME 1100
Cdd:smart00283 83 VEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAgrgfavvadevrklaERSAESA-KEIESLIKEIQEETN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1101 QSPALGQQGSR-----------------------------VQSIDLEAQALF---EETLAMMLRMETLemeIQEsNKALM 1148
Cdd:smart00283 162 EAVAAMEESSSeveegvelveetgdaleeivdsveeiadlVQEIAAATDEQAagsEEVNAAIDEIAQV---TQE-TAAMS 237
|
250 260
....*....|....*....|...
gi 1803687377 1149 SKSAR-LLGLEEQVGRIRDAINK 1170
Cdd:smart00283 238 EEISAaAEELSGLAEELDELVER 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1015-1171 |
1.30e-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: 48.99 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1015 LRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAE 1094
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1095 LKR---RMEQSPAL---------GQQGSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVG 1162
Cdd:COG4942 109 LLRalyRLGRQPPLalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
....*....
gi 1803687377 1163 RIRDAINKR 1171
Cdd:COG4942 189 ALEALKAER 197
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
326-376 |
1.52e-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: 1.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 326 RCNCNGHST---SCHFDpelyrasggasGGVCDgCQHNTEGNNCERCKTNYFRN 376
Cdd:cd00055 1 PCDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
920-1090 |
1.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 920 SESVLSLRlpTDAAAVLRKMTEIQNLATKLQCP-------ESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVG 992
Cdd:PRK04863 285 LEEALELR--RELYTSRRQLAAEQYRLVEMARElaelneaESDLEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 993 NLRQANTVLLEArgairgsdsslrfiQERVDEIEAVLGPAEKNVKSLAGQLdglmerlsqlqrgAD-QNRLratDAQQT- 1070
Cdd:PRK04863 363 RLEEQNEVVEEA--------------DEQQEENEARAEAAEEEVDELKSQL-------------ADyQQAL---DVQQTr 412
|
170 180
....*....|....*....|
gi 1803687377 1071 AGeageQARSAQQAFEQVKQ 1090
Cdd:PRK04863 413 AI----QYQQAVQALERAKQ 428
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
285-318 |
2.35e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.73 E-value: 2.35e-05
10 20 30
....*....|....*....|....*....|....
gi 1803687377 285 QVHGHCVCQHNTAGPNCDRCAALYNDRPWAPAED 318
Cdd:pfam00053 15 PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
965-1098 |
2.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 965 KAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSS--------LRFIQERVDEIEAVLGPAEKNV 1036
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1803687377 1037 KSLAGQLDGLMERLSQLQRGADQNRLRATD----AQQTAGEAGEQARSAQQAFEQVKQMYAELKRR 1098
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEeleaLEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
827-1159 |
2.74e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 827 GIFPLSSAALATAGEAAREFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQI---------EGDLQRIQQ 897
Cdd:TIGR00606 567 GYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeESDLERLKE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 898 FIQQVRNflsDKDMDPATIQEISESVLSLRLPTDAAA-----VLRKMTEIQNLATKLQCpesiLVQTAEDiaKAKQLQQE 972
Cdd:TIGR00606 647 EIEKSSK---QRAMLAGATAVYSQFITQLTDENQSCCpvcqrVFQTEAELQEFISDLQS----KLRLAPD--KLKSTESE 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 973 AEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLG---PAEKNVKSL---AGQLDGL 1046
Cdd:TIGR00606 718 LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAKVCltdVTIMERF 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1047 MERLSQLQRGADQ--NRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKR----RMEQSPALGQQGSRVQSIDLEAQ 1120
Cdd:TIGR00606 798 QMELKDVERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdQQEQIQHLKSKTNELKSEKLQIG 877
|
330 340 350
....*....|....*....|....*....|....*....
gi 1803687377 1121 ALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEE 1159
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
870-1154 |
2.82e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 870 IQSSTRRLADQmsvtrtqiEGDLQRIQQFIQQVRNFlsdkdmdPATIQEISESVLSLRlptDAAAVLRKMTEIQNLATKl 949
Cdd:PRK10929 50 LQSALNWLEER--------KGSLERAKQYQQVIDNF-------PKLSAELRQQLNNER---DEPRSVPPNMSTDALEQE- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 950 qcpesILVQTAEDIAKAKQLQQEAEQAR-------------NRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLR 1016
Cdd:PRK10929 111 -----ILQVSSQLLEKSRQAQQEQDRAReisdslsqlpqqqTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1017 fiQERVDEIE-AVLGP-------------AEKNVKSLAGQLDGLMERL-SQLQRGADQnrlratdaqqtAGEAGEQArsA 1081
Cdd:PRK10929 186 --KALVDELElAQLSAnnrqelarlrselAKKRSQQLDAYLQALRNQLnSQRQREAER-----------ALESTELL--A 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803687377 1082 QQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQALFEETLAMMLRMETLEMEIQ---ESN---KALMSKSARL 1154
Cdd:PRK10929 251 EQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQSQwlgVSNalgEALRAQVARL 329
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
851-1161 |
4.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 851 ARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQiegdLQRIQQFIQQVrNFLSDKDMdPATIQEISESVLSLRlpt 930
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEG----LSALNRLLPRL-NLLADETL-ADRVEEIREQLDEAE--- 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 931 DAAAVLRK----MTEIQNLATKLQCPESILVQTAEDIAKAKQLQQeaeQARNRANAVegnveevvgnlrqanTVLLEARG 1006
Cdd:PRK04863 908 EAKRFVQQhgnaLAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQR---DAKQQAFAL---------------TEVVQRRA 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1007 AIRGSDSslrfiQERVDEiEAVLGPAeknvkslagqldgLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFE 1086
Cdd:PRK04863 970 HFSYEDA-----AEMLAK-NSDLNEK-------------LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYD 1030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1087 QVKQMYAELKRRMEqspALGQQGsrvqSIDLEAQA-LFEETLAMMLR--------MET----LEMEIQESNKALMSKSAR 1153
Cdd:PRK04863 1031 AKRQMLQELKQELQ---DLGVPA----DSGAEERArARRDELHARLSanrsrrnqLEKqltfCEAEMDNLTKKLRKLERD 1103
|
....*...
gi 1803687377 1154 LLGLEEQV 1161
Cdd:PRK04863 1104 YHEMREQV 1111
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1111-1178 |
4.93e-05 |
|
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: 42.46 E-value: 4.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 1111 RVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYESC 1178
Cdd:cd22300 5 KAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1011-1173 |
9.55e-05 |
|
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: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1011 SDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRgadqnrlRATDAQQTAGEAGEQARSAQqafEQVKQ 1090
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-------ELEALQAEIDKLQAEIAEAE---AEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1091 MYAELKRRMEqspALGQQGSRVQSID--LEAQ-------------ALFEETLAMMLRMETLEMEIQESNKALMSKSARLL 1155
Cdd:COG3883 84 RREELGERAR---ALYRSGGSVSYLDvlLGSEsfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170
....*....|....*...
gi 1803687377 1156 GLEEQVGRIRDAINKRVA 1173
Cdd:COG3883 161 ALKAELEAAKAELEAQQA 178
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
844-1123 |
1.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEgDLQRIQQFIQQVRNFLSdkdmdpATIQEISESV 923
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE-ELQKERQDLEQQRKQLE------AQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 924 LSLRlpTDAAAVLRKMTEIQNLATKLQcPESILVQTAEDIAKAKQLQQEAEQ--------ARNRANAVEGNVEEVVGNLR 995
Cdd:COG4372 146 AERE--EELKELEEQLESLQEELAALE-QELQALSEAEAEQALDELLKEANRnaekeeelAEAEKLIESLPRELAEELLE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 996 QANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGP-AEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEA 1074
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKeIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1803687377 1075 GEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQALF 1123
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLL 351
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
845-1170 |
1.34e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLSARLREtaQLIktteTSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFL--------SDKDMDPATI 916
Cdd:pfam12128 280 ERQETSAELNQ--LLR----TLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLdadietaaADQEQLPSWQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 917 QEISESVLSLRLPTDAAAVLRKMTEIQNLATKLQCpesilvqtAEDIAKAKQLQQEAEQARNRANAVEGNVEEVVGN-LR 995
Cdd:pfam12128 354 SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN--------NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESeLR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 996 -QANTVLLEARGAIRGSDSSLRFIQERVDEIEAvlgpAEKNVKSLAgQLDGLMERLSQLQRGADQNRLRATDAQQTAGEA 1074
Cdd:pfam12128 426 eQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA----TPELLLQLE-NFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1075 GEQA----RSAQQAFEQVKQMYAELKRRM------------------EQS------PAL--------------GQQGSRV 1112
Cdd:pfam12128 501 RDQAsealRQASRRLEERQSALDELELQLfpqagtllhflrkeapdwEQSigkvisPELlhrtdldpevwdgsVGGELNL 580
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1803687377 1113 QSIDLEAQAL-FEETLAMMlrmETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINK 1170
Cdd:pfam12128 581 YGVKLDLKRIdVPEWAASE---EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
958-1162 |
1.80e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 958 QTAEDIAKAKQLQQE-----AEQARNRANAVEGNVEEVVGNL------RQANTVLLEARgairgsdsSLRFIQERVDEIE 1026
Cdd:COG3096 447 RAKEQQATEEVLELEqklsvADAARRQFEKAYELVCKIAGEVersqawQTARELLRRYR--------SQQALAQRLQQLR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1027 AVLGPAEKNVKSLAG---QLDGLMERLSQLQRGAD-----QNRLRAT--DAQQTAGEAGEQARSAQQAFEQVKQMYAELK 1096
Cdd:COG3096 519 AQLAELEQRLRQQQNaerLLEEFCQRIGQQLDAAEeleelLAELEAQleELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1097 RR---------------------MEQSPALGQQGSRVQSIDLEAQALFEETLAmmlRMETLEMEIQESNKALMSKSARLL 1155
Cdd:COG3096 599 ARapawlaaqdalerlreqsgeaLADSQEVTAAMQQLLEREREATVERDELAA---RKQALESQIERLSQPGGAEDPRLL 675
|
....*..
gi 1803687377 1156 GLEEQVG 1162
Cdd:COG3096 676 ALAERLG 682
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
845-1054 |
2.01e-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: 44.33 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRT---QIEGDLQRIQQFIQQVRNFLSDKDMDpatIQEISE 921
Cdd:pfam06008 27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAkaqQVNAESERTLGHAKELAEAIKNLIDN---IKEINE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 922 SVLSLRLPTDAAAV---LRKMTEIQNLATKLQCPE-SILVQTAEDIAKAKQ------------LQQE----AEQARNRAN 981
Cdd:pfam06008 104 KVATLGENDFALPSsdlSRMLAEAQRMLGEIRSRDfGTQLQNAEAELKAAQdllsriqtwfqsPQEEnkalANALRDSLA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1803687377 982 AVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQ 1054
Cdd:pfam06008 184 EYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLLLQEID 256
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
285-313 |
2.20e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 2.20e-04
10 20
....*....|....*....|....*....
gi 1803687377 285 QVHGHCVCQHNTAGPNCDRCAALYNDRPW 313
Cdd:smart00180 15 PDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1109-1178 |
2.43e-04 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 40.50 E-value: 2.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1109 GSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVAYYESC 1178
Cdd:cd22299 2 KGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTC 71
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
967-1170 |
2.78e-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: 45.43 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 967 KQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGsdsslrfIQERVDEIEAVLGPAEKNVKSLAGQLDGL 1046
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1047 MERLSQLQRGADQNRLRATDAQQTAGEAGE-----------------------------------QARSAQQAFEQVKQM 1091
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEelaeleekleelkeelesleaeleeleaeleelesRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1092 YAELKRRMEQSPA-LGQQGSRVQSIDLEAQALFEETLAMM-----LRMETLEMEIQESNKALMSKSARLLGLEEQVGRIR 1165
Cdd:TIGR02168 388 VAQLELQIASLNNeIERLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
....*
gi 1803687377 1166 DAINK 1170
Cdd:TIGR02168 468 EELEE 472
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
889-1095 |
2.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 889 EGDLQRIQQFIQQVRNfLSDKdmdPATIQEISESVLSLRlpTDAAAVLRKMTEIQNLATKLQcpesILVQTAEDIAKAKQ 968
Cdd:COG4717 67 ELNLKELKELEEELKE-AEEK---EEEYAELQEELEELE--EELEELEAELEELREELEKLE----KLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 969 LQQEAEQARNRANAVEGNVEEvvgnlrqantvLLEARGAIRGSDSSLRFIQERVDEIEAVLGPA-EKNVKSLAGQLDGLM 1047
Cdd:COG4717 137 LEAELAELPERLEELEERLEE-----------LRELEEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1803687377 1048 ERLSQLQRGADQNRLRATDAQQtAGEAGEQARSAQQAFEQVKQMYAEL 1095
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLL 252
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
900-1137 |
3.15e-04 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 44.28 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 900 QQVRN----FLSDK-DMDPATIQEISESVLSLRLPTDAAAvlrkmtEIQNLATKLQCPESILVQTAEDIAKAKQLQ--QE 972
Cdd:PRK01294 86 RALRDffdyFLSALgELDLAAIDALVEREIAAQLPEPADS------QALDLWLRYKAYLSALAQLEDDGPGKLDLQalQQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 973 AEQARNRANAVEGNVEEVVG-----NLRQANTVlleARGAIRgSDSSLRFIQ--ERVDEIEAVLGPAEKNVKSLAGQLDG 1045
Cdd:PRK01294 160 LLDARLALRARFFSDWEIQAffgeeNQYQRYAL---ERLRIA-QDPSLSDAQkaARLAALEAQLPEDLRAALQESQRQQA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1046 LMERLSQLQ-RGADQNRLRATdAQQTAGEAG----EQARSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLEAQ 1120
Cdd:PRK01294 236 LLQQLAQLQaSGASPQELRLM-RAQLVGPEAaqrlEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQ 314
|
250
....*....|....*..
gi 1803687377 1121 AlFEETLAmmLRMETLE 1137
Cdd:PRK01294 315 R-FSPQEA--LRLAALE 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
884-1110 |
3.41e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 884 TRTQIEGDLQRIQQFIQQVRNFLSdkdmdpATIQEISESVLSLRLPTDAAAVLRKmtEIQNLATKLQCPESILVQTAEDI 963
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELA------ALKKEEKALLKQLAALERRIAALAR--RIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 964 AKA-KQL--QQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAI-----RGSDSSLRFIQERVDEIEAVLGPAEKN 1035
Cdd:COG4942 93 AELrAELeaQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1803687377 1036 VKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQGS 1110
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
958-1128 |
4.62e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 958 QTAEDIAKAKQLQQEAEQARNRANAvegnveevvgnlrqantvlleargairgsdsslrfiqERVDEIEAVLGPAEKNVK 1037
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAEL-------------------------------------DRLQALESELAISRQDYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1038 SLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQspaLGQQGSRVQSIDL 1117
Cdd:pfam00529 100 GATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ---LDQIYVQITQSAA 176
|
170
....*....|.
gi 1803687377 1118 EAQALFEETLA 1128
Cdd:pfam00529 177 ENQAEVRSELS 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1098 |
4.66e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMsvTRTQIEGDLQRIQQFIQQ---VRNFLSDKDMDPATIQEIS 920
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIaaaLLALLGLGGSLLSLILTIA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 921 ESV-LSLRLPTDAAAVLRKMT----------------------EIQNLATKLQCPESI----LVQTAEDIAKAKQLQQEA 973
Cdd:COG4717 277 GVLfLVLGLLALLFLLLAREKaslgkeaeelqalpaleeleeeELEELLAALGLPPDLspeeLLELLDRIEELQELLREA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 974 EQARNRAnAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLD--GLMERLS 1051
Cdd:COG4717 357 EELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELE 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1803687377 1052 QL---------QRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRR 1098
Cdd:COG4717 436 ELeeeleeleeELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
847-1063 |
5.21e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 847 RSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQfIQQVRNFLSDKDMDPATIQ-EISEsvLS 925
Cdd:COG1340 46 DELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDE-LRKELAELNKAGGSIDKLRkEIER--LE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 926 LRLPTdaaAVLRK------MTEIQNLATKLQCPESILVQT---AEDIAKAKQLQQEAEQARNR----ANAVEGNVEEVVG 992
Cdd:COG1340 123 WRQQT---EVLSPeeekelVEKIKELEKELEKAKKALEKNeklKELRAELKELRKEAEEIHKKikelAEEAQELHEEMIE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 993 NLRQANTVLLEARGAIRgsdsSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLR 1063
Cdd:COG1340 200 LYKEADELRKEADELHK----EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
875-1171 |
5.26e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 875 RRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKdmdpatiqeisesvLSLRLPTDAAAvlrkmtEIQNLATKLQCPES 954
Cdd:COG3096 791 RAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGH--------------LAVAFAPDPEA------ELAALRQRRSELER 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 955 ILVQTAEDIakaKQLQQEAEQARNRANAVEGNVEEVvgNLRQANTV---LLEARGAIRGSDSSLRFIQ------ERVDEI 1025
Cdd:COG3096 851 ELAQHRAQE---QQLRQQLDQLKEQLQLLNKLLPQA--NLLADETLadrLEELREELDAAQEAQAFIQqhgkalAQLEPL 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1026 EAVLGPAEKNVKSLAGQLDGLMERLSQLQRGAD------QNR---------------------LRA--TDAQQTAGEAGE 1076
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalsevvQRRphfsyedavgllgensdlnekLRArlEQAEEARREARE 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1077 QARSAQQAFEQV--------------KQMYAELKRRMEqspALGQQGsrvqSIDLEAQAlfeetlammlrmetlEMEIQE 1142
Cdd:COG3096 1006 QLRQAQAQYSQYnqvlaslkssrdakQQTLQELEQELE---ELGVQA----DAEAEERA---------------RIRRDE 1063
|
330 340 350
....*....|....*....|....*....|..
gi 1803687377 1143 SNKALMSKSARLLGLEEQVGRIR---DAINKR 1171
Cdd:COG3096 1064 LHEELSQNRSRRSQLEKQLTRCEaemDSLQKR 1095
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
964-1176 |
6.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 964 AKAKQLQQEaEQARNRANAVEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAvlgpAEKNVKSLAGQL 1043
Cdd:PRK03918 180 RLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1044 DGLMERLSQLQRGADQNRLRATDAQQTAGEAGEqarsaqqaFEQVKQMYAELKRRMEQSpalgqqgsrvqsidLEAQALF 1123
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEY--------------LDELREI 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1803687377 1124 EETLAmmlRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAIN---KRVAYYE 1176
Cdd:PRK03918 313 EKRLS---RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleERHELYE 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
956-1170 |
6.98e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 956 LVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEevvgnLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKN 1035
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRR-----LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1036 VKSLAGQ-LDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQ---GSR 1111
Cdd:COG4913 332 IRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaEAE 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 1112 VQSIDLEAQAlfeetlammlrmETLEMEIQ--ESNKALMskSARLLgleeqvgRIRDAINK 1170
Cdd:COG4913 412 AALRDLRREL------------RELEAEIAslERRKSNI--PARLL-------ALRDALAE 451
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
849-1101 |
7.01e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 849 LSARLRETaqlikttETSANQIQSSTRRLADQMSVTRTQI---EGDLQRIQQfiqqvrnflsDKDMDPATIQEISESVLS 925
Cdd:pfam01576 80 LESRLEEE-------EERSQQLQNEKKKMQQHIQDLEEQLdeeEAARQKLQL----------EKVTTEAKIKKLEEDILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 926 LRLPTDAAAVLRKMTE------IQNLA---------TKLQCP-ESILVQTAEDIAKAKQLQQEAEQARNRANAVEGNVEE 989
Cdd:pfam01576 143 LEDQNSKLSKERKLLEerisefTSNLAeeeekakslSKLKNKhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 990 VVGNLRQAntvLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQlQRGAdqnRLRATDAQQ 1069
Cdd:pfam01576 223 QIAELQAQ---IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES-ERAA---RNKAEKQRR 295
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1803687377 1070 TAGEAGEQARS----------AQQAFE-QVKQMYAELKRRMEQ 1101
Cdd:pfam01576 296 DLGEELEALKTeledtldttaAQQELRsKREQEVTELKKALEE 338
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1029-1176 |
7.05e-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: 42.78 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1029 LGPAEKNVKSLAGQLDGLMERLSQLQRgadqnrlratDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQ 1108
Cdd:pfam06008 42 IEILEKELSSLAQETEELQKKATQTLA----------KAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGEN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803687377 1109 GSRVQSIDLeaQALFEETLAMMLRMETLEMEIQESNKALMSKSARLL--GLEEQVGRIR-------DAINKRVAYYE 1176
Cdd:pfam06008 112 DFALPSSDL--SRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLlsRIQTWFQSPQeenkalaNALRDSLAEYE 186
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
327-377 |
8.92e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 8.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 327 CNCNG---HSTSCHFDpelyrasggasGGVCDgCQHNTEGNNCERCKTNYFRNH 377
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
844-1143 |
9.30e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.47 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMDP-----ATIQE 918
Cdd:COG0840 140 LAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPlrellEVLER 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 919 ISESVLSLRLPTD--------AAAV------LRKM-TEIQNLATKLQCPESILVQTAEDIAK-AKQLQQEAEQARNRANA 982
Cdd:COG0840 220 IAEGDLTVRIDVDskdeigqlADAFnrmienLRELvGQVRESAEQVASASEELAASAEELAAgAEEQAASLEETAAAMEE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 983 VEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQldglMERLSQ---LQRG-AD 1058
Cdd:COG0840 300 LSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGES----SQEIGEivdVIDDiAE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1059 QNRLRATDAqqtAGE---AGEQAR--------------SAQQAFEQVKQMYAELKRR-------MEQSPALGQQGSRVQS 1114
Cdd:COG0840 376 QTNLLALNA---AIEaarAGEAGRgfavvadevrklaeRSAEATKEIEELIEEIQSEteeaveaMEEGSEEVEEGVELVE 452
|
330 340
....*....|....*....|....*....
gi 1803687377 1115 idlEAQALFEETLAMMLRMETLEMEIQES 1143
Cdd:COG0840 453 ---EAGEALEEIVEAVEEVSDLIQEIAAA 478
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
917-1147 |
1.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 917 QEISESVLSLRlpTDAAAVLRKMTEIQNLA-------TKLQCPESIL---VQTAEDiakAKQLQQEAEQARNRANAVEGN 986
Cdd:COG3096 281 RELSERALELR--RELFGARRQLAEEQYRLvemarelEELSARESDLeqdYQAASD---HLNLVQTALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 987 VEEVVGNLRQANTVLLEArgairgsdsslrfiQERVDEIEAVLGPAEKNVKSLAGQLdglmerlsqlqrgADqnRLRATD 1066
Cdd:COG3096 356 LEELTERLEEQEEVVEEA--------------AEQLAEAEARLEAAEEEVDSLKSQL-------------AD--YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1067 AQQTagEAGeQARSAQQAFEQVKQMYAElkrrmeqsPALGQQG--SRVQSIDLEAQALFEETLAMMLRMETLEMEIQESN 1144
Cdd:COG3096 407 VQQT--RAI-QYQQAVQALEKARALCGL--------PDLTPENaeDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFE 475
|
...
gi 1803687377 1145 KAL 1147
Cdd:COG3096 476 KAY 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1171 |
1.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 847 RSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDMDPATiQEISESVLSL 926
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY-EGFLEGVKAA 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 927 RLPTDAAAVLRKMTEIQ----NLATKLQCPESILVQ--TAEDIAKAKQLQQEAEQARN-RANAVEGNVEEVvGNLRQANT 999
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAgRATFLPLDKIRA-RAALAAAL 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1000 VLLEARGAIRGSDSSLRF-----------IQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQ 1068
Cdd:COG1196 593 ARGAIGAAVDLVASDLREadaryyvlgdtLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1069 QTAGEAGEQARSAQQAFEQVKQMYAELKRRMEQSPALGQQ-GSRVQSIDLEAQALFEETLAMMLRMETLEMEIQESNKAL 1147
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAeEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
330 340
....*....|....*....|....
gi 1803687377 1148 MSKSARLLGLEEQVGRIRDAINKR 1171
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREI 776
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
845-1162 |
1.55e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLS---ARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEGDLQRIQQFIQQVRNFLSDKDmdpaTIQEISE 921
Cdd:PRK04863 280 ERRVHLeeaLELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQE----KIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 922 SV--LSLRLpTDAAAVLRKMTEIQ--NLATKLQCPESIL--------VQTAEDIAKAKQLQ-QEAEQARNRANA------ 982
Cdd:PRK04863 356 DLeeLEERL-EEQNEVVEEADEQQeeNEARAEAAEEEVDelksqladYQQALDVQQTRAIQyQQAVQALERAKQlcglpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 983 -----VEGNVEEVVGNLRQANTVLLEARGAIRGSDSSLR-------FIQERVDEIEA---------VLGPAEKNvKSLAG 1041
Cdd:PRK04863 435 ltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfeqayqLVRKIAGEVSRseawdvareLLRRLREQ-RHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1042 QLDGLMERLSQLQRG----ADQNRLRA---------------------------TDAQQTAGEAGEQARSAQQAFEQVKQ 1090
Cdd:PRK04863 514 QLQQLRMRLSELEQRlrqqQRAERLLAefckrlgknlddedeleqlqeelearlESLSESVSEARERRMALRQQLEQLQA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1091 MYAELKRR----MEQSPALGQQGSRVQSIDLEAQALFEETLAMMLRMETLEME---IQESNKALM-----------SKSA 1152
Cdd:PRK04863 594 RIQRLAARapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVErdeLAARKQALDeeierlsqpggSEDP 673
|
410
....*....|
gi 1803687377 1153 RLLGLEEQVG 1162
Cdd:PRK04863 674 RLNALAERFG 683
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
864-1101 |
1.64e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 864 ETSANQiQSSTRRLADQMSVTRtQIEGDLQRIQQFIQQvrNFLSDKDMDPATI---QEISESVLSLRLPTDAAAVLRKMT 940
Cdd:pfam05667 223 EEEWNS-QGLASRLTPEEYRKR-KRTKLLKRIAEQLRS--AALAGTEATSGASrsaQDLAELLSSFSGSSTTDTGLTKGS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 941 --------EIQNLATKLQCPESILVQTAEDIAKAKQ-----LQQEAEQARNRANAVEGNVEEVVGNLRQANTVLLEARGA 1007
Cdd:pfam05667 299 rfthteklQFTNEAPAATSSPPTKVETEEELQQQREeeleeLQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1008 IRGSDSSLRfIQERVDEIeavLGPAEKNVKSLAGQLDGLMERLSQLQ------RGADQNRLRATDAQQT--AGEAGEQAR 1079
Cdd:pfam05667 379 NEELEKQYK-VKKKTLDL---LPDAEENIAKLQALVDASAQRLVELAgqwekhRVPLIEEYRALKEAKSnkEDESQRKLE 454
|
250 260
....*....|....*....|..
gi 1803687377 1080 SAQQAFEQVKQMYAELKRRMEQ 1101
Cdd:pfam05667 455 EIKELREKIKEVAEEAKQKEEL 476
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
845-1118 |
1.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 845 EFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSvtrtQIEGDLQRIQQFIQQVRNFLSDKDmdpATIQEISESVL 924
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQAQ---EELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 925 SLRlptDAAAVLRKmtEIQNLATKLQCPESILVQTAEDIA----KAKQLQQEAEQARNRANAVEGNVEEV-VGNLRQA-N 998
Cdd:COG4372 112 ELQ---EELEELQK--ERQDLEQQRKQLEAQIAELQSEIAereeELKELEEQLESLQEELAALEQELQALsEAEAEQAlD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 999 TVLLEARGAIRGSDSSLRFIQERVDE-IEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQTAGEAGEQ 1077
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLpRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1803687377 1078 ARSAQQAFEQVKQMYAELKRRMEQSPALGQQGSRVQSIDLE 1118
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1173 |
2.97e-03 |
|
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: 41.97 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 963 IAKAKQLQQEAEQARNRANA----VEGNVEEVVGNLrqaNTVLLEARGAIRgsdssLRFIQERVDEIEavlgpaeknvKS 1038
Cdd:TIGR02168 167 ISKYKERRKETERKLERTREnldrLEDILNELERQL---KSLERQAEKAER-----YKELKAELRELE----------LA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1039 LAGQldglmeRLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQAFEQVKQMYAELKRRMEqspalgqqgsrvqsidlE 1118
Cdd:TIGR02168 229 LLVL------RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE-----------------E 285
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1803687377 1119 AQALFEETLAMMLRMETLEMEIQESNKALMSKSARLLGLEEQVGRIRDAINKRVA 1173
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
854-1040 |
3.17e-03 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 40.30 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 854 RETAQLIKTTETSANQIQSSTRRLADQMSvtrtQIEGDLQRIQQFIQqvrnflsdkdmdpaTIQEISE--SVLSLRLPTD 931
Cdd:cd11386 29 EKGREAAEDAINQMNQIDESVDEAVSAVE----ELEESSAEIGEIVE--------------VIDDIAEqtNLLALNAAIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 932 AA---------AVLRKmtEIQNLATKLQcpesilvQTAEDIAK-AKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTVL 1001
Cdd:cd11386 91 AArageagrgfAVVAD--EVRKLAEESA-------EAAKEIEElIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAF 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1803687377 1002 LEARGAIRGSDSSLRFIQERVDEIEAVlgpAEKNVKSLA 1040
Cdd:cd11386 162 EEIVASVEEVADGIQEISAATQEQSAS---TQEIAAAVE 197
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1046-1146 |
3.19e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1046 LMERLSQLQRGADQNRLRATDAQQTAGEAGEQARSAQQA---FEQVKQMYAELKRRMEQSpALGQQGSRVQsidLEAQAL 1122
Cdd:pfam20492 11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEES-AEMEAEEKEQ---LEAELA 86
|
90 100
....*....|....*....|....
gi 1803687377 1123 fEETLAMMLRMETLEMEIQESNKA 1146
Cdd:pfam20492 87 -EAQEEIARLEEEVERKEEEARRL 109
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
858-1128 |
5.18e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 858 QLIKTTETSANQIQSSTRRladQMSVTRTQIegdlQRIqqfiqqvrnflsdkdmdpatIQEISESVLSLRLPTDAAAVLR 937
Cdd:NF041483 76 QLLRNAQIQADQLRADAER---ELRDARAQT----QRI--------------------LQEHAEHQARLQAELHTEAVQR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 938 KMTEIQNLATKLQCPESilvQTAEDIAKAKQLQQEAE-QARNRANAVEGNVEEVVGNLR-QANTVLLEARGAIRGSDSSL 1015
Cdd:NF041483 129 RQQLDQELAERRQTVES---HVNENVAWAEQLRARTEsQARRLLDESRAEAEQALAAARaEAERLAEEARQRLGSEAESA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1016 RfiqervDEIEAVLGPAEKNVkslagqldglmERLsqlqrgadqnrLRATDAQ-QTAGEAGEQARSAQQA-FEQVKQMYA 1093
Cdd:NF041483 206 R------AEAEAILRRARKDA-----------ERL-----------LNAASTQaQEATDHAEQLRSSTAAeSDQARRQAA 257
|
250 260 270
....*....|....*....|....*....|....*
gi 1803687377 1094 ELKRRMEQSPALGQQGSRvqsidlEAQALFEETLA 1128
Cdd:NF041483 258 ELSRAAEQRMQEAEEALR------EARAEAEKVVA 286
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
927-1066 |
6.83e-03 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 38.58 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 927 RLPTDAAAVLRKMTEIQNLATKLQCPESILVQTAEDIAKAkqlQQEAEQARNRANAVEGNVEE--------VVGNLRQAN 998
Cdd:pfam09486 2 RASAWRTLVERRTRRYQRLRAELEAARAALAQAEAALAAA---QAQAEQARDRVRAHEERLDDlttggspfSAADYLACR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803687377 999 TVLLEARGAIRGSDSSLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATD 1066
Cdd:pfam09486 79 AYRDVLEGRVGAAEAALAAARQALDAAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERAREDAAD 146
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
851-1090 |
6.96e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 39.59 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 851 ARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRtQIEGDLQRIQQfiqqvrnflSDKDMDPATIQEISESVLSLRLPT 930
Cdd:pfam12795 20 QDLQQALSLLDKIDASKQRAAAYQKALDDAPAELR-ELRQELAALQA---------KAEAAPKEILASLSLEELEQRLLQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 931 DAAAVLRKMTEIQNLATKLQCPESILVQTAEDIAKAKQLQQEAEQARNrANAVEGNVeevvgnLRQANTVLLEARgairg 1010
Cdd:pfam12795 90 TSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLN-GPAPPGEP------LSEAQRWALQAE----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1011 sdssLRFIQERVDEIEAVLGPAEKNVKSLAGQLDGLMERLSQLQRGAD-----QNRLRATDAQQTAGEAGEQARSAQQAF 1085
Cdd:pfam12795 158 ----LAALKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQalqelLNEKRLQEAEQAVAQTEQLAEEAAGDH 233
|
....*
gi 1803687377 1086 EQVKQ 1090
Cdd:pfam12795 234 PLVQQ 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
844-1032 |
8.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 844 REFRSLSARLRETAQLIKTTETSANQIQSSTRRLADQMSVTRTQIEG----DLQRIQQFIQQVRNFLSDKDMDPATIQEI 919
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 920 SESvLSLRLPTDAAAVLRKMTEIQNLATKLqcpESILVQTAEDIAKAK-----------QLQQEAEQARNRANAVEGNVE 988
Cdd:COG4913 368 LAA-LGLPLPASAEEFAALRAEAAALLEAL---EEELEALEEALAEAEaalrdlrrelrELEAEIASLERRKSNIPARLL 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1803687377 989 EVVGNLRQantvlleargAIRGSDSSLRF----IQERVDE------IEAVLGPA 1032
Cdd:COG4913 444 ALRDALAE----------ALGLDEAELPFvgelIEVRPEEerwrgaIERVLGGF 487
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
861-1152 |
8.76e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.19 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 861 KTTETSANQIQSSTRRLADQMSvtrtQIEGDLQRIQQFIQQVRNFLSDKDMDPATIQEISESVLSLRLPTDA------AA 934
Cdd:pfam10174 450 RIIERLKEQREREDRERLEELE----SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSklksleIA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 935 VLRKMTEIQNLATKLQCPESI--LVQTAEDIA-KAKQLQQEAEQARNRANAVEGNVEEVVGNLRQANTvlleargairgs 1011
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAeeAVRTNPEINdRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN------------ 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803687377 1012 DSSLRfiQERVDEIEAVLG-----PAEKNVKSLAGQLDGLMERLSQLQRGADQNRLRATDAQQtageagEQARSAQQAFE 1086
Cdd:pfam10174 594 EKNDK--DKKIAELESLTLrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ------LQLEELMGALE 665
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803687377 1087 QVKQMYAELKRR---MEQSpaLGQQGSRVQSIDLEAQALFEETLAMmlRMETLEMEIQE--SNKALMSKSA 1152
Cdd:pfam10174 666 KTRQELDATKARlssTQQS--LAEKDGHLTNLRAERRKQLEEILEM--KQEALLAAISEkdANIALLELSS 732
|
|
| |
