|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
45-285 |
4.63e-121 |
|
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: 379.40 E-value: 4.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 45 TRQPQRCVPDFVNAAFNLEVQVTNTCGTKRPTKFCVQSGHTGQRSVCETCDDRHEGFSHPAKYLTDFNVGNNETWWQSDT 124
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 125 MQEGQQYpttTNLTLVLGKSFDITYVRLKFISPRPeSFTIYKKTHTDSEWEPWQFYSGSCRATYGLSDRAPILPGNEATA 204
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKGNEDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 205 QCTKEFSDISPITGGNIAFSTLEGRPSAHAFEESEVLQKWVTASAIRISLNRMNTFGDEVFKD-PQVLRSYYYAISDFAV 283
Cdd:smart00136 157 ICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIAV 236
|
..
gi 392926425 284 GG 285
Cdd:smart00136 237 GG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
51-285 |
2.23e-107 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 341.10 E-value: 2.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 51 CVPDFVNAAFNLEVQVTNTCGTKRPTKFCVQSGHTGQRSvCETCDDRHEGFSHPAKYLTDFNVGNNETWWQSDTMQEGQQ 130
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGKK-CFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVIQYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 131 YpttTNLTLVLGKSFDITYVRLKFISPRPESFTIYKKTHTDSEWEPWQFYSGSCRATYGLSDRAPiLPGNEATAQCTKEF 210
Cdd:pfam00055 80 N---VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPS-RGIKDDEVICTSEY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926425 211 SDISPITGGNIAFSTLEGRPSAHAFEESEVLQKWVTASAIRISLNRMNTFGDEVFKDPQVLRSYYYAISDFAVGG 285
Cdd:pfam00055 156 SDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
560-684 |
3.31e-38 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 139.32 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 560 DNSPVYFVAPEQFLGDQRSSYNQDLVFTLKVAK---HVTNQDvKDIIIVGADrqeLSTSITAQGNPFPTTEAQ-TYRFRV 635
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGrrgGTHVSA-PDVILEGNG---LRISHPAEGPPLPDELTTvEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 392926425 636 HADPYFGWYPRINElDFIGILSNITAIKIRGTYSYKDIG-YLSNVNLGTA 684
Cdd:smart00281 77 ENWQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVA 125
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
565-700 |
4.85e-27 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 107.74 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 565 YFVAPEQFLGDQRSSYNQDLVFTLKV---AKHVTNQDVKDIIIVGADRQeLSTSITAQGNPFPTTEaQTYRFRVHADpyf 641
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYeplPGGGSLNSEPDVILEGNGLR-LSYSSPDQPPPDPGQE-QTYSVRLHEE--- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926425 642 GWYPR----INELDFIGILSNITAIKIRGTYSYKDIG-YLSNVNLGTAGVAPSaanPKQATWIE 700
Cdd:pfam00052 76 NWRDSdgapVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
946-991 |
4.92e-17 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 76.20 E-value: 4.92e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 392926425 946 CNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFSANGC 991
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
946-994 |
3.15e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.93 E-value: 3.15e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 946 CNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFSANGCQPC 994
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
946-992 |
2.32e-15 |
|
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: 71.62 E-value: 2.32e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 946 CNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFS--ANGCQ 992
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1087-1617 |
6.43e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1087 ETSRAASEVWEAVKQKTKEgggTIKTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENV 1166
Cdd:COG1196 252 EAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1167 LHYLETEGEERAQIA---YNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAIYGGEQ 1243
Cdd:COG1196 329 EEELEELEEELEELEeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1244 IS---KQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRNDVAGVLEESENLVDS 1320
Cdd:COG1196 409 EEallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1321 SV------KENSANDELFDEvnrSVADARNELQSSQDQQRVSDQLMLELEKSRE-RIVDSVSTADKTLKDAEAALQVLEE 1393
Cdd:COG1196 489 AAarllllLEAEADYEGFLE---GVKAALLLAGLRGLAGAVAVLIGVEAAYEAAlEAALAAALQNIVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1394 fgakiEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRD 1473
Cdd:COG1196 566 -----LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1474 STEAVQYDIEQLMEELTDSNEnlqyyKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEEVNN 1553
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGS-----LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926425 1554 AELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNL 1617
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
993-1041 |
3.11e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.45 E-value: 3.11e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 993 PCDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGITQGCLPC 1041
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
403-447 |
4.51e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.03 E-value: 4.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 392926425 403 CGCNEIGSLSTQCDNE-GKCQCKPGVTGRFCDQCLDGFYDFSTNGC 447
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
994-1038 |
2.97e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 2.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 392926425 994 CDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGIT-QGC 1038
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGpPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
403-450 |
6.91e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 6.91e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 403 CGCNEIGSLSTQCD-NEGKCQCKPGVTGRFCDQCLDGFYDFSTNGCKNC 450
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
402-448 |
8.20e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 8.20e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392926425 402 ACGCNEIGSLSTQCDNE-GKCQCKPGVTGRFCDQCLDGFYDFST--NGCK 448
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1080-1617 |
1.10e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1080 KFDEKVKETSRAASEVwEAVKQKTKEGGGTIKTKSKAIKDEIVAALEKLTSIDEsvAQAKVGADAAE-NDMKRWEIIIEN 1158
Cdd:TIGR02168 233 RLEELREELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE--LQKELYALANEiSRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1159 ARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELA---SGTREEAEKHLKQASEIEQLSEQAIANATQANKEAS 1235
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1236 DAIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANnlaavsltnVEAVKIPSVDPKELRNDVAGVLEESE 1315
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1316 NLVDSSVKENSANDELFDEVNRSVADARNELQSSQD-QQRVSD--QLMLELEKSRERI------------VDS-----VS 1375
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLEGfsEGVKALLKNQSGLsgilgvlselisVDEgyeaaIE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1376 TA---------DKTLKDAEAALQVLEE--------------FGAKIEKSRNDAVAEFAGVEGINQRL------------- 1419
Cdd:TIGR02168 541 AAlggrlqavvVENLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLvkfdpklrkalsy 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1420 --------DDIIDAQDKRRNSLP-----------IDKQFVIdYRKSAD---VLLNETHALADRYKDIIHSDVDTRDSTEA 1477
Cdd:TIGR02168 621 llggvlvvDDLDNALELAKKLRPgyrivtldgdlVRPGGVI-TGGSAKtnsSILERRREIEELEEKIEELEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1478 VQyDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEEVNNAELD 1557
Cdd:TIGR02168 700 LA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926425 1558 ELEEEIDRLDQLLAQAQ------------LAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNL 1617
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKeelkalrealdeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
994-1044 |
2.30e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 2.30e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 392926425 994 CDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGITQGclPCDDC 1044
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD--PPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
736-783 |
7.11e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 7.11e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 392926425 736 CDCHNH---SNSCEAESGSCICEHNTAGDTCERCARGYYGDALQGteEDCQ 783
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1087-1614 |
1.38e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1087 ETSRAASEVWEAVKQKTKEGGGTIKTKSKAikDEIVAALEKLTSIDES---VAQAKVGADAAENDMKRWEIIIENARREI 1163
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1164 ENVLHYLEtEGEERAQiaynASQKYGEQSKRMSELASGTREEAEK--HLKQASEIEQLSEQAIANATQANKEASDAIYGG 1241
Cdd:PTZ00121 1353 EAAADEAE-AAEEKAE----AAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1242 EQIsKQIAELKEKQNQLNEsihrtldlAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRNDVAGVL----EESENL 1317
Cdd:PTZ00121 1428 EEK-KKADEAKKKAEEAKK--------ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKK 1498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1318 VDSSVKENSANDELfDEVNRSVADARNELQSSQDQQRVSDqlmlELEKSRE-RIVDSVSTADKtLKDAEAALQVleEFGA 1396
Cdd:PTZ00121 1499 ADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKAD----EAKKAEEkKKADELKKAEE-LKKAEEKKKA--EEAK 1570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1397 KIEKSRNDAVaefagveginQRLDDIIDAQDKRRNSlpIDKQFVIDYRKSADVLLNETHAladRYKdiihsdVDTRDSTE 1476
Cdd:PTZ00121 1571 KAEEDKNMAL----------RKAEEAKKAEEARIEE--VMKLYEEEKKMKAEEAKKAEEA---KIK------AEELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1477 AVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANAtilAEEDEIKKIINSLDTMEEVNNAel 1556
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK---AEEDEKKAAEALKKEAEEAKKA-- 1704
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926425 1557 deleeeidrlDQLlaQAQLAKEVPTYQQYRADEDV---KVAQLKNDISELQKEVlnlEEIR 1614
Cdd:PTZ00121 1705 ----------EEL--KKKEAEEKKKAEELKKAEEEnkiKAEEAKKEAEEDKKKA---EEAK 1750
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
736-777 |
1.98e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 1.98e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 392926425 736 CDCH---NHSNSCEAESGSCICEHNTAGDTCERCARGYYGDALQG 777
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
889-944 |
4.00e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 4.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 392926425 889 SCGCFAAGTRRPnndytllECNQQDGQCDCLPNVIGIQCDQCAHGFYNITS-GLGCQ 944
Cdd:cd00055 1 PCDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1163-1388 |
4.61e-09 |
|
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: 58.96 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1163 IENVLHYLEtegEERAQIAYNASQKYGeQSKRMSELASGTR---EEAEKHLKQASEIEQLSEQAIANATQANKEASDAIY 1239
Cdd:pfam06008 21 LENLTKQLQ---EYLSPENAHKIQIEI-LEKELSSLAQETEelqKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1240 GGEQISKQIAELKEKQNQL-NESIHRTLDLAE---EQKKSADEANNLAAVSLTNVEAVKIPSvdpkELRNDVAGVLEESE 1315
Cdd:pfam06008 97 NIKEINEKVATLGENDFALpSSDLSRMLAEAQrmlGEIRSRDFGTQLQNAEAELKAAQDLLS----RIQTWFQSPQEENK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1316 NLvdssvkENSANDELfDEVNRSVADARNELQSSQDQQRVSDQLML-------ELEKSRERIVDSVSTADKTLKDAEAAL 1388
Cdd:pfam06008 173 AL------ANALRDSL-AEYEAKLSDLRELLREAAAKTRDANRLNLanqanlrEFQRKKEEVSEQKNQLEETLKTARDSL 245
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
736-782 |
7.38e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.38e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392926425 736 CDCHNH---SNSCEAESGSCICEHNTAGDTCERCARGYYGDAlQGTEEDC 782
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
890-943 |
1.35e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 392926425 890 CGCFAAGTRRPnndytllECNQQDGQCDCLPNVIGIQCDQCAHGFYNItSGLGC 943
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
890-943 |
4.10e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 4.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 890 CGCFAAGTRRPNndytlleCNQQDGQCDCLPNVIGIQCDQCAHGFYN--ITSGLGC 943
Cdd:pfam00053 1 CDCNPHGSLSDT-------CDPETGQCLCKPGVTGRHCDRCKPGYYGlpSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-337 |
4.68e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 4.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392926425 286 RCKCNGHASECVGSSSVDGenrlVCRCEHNTQGADCNECLPFYNDRPWRSGT 337
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
835-890 |
1.86e-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: 46.19 E-value: 1.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 835 CACSGNTDPNsiGNCDKITGECKkCIFNTHGFNCENCKPGYWGDaliePKGNCQSC 890
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGL----PSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
835-888 |
4.38e-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: 45.04 E-value: 4.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 392926425 835 CACSGNTDPNsiGNCDKITGECKkCIFNTHGFNCENCKPGYWGDALIepKGNCQ 888
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1048-1262 |
1.08e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.82 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1048 IQSRVNVFREKVKSLDNTLQEIIENPAPVNDTKfdEKVKETSRAASEVWEAVKQKTKEGGGTIKTKSKAIKD--EIVAAL 1125
Cdd:smart00283 16 QAEELEELAERMEELSASIEEVAANADEIAATA--QSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEEleESSDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1126 EKLTS-IDESVAQ------------AKVG--------------------ADAAEndmkrwEI--IIENARREIENVLHYL 1170
Cdd:smart00283 94 GEIVSvIDDIADQtnllalnaaieaARAGeagrgfavvadevrklaersAESAK------EIesLIKEIQEETNEAVAAM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1171 E---TEGEERAQIAYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSeQAIANATQANKEASDAIyggEQISKQ 1247
Cdd:smart00283 168 EessSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVN-AAIDEIAQVTQETAAMS---EEISAA 243
|
250
....*....|....*
gi 392926425 1248 IAELKEKQNQLNESI 1262
Cdd:smart00283 244 AEELSGLAEELDELV 258
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
785-833 |
2.24e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 2.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392926425 785 CPCPNDGPCILHAD-GDVICtECPNGYTGRRCDECSDGYFGNPKDGTECV 833
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1083-1526 |
7.40e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.90 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1083 EKVKETSRAASEVWEAVK--QKTKEgggtikTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEI--IIEN 1158
Cdd:NF041483 608 EAAEETERLRTEAAERIRtlQAQAE------QEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAqeSADR 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1159 ARREIENVLHYLETEGEEraqiAYNASQKYGEQSKRMSE-LASGTREEAEKHLKQASE------------IEQLSEQAIA 1225
Cdd:NF041483 682 VRAEAAAAAERVGTEAAE----ALAAAQEEAARRRREAEeTLGSARAEADQERERAREqseellasarkrVEEAQAEAQR 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1226 NATQANKEASDAIYGGEQISKQI----AELKEKQNQ--------LNESIHRT------------LDLAEEQKKSADEANN 1281
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQVrdsvAGLQEQAEEeiaglrsaAEHAAERTrteaqeeadrvrSDAYAERERASEDANR 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1282 LAAVSLTNVEAVKIPSvdpkelRNDVAGVLEESENL-VDSSVKENSANDELFDEV-------NRSVADAR---NELQSSQ 1350
Cdd:NF041483 838 LRREAQEETEAAKALA------ERTVSEAIAEAERLrSDASEYAQRVRTEASDTLasaeqdaARTRADARedaNRIRSDA 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1351 DQQrvSDQLMLELEKSRERIVDSVSTADKTLKD--AEAALQVLEEFGAKIEKSRNDAVAEfagvegiNQRL-----DDII 1423
Cdd:NF041483 912 AAQ--ADRLIGEATSEAERLTAEARAEAERLRDeaRAEAERVRADAAAQAEQLIAEATGE-------AERLraeaaETVG 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1424 DAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRDSTEAVQYDieQLMEELTDSNENL------Q 1497
Cdd:NF041483 983 SAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQAD--TLITEAAAEADQLtakaqeE 1060
|
490 500 510
....*....|....*....|....*....|....*....
gi 392926425 1498 YYKKQAEDDKQMAT-------EAVR---KATLAKNSAIE 1526
Cdd:NF041483 1061 ALRTTTEAEAQADTmvgaarkEAERivaEATVEGNSLVE 1099
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
1083-1293 |
7.82e-05 |
|
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: 45.31 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1083 EKVKETSRAASEVWEAVKQKTKegggtiktKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARR- 1161
Cdd:cd11386 5 ASIEEVAASADQVAETSQQAAE--------LAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1162 -EIENVLhyletegeeraqiAYNAS---QKYGEQSKRMSELASGTREEAEKHLKQASEIEQL---SEQAIANATQANKEA 1234
Cdd:cd11386 77 aEQTNLL-------------ALNAAieaARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeIQEQTEEAVEAMEET 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392926425 1235 SDAIyggEQISKQIAELKEkqnQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAV 1293
Cdd:cd11386 144 SEEV---EEGVELVEETGR---AFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
835-878 |
9.12e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 9.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 392926425 835 CACsgNTDPNSIGNCDKITGECKkCIFNTHGFNCENCKPGYWGD 878
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
287-338 |
1.20e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.18 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392926425 287 CKCNGHASECVGSSSVDGenrlVCRCEHNTQGADCNECLPFYNDRPWRSGTS 338
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG----QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
347-405 |
4.21e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926425 347 CNCSQ---LSNRCYFdqqlfeetgHGGHCiDCQGNTQGVHCEQCIANHWRRPGENycvACGC 405
Cdd:pfam00053 1 CDCNPhgsLSDTCDP---------ETGQC-LCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
785-828 |
2.34e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.33 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 392926425 785 CPCPNDGP----CILHadgDVICtECPNGYTGRRCDECSDGYFGNPKD 828
Cdd:pfam00053 1 CDCNPHGSlsdtCDPE---TGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
785-829 |
3.51e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 785 CPCPNDG----PCILHadgDVICtECPNGYTGRRCDECSDGYFGNPKDG 829
Cdd:smart00180 1 CDCDPGGsasgTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
45-285 |
4.63e-121 |
|
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: 379.40 E-value: 4.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 45 TRQPQRCVPDFVNAAFNLEVQVTNTCGTKRPTKFCVQSGHTGQRSVCETCDDRHEGFSHPAKYLTDFNVGNNETWWQSDT 124
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 125 MQEGQQYpttTNLTLVLGKSFDITYVRLKFISPRPeSFTIYKKTHTDSEWEPWQFYSGSCRATYGLSDRAPILPGNEATA 204
Cdd:smart00136 81 LSNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKGNEDEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 205 QCTKEFSDISPITGGNIAFSTLEGRPSAHAFEESEVLQKWVTASAIRISLNRMNTFGDEVFKD-PQVLRSYYYAISDFAV 283
Cdd:smart00136 157 ICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIAV 236
|
..
gi 392926425 284 GG 285
Cdd:smart00136 237 GG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
51-285 |
2.23e-107 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 341.10 E-value: 2.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 51 CVPDFVNAAFNLEVQVTNTCGTKRPTKFCVQSGHTGQRSvCETCDDRHEGFSHPAKYLTDFNVGNNETWWQSDTMQEGQQ 130
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGKK-CFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVIQYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 131 YpttTNLTLVLGKSFDITYVRLKFISPRPESFTIYKKTHTDSEWEPWQFYSGSCRATYGLSDRAPiLPGNEATAQCTKEF 210
Cdd:pfam00055 80 N---VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPS-RGIKDDEVICTSEY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926425 211 SDISPITGGNIAFSTLEGRPSAHAFEESEVLQKWVTASAIRISLNRMNTFGDEVFKDPQVLRSYYYAISDFAVGG 285
Cdd:pfam00055 156 SDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
560-684 |
3.31e-38 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 139.32 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 560 DNSPVYFVAPEQFLGDQRSSYNQDLVFTLKVAK---HVTNQDvKDIIIVGADrqeLSTSITAQGNPFPTTEAQ-TYRFRV 635
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGrrgGTHVSA-PDVILEGNG---LRISHPAEGPPLPDELTTvEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 392926425 636 HADPYFGWYPRINElDFIGILSNITAIKIRGTYSYKDIG-YLSNVNLGTA 684
Cdd:smart00281 77 ENWQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVA 125
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
565-700 |
4.85e-27 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 107.74 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 565 YFVAPEQFLGDQRSSYNQDLVFTLKV---AKHVTNQDVKDIIIVGADRQeLSTSITAQGNPFPTTEaQTYRFRVHADpyf 641
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYeplPGGGSLNSEPDVILEGNGLR-LSYSSPDQPPPDPGQE-QTYSVRLHEE--- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926425 642 GWYPR----INELDFIGILSNITAIKIRGTYSYKDIG-YLSNVNLGTAGVAPSaanPKQATWIE 700
Cdd:pfam00052 76 NWRDSdgapVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPGGS---GPPASWVE 136
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
946-991 |
4.92e-17 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 76.20 E-value: 4.92e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 392926425 946 CNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFSANGC 991
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
946-994 |
3.15e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.93 E-value: 3.15e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 946 CNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFSANGCQPC 994
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
946-992 |
2.32e-15 |
|
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: 71.62 E-value: 2.32e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 946 CNCDPLGSEGNTCDVNTGQCQCKPGVTGQRCDRCADYHFGFS--ANGCQ 992
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsqGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1087-1617 |
6.43e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1087 ETSRAASEVWEAVKQKTKEgggTIKTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENV 1166
Cdd:COG1196 252 EAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1167 LHYLETEGEERAQIA---YNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAIYGGEQ 1243
Cdd:COG1196 329 EEELEELEEELEELEeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1244 IS---KQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRNDVAGVLEESENLVDS 1320
Cdd:COG1196 409 EEallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1321 SV------KENSANDELFDEvnrSVADARNELQSSQDQQRVSDQLMLELEKSRE-RIVDSVSTADKTLKDAEAALQVLEE 1393
Cdd:COG1196 489 AAarllllLEAEADYEGFLE---GVKAALLLAGLRGLAGAVAVLIGVEAAYEAAlEAALAAALQNIVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1394 fgakiEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRD 1473
Cdd:COG1196 566 -----LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1474 STEAVQYDIEQLMEELTDSNEnlqyyKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEEVNN 1553
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGS-----LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926425 1554 AELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNL 1617
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
993-1041 |
3.11e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.45 E-value: 3.11e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 993 PCDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGITQGCLPC 1041
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
403-447 |
4.51e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.03 E-value: 4.51e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 392926425 403 CGCNEIGSLSTQCDNE-GKCQCKPGVTGRFCDQCLDGFYDFSTNGC 447
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
994-1038 |
2.97e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.71 E-value: 2.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 392926425 994 CDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGIT-QGC 1038
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGpPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1120-1617 |
3.96e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1120 EIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENvlhyLETEGEERAQIAYNASQKYGEQSKRMSELA 1199
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1200 SGTREEAEKHLKQASEIEQLSEQAIANATQANKEAsdaiyggEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEA 1279
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELE-------EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1280 NNLAAVSLTNVEAVKIPSVDPKELRNDVAGVLEESENLVDSSVKENSANDEL---FDEVNRSVADARNELQSSQDQQRVS 1356
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1357 DQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEE-------FGAKIEKSRN----------------------DAVA 1407
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEaeadyegFLEGVKAALLlaglrglagavavligveaayeAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1408 EFAGVEGINQRLDDIIDAQD-----KRRNS-----LPIDKQ-------------FVIDYRKSADVLLNETHALADRYKDI 1464
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAaieylKAAKAgratfLPLDKIraraalaaalargAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1465 IHSDVDTRDSTEAVQYDIEQLMEELTD------------SNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATIL 1532
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREvtlegeggsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1533 AEEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEE 1612
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGP 781
|
....*
gi 392926425 1613 IrdNL 1617
Cdd:COG1196 782 V--NL 784
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
403-450 |
6.91e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 6.91e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 403 CGCNEIGSLSTQCD-NEGKCQCKPGVTGRFCDQCLDGFYDFSTNGCKNC 450
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
402-448 |
8.20e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 61.60 E-value: 8.20e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392926425 402 ACGCNEIGSLSTQCDNE-GKCQCKPGVTGRFCDQCLDGFYDFST--NGCK 448
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1080-1617 |
1.10e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1080 KFDEKVKETSRAASEVwEAVKQKTKEGGGTIKTKSKAIKDEIVAALEKLTSIDEsvAQAKVGADAAE-NDMKRWEIIIEN 1158
Cdd:TIGR02168 233 RLEELREELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE--LQKELYALANEiSRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1159 ARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELA---SGTREEAEKHLKQASEIEQLSEQAIANATQANKEAS 1235
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1236 DAIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANnlaavsltnVEAVKIPSVDPKELRNDVAGVLEESE 1315
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1316 NLVDSSVKENSANDELFDEVNRSVADARNELQSSQD-QQRVSD--QLMLELEKSRERI------------VDS-----VS 1375
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLEGfsEGVKALLKNQSGLsgilgvlselisVDEgyeaaIE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1376 TA---------DKTLKDAEAALQVLEE--------------FGAKIEKSRNDAVAEFAGVEGINQRL------------- 1419
Cdd:TIGR02168 541 AAlggrlqavvVENLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLvkfdpklrkalsy 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1420 --------DDIIDAQDKRRNSLP-----------IDKQFVIdYRKSAD---VLLNETHALADRYKDIIHSDVDTRDSTEA 1477
Cdd:TIGR02168 621 llggvlvvDDLDNALELAKKLRPgyrivtldgdlVRPGGVI-TGGSAKtnsSILERRREIEELEEKIEELEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1478 VQyDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEEVNNAELD 1557
Cdd:TIGR02168 700 LA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926425 1558 ELEEEIDRLDQLLAQAQ------------LAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNL 1617
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKeelkalrealdeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1048-1281 |
2.24e-11 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 66.47 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1048 IQSRVNVFREKVKSLDNTLQEIIENPAPVNDTKFD--EKVKETSRAASEVWEAVKQKTKEgggtIKtKSKAIKDEIvaaL 1125
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDElnAQVKELREEAQELREKRDELNEK----VK-ELKEERDEL---N 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1126 EKLTSIDESVAQAKvgADAAENDMKRWEIiiENARREIENVLHYLETEG----EERAQIaynasqkygEQSKRMSELAsg 1201
Cdd:COG1340 85 EKLNELREELDELR--KELAELNKAGGSI--DKLRKEIERLEWRQQTEVlspeEEKELV---------EKIKELEKEL-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1202 trEEAEKHLKQASEIEQLSEQAianaTQANKEASDaiyggeqISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANN 1281
Cdd:COG1340 150 --EKAKKALEKNEKLKELRAEL----KELRKEAEE-------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
994-1044 |
2.30e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 2.30e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 392926425 994 CDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGITQGclPCDDC 1044
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD--PPQGC 49
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1067-1442 |
6.01e-11 |
|
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: 67.29 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1067 QEIIENPAPVNDTKFDEKVKETSRAASEVWEAVKQKTKEG--GGTIKTKSKAIKDEIVAALEKLTSIDESVAQAKVGaDA 1144
Cdd:COG5185 195 LKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEAlkGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLG-EN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1145 AENdMKRWEIIIENARREIENVLHYLEtEGEERAQIAyNASQKYGEQSKRMS---ELASGTREEAEKHLKQASEIEQLSE 1221
Cdd:COG5185 274 AES-SKRLNENANNLIKQFENTKEKIA-EYTKSIDIK-KATESLEEQLAAAEaeqELEESKRETETGIQNLTAEIEQGQE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1222 QAIANATQANKEASDaIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEAnnLAAVSltnvEAVKIPSVDPK 1301
Cdd:COG5185 351 SLTENLEAIKEEIEN-IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEI--LATLE----DTLKAADRQIE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1302 ELRNDVAGvleesenlVDSSVKENS-ANDELFDEVNRSVADARNELQSSQDQQRV----SDQLMLE-LEKSRERIVDSVS 1375
Cdd:COG5185 424 ELQRQIEQ--------ATSSNEEVSkLLNELISELNKVMREADEESQSRLEEAYDeinrSVRSKKEdLNEELTQIESRVS 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926425 1376 TADKTLKDAEAALQVleefgaKIEKSRN--DAVAEFAGVEGINQRLDDIIDAQDKRRNSlpIDKQFVID 1442
Cdd:COG5185 496 TLKATLEKLRAKLER------QLEGVRSklDQVAESLKDFMRARGYAHILALENLIPAS--ELIQASNA 556
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
736-783 |
7.11e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 7.11e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 392926425 736 CDCHNH---SNSCEAESGSCICEHNTAGDTCERCARGYYGDALQGteEDCQ 783
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG--GGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1190-1619 |
1.14e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1190 EQSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAiyggeqiSKQIAELKEKQNQL---NESIHRTL 1266
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-------RKDLARLEAEVEQLeerIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1267 DLAEEQKKSADEANNLAAVSLTNVEAVkipsvdpkelRNDVAGVLEESENLVDSSVKE-NSANDELFDEvNRSVADARNE 1345
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAE----------IEELEAQIEQLKEELKALREAlDELRAELTLL-NEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1346 LQSSQDQqrvsdqlMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVE-GINQRLDDIID 1424
Cdd:TIGR02168 826 LESLERR-------IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEeALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1425 AQDKRRnslpidkqfviDYRKSADVLLNETHALADRykdiiHSDVDTRdsTEAVQYDIEQLMEELTDsnenlqyykkQAE 1504
Cdd:TIGR02168 899 LSEELR-----------ELESKRSELRRELEELREK-----LAQLELR--LEGLEVRIDNLQERLSE----------EYS 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1505 DDKQMATEAVRKATLAKNSAieanatilaeEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLAQaqlakevptyqq 1584
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEA----------RRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQ------------ 1008
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 392926425 1585 yraDEDVK--VAQLKNDISELQKEVLNL-----EEIRDNLPT 1619
Cdd:TIGR02168 1009 ---KEDLTeaKETLEEAIEEIDREARERfkdtfDQVNENFQR 1047
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1172-1626 |
5.66e-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: 64.32 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1172 TEGEERAQIAYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSEQaianATQANKEASDAIyggEQISKQIAEL 1251
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE----LSQELSDASRKI---GEIEKEIEQL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1252 KEKQNQLNESIHrtlDLAEEQKKSADEannlaavsLTNVEAvkipsvdpkELRnDVAGVLEESEnlvdssvkensandel 1331
Cdd:TIGR02169 729 EQEEEKLKERLE---ELEEDLSSLEQE--------IENVKS---------ELK-ELEARIEELE---------------- 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1332 fdEVNRSVADARNELQSSQDQQRV--SDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDavaef 1409
Cdd:TIGR02169 772 --EDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----- 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1410 agveginqrLDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNEthaLADRYKDiIHSDVDTRDST-EAVQYDIEQLMEE 1488
Cdd:TIGR02169 845 ---------LKEQIKSIEKEIENLNGKKEELEEELEELEAALRD---LESRLGD-LKKERDELEAQlRELERKIEELEAQ 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1489 LTDSNENLQYYKKQAEDDKQMATEAVRkatlAKNSAIEANATILAEED---EIKKIINSLDTMEEVNNAELDELEEEIDR 1565
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIED----PKGEDEEIPEEELSLEDvqaELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926425 1566 LDQLlaQAQLAKevptyqqyradedvkvaqLKNDISELQKEVLNLEEIRDNLPTKCFNVIN 1626
Cdd:TIGR02169 988 LDEL--KEKRAK------------------LEEERKAILERIEEYEKKKREVFMEAFEAIN 1028
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1171-1543 |
8.83e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1171 ETEGEERAQIaYNASQKYGEQSKRMSELASGTREEAEkhlKQASEIEQLSEQaiANATQANKEASDaiyggEQISKQIAE 1250
Cdd:COG4372 6 EKVGKARLSL-FGLRPKTGILIAALSEQLRKALFELD---KLQEELEQLREE--LEQAREELEQLE-----EELEQARSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1251 LKEKQNQLNEsihRTLDLAEEQKKSADEANNLAAVSLTNveavkipsvdpKELRNDVAGVLEESENLvdssVKENSANDE 1330
Cdd:COG4372 75 LEQLEEELEE---LNEQLQAAQAELAQAQEELESLQEEA-----------EELQEELEELQKERQDL----EQQRKQLEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1331 LFDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIvdSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFA 1410
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1411 GVEGINQRLDDIidaqDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKD---IIHSDVDTRDSTEAVQYDIEQLME 1487
Cdd:COG4372 215 ELAEELLEAKDS----LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELelaILVEKDTEEEELEIAALELEALEE 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 1488 ELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIIN 1543
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1087-1614 |
1.38e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1087 ETSRAASEVWEAVKQKTKEGGGTIKTKSKAikDEIVAALEKLTSIDES---VAQAKVGADAAENDMKRWEIIIENARREI 1163
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1164 ENVLHYLEtEGEERAQiaynASQKYGEQSKRMSELASGTREEAEK--HLKQASEIEQLSEQAIANATQANKEASDAIYGG 1241
Cdd:PTZ00121 1353 EAAADEAE-AAEEKAE----AAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1242 EQIsKQIAELKEKQNQLNEsihrtldlAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRNDVAGVL----EESENL 1317
Cdd:PTZ00121 1428 EEK-KKADEAKKKAEEAKK--------ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKK 1498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1318 VDSSVKENSANDELfDEVNRSVADARNELQSSQDQQRVSDqlmlELEKSRE-RIVDSVSTADKtLKDAEAALQVleEFGA 1396
Cdd:PTZ00121 1499 ADEAKKAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKAD----EAKKAEEkKKADELKKAEE-LKKAEEKKKA--EEAK 1570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1397 KIEKSRNDAVaefagveginQRLDDIIDAQDKRRNSlpIDKQFVIDYRKSADVLLNETHAladRYKdiihsdVDTRDSTE 1476
Cdd:PTZ00121 1571 KAEEDKNMAL----------RKAEEAKKAEEARIEE--VMKLYEEEKKMKAEEAKKAEEA---KIK------AEELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1477 AVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANAtilAEEDEIKKIINSLDTMEEVNNAel 1556
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK---AEEDEKKAAEALKKEAEEAKKA-- 1704
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926425 1557 deleeeidrlDQLlaQAQLAKEVPTYQQYRADEDV---KVAQLKNDISELQKEVlnlEEIR 1614
Cdd:PTZ00121 1705 ----------EEL--KKKEAEEKKKAEELKKAEEEnkiKAEEAKKEAEEDKKKA---EEAK 1750
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
736-777 |
1.98e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 1.98e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 392926425 736 CDCH---NHSNSCEAESGSCICEHNTAGDTCERCARGYYGDALQG 777
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1120-1620 |
2.44e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1120 EIVAALEKLTSIDESVAQAkVGADAAENDMKRWEIIIENARREIENVLHYLETEGEERAQIAyNASQKYGEQSKRMSELA 1199
Cdd:PRK03918 136 EIDAILESDESREKVVRQI-LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK-EKEKELEEVLREINEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1200 S---GTREEAEKHLKQASEIEQLSEQaIANATQANKEASDAIYGGE----QISKQIAELKEKQNQLNESIHRT------- 1265
Cdd:PRK03918 214 SelpELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEekirELEERIEELKKEIEELEEKVKELkelkeka 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1266 ---LDLAEEQKKSADEANNLaAVSLTNVEavkipsvdpkELRNDVAGVLEESENLVdSSVKENSandELFDEVNRSVada 1342
Cdd:PRK03918 293 eeyIKLSEFYEEYLDELREI-EKRLSRLE----------EEINGIEERIKELEEKE-ERLEELK---KKLKELEKRL--- 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1343 rNELQSSQDQQRVSDQLMLELEKSRERIvdsvstADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDI 1422
Cdd:PRK03918 355 -EELEERHELYEEAKAKKEELERLKKRL------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1423 IDAQDKRRNSLPIDKQfvidyrksadvLLNETHAladryKDIIhsdvdtRDSTEAVQyDIEQLMEELTDSNENLQYYKKQ 1502
Cdd:PRK03918 428 IEELKKAKGKCPVCGR-----------ELTEEHR-----KELL------EEYTAELK-RIEKELKEIEEKERKLRKELRE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1503 AEddkqmateavrkATLAKNSAIEANATILAEEDEIKKIINSLDtMEEVnNAELDELEEEIDRLDQLLAQAQ-LAKEVPt 1581
Cdd:PRK03918 485 LE------------KVLKKESELIKLKELAEQLKELEEKLKKYN-LEEL-EKKAEEYEKLKEKLIKLKGEIKsLKKELE- 549
|
490 500 510
....*....|....*....|....*....|....*....
gi 392926425 1582 yqqyradedvKVAQLKNDISELQKEVLNLEEIRDNLPTK 1620
Cdd:PRK03918 550 ----------KLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1207-1553 |
2.79e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.07 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1207 EKHLKQASEIEQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANnlaavs 1286
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1287 ltnveavkipsvdpKELRndvagvlEESENLVDSSVKENSANDELfDEVNRSVADARNELQSSQDQQRVSDQLMLELEKS 1366
Cdd:COG4372 80 --------------EELE-------ELNEQLQAAQAELAQAQEEL-ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1367 RERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAgvegiNQRLDDIIDAQDKRRNSLPIDKQFVIDYRKS 1446
Cdd:COG4372 138 IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA-----EQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1447 ADVLLNEthALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIE 1526
Cdd:COG4372 213 PRELAEE--LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
330 340
....*....|....*....|....*..
gi 392926425 1527 ANATILAEEDEIKKIINSLDTMEEVNN 1553
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDAL 317
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1048-1572 |
2.95e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1048 IQSRVNVFREKVKSLDNTLQEIIENpapvndtkfDEKVKETSRAASEVwEAVKQKTKEGGGTIKTKSKAIKDEIVAALEK 1127
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARL---------EERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1128 LTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLhylETEGEERAQIAYNASQKYGEQsKRMSELASGTREEAE 1207
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL---RAAAELAAQLEELEEAEEALL-ERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1208 KHLKQASEIEQLSEQAIANATQANKEASDAiyggEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSL 1287
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEE----EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1288 TNVEAVKIPSVDPKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQDQQ----------RVSD 1357
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratflpldKIRA 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1358 QLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEF--GAKIEKSRNDAVAEFAgvEGINQRLDDIIDAQDKRRNSLPI 1435
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTllGRTLVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1436 DKQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVR 1515
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926425 1516 KATLAKNSAIEANATILAEEDEIKKIINSL----DTMEEVNNAELDELEEEIDRLDQLLAQ 1572
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLereiEALGPVNLLAIEEYEELEERYDFLSEQ 803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1042-1626 |
3.50e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1042 DDCYTLIQSRVNVFREKVKSLDnTLQEIIENPAPVNDTKFDEKVKETSRAASEVWEAVKQKTKEgggtiKTKSKAIKDEI 1121
Cdd:TIGR04523 60 DKNLNKDEEKINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL-----EVELNKLEKQK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1122 VAALEKLTSIDESVAQAKVGADAAENDMKRweiiIENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELASG 1201
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYND----LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1202 TreeaEKHLKQASEIEQLSEQAIANATQANKEASDaiyggeqISKQIAELKEKQNQLN----ESIHRTLDLAEEQKKSad 1277
Cdd:TIGR04523 210 I----QKNKSLESQISELKKQNNQLKDNIEKKQQE-------INEKTTEISNTQTQLNqlkdEQNKIKKQLSEKQKEL-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1278 EANNLAAVSLTN------VEAVKIPSVDPKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQD 1351
Cdd:TIGR04523 277 EQNNKKIKELEKqlnqlkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1352 QQRVSDQlmlELEKSRERIvdsvstaDKTLKDAEAALQVLEefgaKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRN 1431
Cdd:TIGR04523 357 ENSEKQR---ELEEKQNEI-------EKLKKENQSYKQEIK----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1432 SL--PID--KQFVIDYRKSADVLLNETHALA------DRYKDIIHSDVDT-RDSTEAVQYDIEQLMEELTDSNENLQYYK 1500
Cdd:TIGR04523 423 LLekEIErlKETIIKNNSEIKDLTNQDSVKEliiknlDNTRESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1501 KQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKiinsldtmeevnnaeldeLEEEIDRLDQLLAQAQLAKEVP 1580
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD------------------LEDELNKDDFELKKENLEKEID 564
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 392926425 1581 TYQQyradedvKVAQLKNDISELQKEVLNLEEIRDNLPTKCFNVIN 1626
Cdd:TIGR04523 565 EKNK-------EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
889-944 |
4.00e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 4.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 392926425 889 SCGCFAAGTRRPnndytllECNQQDGQCDCLPNVIGIQCDQCAHGFYNITS-GLGCQ 944
Cdd:cd00055 1 PCDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1082-1597 |
4.57e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1082 DEKVKETSRAASEVWEAVKQKTKEGGGTIKTKSKAIkdEIVAALEKLTSIDESVAQAkvgADAAENDMKRWEIIIENARR 1161
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE--EVRKAEELRKAEDARKAEA---ARKAEEERKAEEARKAEDAK 1224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1162 EIENVLHYLETEGEE----RAQIAYNASQKYGEQSKRMSELASGTR----EEAEK--HLKQASEIEQLSE----QAIANA 1227
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAeeakKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKadELKKAEEKKKADEakkaEEKKKA 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1228 TQANKEASDAiYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKElRNDV 1307
Cdd:PTZ00121 1305 DEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK-KADA 1382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1308 AGVLEESENLVDSSVKENSANDELFDEVNRSVADAR--NELQSSQDQQRVSDQLMLELEKSRE-----RIVDSVSTADKT 1380
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKadeakKKAEEAKKAEEA 1462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1381 LKDAEAALQVlEEFGAKIEKSRNDAVAEfAGVEGINQRLDDIIDAQDKRRNSLPIDKqfVIDYRKSADVLLNETHALADr 1460
Cdd:PTZ00121 1463 KKKAEEAKKA-DEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKAD- 1537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1461 ykdiihsdvDTRDSTEAVQYDIEQLMEELTDSNENLQY-YKKQAEDDKQMAteaVRKATLAKNsaieanatilAEEDEIK 1539
Cdd:PTZ00121 1538 ---------EAKKAEEKKKADELKKAEELKKAEEKKKAeEAKKAEEDKNMA---LRKAEEAKK----------AEEARIE 1595
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 392926425 1540 KIINSLDTMEEVNNAELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLK 1597
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1163-1388 |
4.61e-09 |
|
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: 58.96 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1163 IENVLHYLEtegEERAQIAYNASQKYGeQSKRMSELASGTR---EEAEKHLKQASEIEQLSEQAIANATQANKEASDAIY 1239
Cdd:pfam06008 21 LENLTKQLQ---EYLSPENAHKIQIEI-LEKELSSLAQETEelqKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1240 GGEQISKQIAELKEKQNQL-NESIHRTLDLAE---EQKKSADEANNLAAVSLTNVEAVKIPSvdpkELRNDVAGVLEESE 1315
Cdd:pfam06008 97 NIKEINEKVATLGENDFALpSSDLSRMLAEAQrmlGEIRSRDFGTQLQNAEAELKAAQDLLS----RIQTWFQSPQEENK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1316 NLvdssvkENSANDELfDEVNRSVADARNELQSSQDQQRVSDQLML-------ELEKSRERIVDSVSTADKTLKDAEAAL 1388
Cdd:pfam06008 173 AL------ANALRDSL-AEYEAKLSDLRELLREAAAKTRDANRLNLanqanlrEFQRKKEEVSEQKNQLEETLKTARDSL 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1142-1537 |
5.05e-09 |
|
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: 61.24 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1142 ADAAENDMKrweiiIENARREIENVlhyleTEGEERAQIaynasqKYGEQSKRMSELaSGTREEAEKHLKQASEIEQLSE 1221
Cdd:TIGR02169 163 AGVAEFDRK-----KEKALEELEEV-----EENIERLDL------IIDEKRQQLERL-RREREKAERYQALLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1222 QAIANATQANKEASdaiyggEQISKQIAELKEKQNQLNESIHrtlDLAEEQKKSADEANNLAA--VSLTNVEAVkipsvd 1299
Cdd:TIGR02169 226 YELLKEKEALERQK------EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKkiKDLGEEEQL------ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1300 pkELRNDVAGVLEESENLVDSsvkensandelFDEVNRSVADARNELQssQDQQRVsDQLMLELEKSRERI------VDS 1373
Cdd:TIGR02169 291 --RVKEKIGELEAEIASLERS-----------IAEKERELEDAEERLA--KLEAEI-DKLLAEIEELEREIeeerkrRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1374 VSTADKTLKDAEAALQV-LEEfgakIEKSRNDAVAEFAGVEginQRLDDIIDaqdkRRNSLPIDKQFVIDYRKSADVLLN 1452
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAeLEE----VDKEFAETRDELKDYR---EKLEKLKR----EINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1453 ETHALADRYKDIIhSDVDTRdsTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATIL 1532
Cdd:TIGR02169 424 DLNAAIAGIEAKI-NELEEE--KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
....*
gi 392926425 1533 AEEDE 1537
Cdd:TIGR02169 501 ASEER 505
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
736-782 |
7.38e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 7.38e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392926425 736 CDCHNH---SNSCEAESGSCICEHNTAGDTCERCARGYYGDAlQGTEEDC 782
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1143-1433 |
1.03e-08 |
|
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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1143 DAAENDMKRWEIIIEnarrEIENVLHYLE-------------TEGEER-AQIAYNASQKYGEQSKRMSELASGTREEAEK 1208
Cdd:COG1196 182 EATEENLERLEDILG----ELERQLEPLErqaekaeryrelkEELKELeAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1209 HLKQASEIE---QLSEQAIANATQANKEASDAIYGG----EQISKQIAELKEKQNQLNESIHR-TLDLAEEQKKSADEAN 1280
Cdd:COG1196 258 LEAELAELEaelEELRLELEELELELEEAQAEEYELlaelARLEQDIARLEERRRELEERLEElEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1281 NLAAV--SLTNVEAVKipsvdpKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQDQQRVSDQ 1358
Cdd:COG1196 338 ELEELeeELEEAEEEL------EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926425 1359 LMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSL 1433
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
890-943 |
1.35e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 392926425 890 CGCFAAGTRRPnndytllECNQQDGQCDCLPNVIGIQCDQCAHGFYNItSGLGC 943
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
890-943 |
4.10e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 4.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 890 CGCFAAGTRRPNndytlleCNQQDGQCDCLPNVIGIQCDQCAHGFYN--ITSGLGC 943
Cdd:pfam00053 1 CDCNPHGSLSDT-------CDPETGQCLCKPGVTGRHCDRCKPGYYGlpSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1116-1466 |
4.59e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1116 AIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLHYLEtegeeRAQIAYNASQKYGEQSKRM 1195
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-----ELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1196 SELASGTREEAEKHLKQA-SEIEQLSEQAIanatQANKEASDAIYGGEQISKQIAELKEKQNQLNESI------HRTLDL 1268
Cdd:COG4372 103 LESLQEEAEELQEELEELqKERQDLEQQRK----QLEAQIAELQSEIAEREEELKELEEQLESLQEELaaleqeLQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1269 AEEQKKSA---DEANNLAAVSLTNVEAVKIPSVDPKELRndvagvlEESENLVDSSVKENSANDELfdevnrsvadaRNE 1345
Cdd:COG4372 179 AEAEQALDellKEANRNAEKEEELAEAEKLIESLPRELA-------EELLEAKDSLEAKLGLALSA-----------LLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1346 LQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDA 1425
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 392926425 1426 QDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIIH 1466
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSK 361
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1069-1538 |
4.73e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 57.73 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1069 IIENPAPVndtkfdEKVKEtsrAASEV-----WEAVKQKTKEgggtiktKSKAIKDEivaaLEKltsIDESVAQAKVGAD 1143
Cdd:pfam05701 3 LIDTAAPF------ESVKE---AVSKFggivdWKAHRIQTVE-------RRKLVELE----LEK---VQEEIPEYKKQSE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1144 AAEndMKRWEII--IENARREIENVLHYLetegeERAQIAynasqkyGEQSKRMSELASGTREEAEK------------- 1208
Cdd:pfam05701 60 AAE--AAKAQVLeeLESTKRLIEELKLNL-----ERAQTE-------EAQAKQDSELAKLRVEEMEQgiadeasvaakaq 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1209 -------HLKQAS-------EIEQLSEQAIANATQ---ANKEASDAIYGGEQISKQIAELKEKQNQLNESI---HRTLDL 1268
Cdd:pfam05701 126 levakarHAAAVAelksvkeELESLRKEYASLVSErdiAIKRAEEAVSASKEIEKTVEELTIELIATKESLesaHAAHLE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1269 AEEQKKSADEANNLAAVSLTnveavkipsvdpKELRNdvagVLEESENLvdssvkensaNDELfdevnRSVADARNELQS 1348
Cdd:pfam05701 206 AEEHRIGAALAREQDKLNWE------------KELKQ----AEEELQRL----------NQQL-----LSAKDLKSKLET 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1349 SQD-QQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAAL----QVLEEFGAKIEKSRNDAVAEFAGVEGINQRLddii 1423
Cdd:pfam05701 255 ASAlLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAALasakKELEEVKANIEKAKDEVNCLRVAAASLRSEL---- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1424 daqDKRRNSLPIDKQfvidyRKS-ADVLLNETHALADRykdiihsdvdTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQ 1502
Cdd:pfam05701 331 ---EKEKAELASLRQ-----REGmASIAVSSLEAELNR----------TKSEIALVQAKEKEAREKMVELPKQLQQAAQE 392
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 392926425 1503 AEDDK---QMATEAVRKAT----LAKNSAIEANATILAEEDEI 1538
Cdd:pfam05701 393 AEEAKslaQAAREELRKAKeeaeQAKAAASTVESRLEAVLKEI 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1143-1433 |
5.44e-08 |
|
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: 58.14 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1143 DAAENDMKRweiiIENARREIENVLHYLETEgeerAQIAynasQKYGEQSKRMSELA---SGTR-EEAEKHLkqaseiEQ 1218
Cdd:TIGR02168 182 ERTRENLDR----LEDILNELERQLKSLERQ----AEKA----ERYKELKAELRELElalLVLRlEELREEL------EE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1219 LSEQAIANATQANKEASDAIYGGEQIS---KQIAELKEKQNQLN------------------------ESIHRTLDLAEE 1271
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEelrLEVSELEEEIEELQkelyalaneisrleqqkqilrerlANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1272 QKKSADEANNLAAVSLTNVEAVKipsvdpKELRNDVAGVLEESENLVDSSVKENSANDELFDEV---NRSVADARNELQS 1348
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKL------EELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1349 SQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKdaEAALQVLEEFGAKIEKSRNDAVAEFAGV----EGINQRLDDIID 1424
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLeealEELREELEEAEQ 475
|
....*....
gi 392926425 1425 AQDKRRNSL 1433
Cdd:TIGR02168 476 ALDAAEREL 484
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1157-1617 |
6.49e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1157 ENARREIENVLHYLETEGEERAQIAYNAS---QKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSEQaIANATQANKE 1233
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELAEE-VRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1234 ASDAIYGG-----------EQISKQIAELKEKQNQLNESIhrtldlaEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKE 1302
Cdd:PRK02224 291 LEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRL-------EECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1303 LRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQDQqrvSDQLMLELEKSRERIVD---SVSTADK 1379
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF---LEELREERDELREREAEleaTLRTARE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1380 TLKDAEAALQV--LEEFGAKIEKS-RNDAVAEFAG-VEGINQRLDDIIDAQDKRRNSlpidkqfvIDYRKSADVLLNETH 1455
Cdd:PRK02224 441 RVEEAEALLEAgkCPECGQPVEGSpHVETIEEDRErVEELEAELEDLEEEVEEVEER--------LERAEDLVEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1456 ALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEEltdsnenlqyyKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEE 1535
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1536 DEIKKIINSLDTME------------------------EVNNAELDELEEEIDRLDQL--------LAQAQLAKEvpTYQ 1583
Cdd:PRK02224 582 AELKERIESLERIRtllaaiadaedeierlrekrealaELNDERRERLAEKRERKRELeaefdearIEEAREDKE--RAE 659
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 392926425 1584 QYRADEDVKVAQLKNDISELQK-------EVLNLEEIRDNL 1617
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAeigavenELEELEELRERR 700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1083-1551 |
7.17e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1083 EKVKETSRAASEVWEAVKQKTKEG---GGTIKTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENA 1159
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAkkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1160 RREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELASGTRE-----EAEKHLKQASEIEQLSEQA--IANATQANK 1232
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKAEEAKKKAeeAKKADEAKK 1477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1233 EASDAiYGGEQISKQIAELKEKQNQLNEsihrtldlAEEQKKSADEANNL----AAVSLTNVEAVKIPSVDPKELRNDVA 1308
Cdd:PTZ00121 1478 KAEEA-KKADEAKKKAEEAKKKADEAKK--------AAEAKKKADEAKKAeeakKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1309 GVLEESENLVDSSVKENsANDELFDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEaaL 1388
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--L 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1389 QVLEEFGAKIEKSRNDAVAEFAGVEGIN--QRLDDIIDAQDKRRNSlpidkqfviDYRKSADVLLNETHALADRYKDIIH 1466
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKAE---------EDKKKAEEAKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1467 SDVDTRDSTEAVQYDIEQL--MEELTDSNENlqyYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINS 1544
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKkkAEELKKAEEE---NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
....*..
gi 392926425 1545 LDTMEEV 1551
Cdd:PTZ00121 1774 RKEKEAV 1780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1080-1397 |
1.45e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1080 KFDEKVK-ETSRAASEVWEAVKQKTKEGGGTIKTKSKAikDEIVAAlEKLTSIDE--SVAQAKVGADAAENDMKRWEIII 1156
Cdd:PTZ00121 1511 KADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKA-EELKKAEEkkKAEEAKKAEEDKNMALRKAEEAK 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1157 ENARREIENVLHYLETEGEERAQIAynasQKYGEQSKRMSELasgTREEAEKhlKQASEIEQLSEQAIANATQANKEASD 1236
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEEL---KKAEEEK--KKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1237 AIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVKipsvDPKELRNDVAGVLEESEN 1316
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK----KAEELKKAEEENKIKAEE 1734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1317 LVDSSVKENSANDELF--DEVNRSVADARNELQSSQDQQRVSDQLMLElEKSRERIVDSVSTADKTLKDAEAALQVLEEF 1394
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFANIIEG 1813
|
...
gi 392926425 1395 GAK 1397
Cdd:PTZ00121 1814 GKE 1816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1203-1550 |
2.58e-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: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1203 REEAEKHLKQASE---------------IEQLSEQAianaTQANKeasdaiYggeqisKQI-AELKEKQNQLN----ESI 1262
Cdd:COG1196 174 KEEAERKLEATEEnlerledilgelerqLEPLERQA----EKAER------Y------RELkEELKELEAELLllklREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1263 HRTLDLAEEQKKSADEANNLAAVSLTNVEAVKipsvdpKELRNDVAgvlEESENLVDSSVKENSANDELfdevNRSVADA 1342
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAEL------EELRLELE---ELELELEEAQAEEYELLAEL----ARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1343 RNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDI 1422
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1423 IDAQDKRRNSLpidkqfvIDYRKSADVLLNETHALADRyKDIIHSDVDTRDSTEAvqyDIEQLMEELTDSNENLQYYKKQ 1502
Cdd:COG1196 385 AEELLEALRAA-------AELAAQLEELEEAEEALLER-LERLEEELEELEEALA---ELEEEEEEEEEALEEAAEEEAE 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 392926425 1503 AEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEE 1550
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1057-1539 |
3.09e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1057 EKVKSLDNTLQEIIENPAPVNDTKFDEKVKETSRAASEVWEAVKQKTKEGGGtIKTKSKAIKDeivaALEKLTSidesvA 1136
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKELKK----AIEELKK-----A 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1137 QAKV---GADAAENDMKRweiIIENARREIENVLHYLETEGEERAQIaynasqkygeqSKRMSELasgtreeaEKHLKQA 1213
Cdd:PRK03918 435 KGKCpvcGRELTEEHRKE---LLEEYTAELKRIEKELKEIEEKERKL-----------RKELREL--------EKVLKKE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1214 SEI---EQLSEQaIANATQANKEasdaiYGGEQISKQIAE---LKEKQNQLNESIHRtldLAEEQKKSADEANNLAAVSl 1287
Cdd:PRK03918 493 SELiklKELAEQ-LKELEEKLKK-----YNLEELEKKAEEyekLKEKLIKLKGEIKS---LKKELEKLEELKKKLAELE- 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1288 tnveaVKIpsvdpKELRNDVAGVLEESENLVDSSVKE-NSANDELfdevnRSVADARNELQSSQDqqrvsdqlmlELEKS 1366
Cdd:PRK03918 563 -----KKL-----DELEEELAELLKELEELGFESVEElEERLKEL-----EPFYNEYLELKDAEK----------ELERE 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1367 RERIVDSVSTADKTLKDAEAALQVLEEFGAKI-EKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLpidkqfvidyRK 1445
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELeELEKKYSEEEYEELREEYLELSRELAGLRAELEEL----------EK 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1446 SADvllnETHALADRYKDiihsDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDD-----KQMATEAVRKATLA 1520
Cdd:PRK03918 688 RRE----EIKKTLEKLKE----ELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERalskvGEIASEIFEELTEG 759
|
490
....*....|....*....
gi 392926425 1521 KNSAIeanaTILAEEDEIK 1539
Cdd:PRK03918 760 KYSGV----RVKAEENKVK 774
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1050-1588 |
4.56e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1050 SRVNVFREKVKSLDNTLQEIIENpapvndtkfDEKVKETSRAASEVWEAVKQKTKE--------------GGGTIKTKsK 1115
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQ---------REQARETRDEADEVLEEHEERREEletleaeiedlretIAETERER-E 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1116 AIKDEIVAALEKLTSIDE--SVAQAKVGADAAENDmkrweiIIENARREIENVlhylETEGEERAQIAYNASQKYGEQSK 1193
Cdd:PRK02224 276 ELAEEVRDLRERLEELEEerDDLLAEAGLDDADAE------AVEARREELEDR----DEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1194 RMSELASGTREEAEKHLKQASEIEQlseqAIANATQANKEASDAIyggEQISKQIAELKEKQNQLNESIHRTLDLAEEQK 1273
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELES----ELEEAREAVEDRREEI---EELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1274 KSADEANNlaavSLTNVEAvkipsvDPKELRNDVagvlEESENLVDS--------SVKENSANDELfDEVNRSVADARNE 1345
Cdd:PRK02224 419 EERDELRE----REAELEA------TLRTARERV----EEAEALLEAgkcpecgqPVEGSPHVETI-EEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1346 LQSSQDQQ-RVSDQL-----MLELEKSRERIVDSVSTADKTLKDAEA-------ALQVLEEFGAKIE------------- 1399
Cdd:PRK02224 484 LEDLEEEVeEVEERLeraedLVEAEDRIERLEERREDLEELIAERREtieekreRAEELRERAAELEaeaeekreaaaea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1400 KSRNDAVAEFAGVegINQRLDDI---IDAQDKRRNSLpidkQFVIDYRKSADvllnethALADRYKDIIHSDVDTRDSTE 1476
Cdd:PRK02224 564 EEEAEEAREEVAE--LNSKLAELkerIESLERIRTLL----AAIADAEDEIE-------RLREKREALAELNDERRERLA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1477 AVQYDIEQLMEELTDSN-ENLQYYKKQAEDDKQMATEAVRKATlaknsaieanatilAEEDEIKKII----NSLDTMEev 1551
Cdd:PRK02224 631 EKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELR--------------EERDDLQAEIgaveNELEELE-- 694
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 392926425 1552 nnaeldeleEEIDRLDQLLAQAQ----LAKEV----PTYQQYRAD 1588
Cdd:PRK02224 695 ---------ELRERREALENRVEaleaLYDEAeeleSMYGDLRAE 730
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
286-337 |
4.68e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 4.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392926425 286 RCKCNGHASECVGSSSVDGenrlVCRCEHNTQGADCNECLPFYNDRPWRSGT 337
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG----QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1050-1554 |
5.29e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1050 SRVNVFREKVKS----LDNTLQEIIENPAPVNDTkfdEKVKEtsrAASEVWEAVKQKTKEGGGTIKTKSkAIKDEIVAAL 1125
Cdd:PRK01156 183 SNIDYLEEKLKSsnleLENIKKQIADDEKSHSIT---LKEIE---RLSIEYNNAMDDYNNLKSALNELS-SLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1126 EKLTSIDESVAQAKVGADAAENDMKRWEIIIENA----RREIENVLHYLETEGEERaQIAYNAS---QKYGEQSKRMSEL 1198
Cdd:PRK01156 256 SEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDIENKK-QILSNIDaeiNKYHAIIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1199 ASgtreEAEKHLKQASEIEQLSEQAIANATQANKEASdAIYGGEQISKQIAELKEKQNQLNESIHRTLDLA----EEQKK 1274
Cdd:PRK01156 335 QK----DYNDYIKKKSRYDDLNNQILELEGYEMDYNS-YLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDAIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1275 SADEANnlaaVSLTNVEAvKIPSVDPK---------ELRNDVA-----GVL---------EESENLVDSSVKENSANDEL 1331
Cdd:PRK01156 410 ELNEIN----VKLQDISS-KVSSLNQRiralrenldELSRNMEmlngqSVCpvcgttlgeEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1332 FDEVNRSVADARNELQ---------SSQDQQRV--SDQLMLELEKSRERIVDSVST-ADKTLKDAEAALQV----LEEFG 1395
Cdd:PRK01156 485 IREIEIEVKDIDEKIVdlkkrkeylESEEINKSinEYNKIESARADLEDIKIKINElKDKHDKYEEIKNRYkslkLEDLD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1396 AKIEkSRNDAVAEFAGV---------EGINQRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADvllNETHALADRYKDI-- 1464
Cdd:PRK01156 565 SKRT-SWLNALAVISLIdietnrsrsNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE---NEANNLNNKYNEIqe 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1465 -------IHSDVDTRDSTEAVQYDIEQLMEELT----DSNENLQYYKKQAEDDK--QMATEAVRKATLAKNSAIE-ANAT 1530
Cdd:PRK01156 641 nkiliekLRGKIDNYKKQIAEIDSIIPDLKEITsrinDIEDNLKKSRKALDDAKanRARLESTIEILRTRINELSdRIND 720
|
570 580
....*....|....*....|....
gi 392926425 1531 ILAEEDEIKKIINSLDTMEEVNNA 1554
Cdd:PRK01156 721 INETLESMKKIKKAIGDLKRLREA 744
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1301-1633 |
7.79e-07 |
|
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: 54.29 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1301 KELRNdvagvlEESENLVDSSVKE-NSANDELfDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADK 1379
Cdd:TIGR02168 216 KELKA------ELRELELALLVLRlEELREEL-EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1380 TLKDAEAALQVLEEFGAKIEKSRNDAVAEFAgveginqRLDDIIDAQDKRRnslpidkqfvidyrksaDVLLNETHALAD 1459
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLE-------ELEAQLEELESKL-----------------DELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1460 RYkdiihsdvdtrdstEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIK 1539
Cdd:TIGR02168 345 KL--------------EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1540 KIINSLDTMEEVN--------NAELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQ-----LKNDISELQKE 1606
Cdd:TIGR02168 411 RLEDRRERLQQEIeellkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEqaldaAERELAQLQAR 490
|
330 340
....*....|....*....|....*..
gi 392926425 1607 VLNLEEIRDNLPTKCFNVINLEQEGQK 1633
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1081-1617 |
8.45e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1081 FDEKVKETSRAASEVWEAVKQKTKEGGGTIKTKSKAIKDEIV-------AALEKLTS-IDESVAQAKVGADAAEndmKRW 1152
Cdd:pfam12128 366 LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDrqlavaeDDLQALESeLREQLEAGKLEFNEEE---YRL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1153 EIIIENARREIENVLHYLET--------EGEERAQIAYNASQKygEQSKRMSEL--ASGTREEAEKHLKQASeiEQLSEQ 1222
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELllqlenfdERIERAREEQEAANA--EVERLQSELrqARKRRDQASEALRQAS--RRLEER 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1223 aiANATQANKEASDAIYGG--EQISKQIAELKEKQNQL--NESIHRTlDL-AEEQKKSADEANNLAAVSLtNVEAVKIPS 1297
Cdd:pfam12128 519 --QSALDELELQLFPQAGTllHFLRKEAPDWEQSIGKVisPELLHRT-DLdPEVWDGSVGGELNLYGVKL-DLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1298 --VDPKELRNDVAGVleeSENLVDSSVKENSANDEL------FDEVNRSVADARNELQSSQ-DQQRVSDQ---LMLELEK 1365
Cdd:pfam12128 595 waASEEELRERLDKA---EEALQSAREKQAAAEEQLvqangeLEKASREETFARTALKNARlDLRRLFDEkqsEKDKKNK 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1366 SRERIVDSVSTADKTLkDAEAAL------QVLEEFGAKIEKSRNDAVAEFAGVEG-INQRLDDIIDAQDKRRNSlpidkq 1438
Cdd:pfam12128 672 ALAERKDSANERLNSL-EAQLKQldkkhqAWLEEQKEQKREARTEKQAYWQVVEGaLDAQLALLKAAIAARRSG------ 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1439 fvidyRKSadvllnETHALADRYkdiiHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAE--DDKQMATEAVRK 1516
Cdd:pfam12128 745 -----AKA------ELKALETWY----KRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLryFDWYQETWLQRR 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1517 ATLAKNSAiEANATILAEEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLAQAQLakevptYQQYRAD--EDVKVA 1594
Cdd:pfam12128 810 PRLATQLS-NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATlkEDANSE 882
|
570 580
....*....|....*....|...
gi 392926425 1595 QLKNDISELQKEVLNLEEIRDNL 1617
Cdd:pfam12128 883 QAQGSIGERLAQLEDLKLKRDYL 905
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1054-1552 |
1.19e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.90 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1054 VFREKVKSLDNTLQEIIenpapvndTKFDEK---VKETSRAASEVWEAVKQKTKegggtiKTKSKAIKDEIVAALEKL-- 1128
Cdd:TIGR01612 1163 ISNDDPEEIEKKIENIV--------TKIDKKkniYDEIKKLLNEIAEIEKDKTS------LEEVKGINLSYGKNLGKLfl 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1129 TSIDESVAQAKVGADAAENDMKRWEIIIENARrEIENVLHYLETEGEERA--QIAYNASQKYGEQSKRMSELASGTREEA 1206
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSP-EIENEMGIEMDIKAEMEtfNISHDDDKDHHIISKKHDENISDIREKS 1307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1207 EKHLK---QASEIEQLSEQAIANATQANKEASDA------------IYGGEQISKQIAELKEKQNQLNE----------- 1260
Cdd:TIGR01612 1308 LKIIEdfsEESDINDIKKELQKNLLDAQKHNSDInlylneianiynILKLNKIKKIIDEVKEYTKEIEEnnknikdeldk 1387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1261 -------------------SIHRTLD------------------LAEEQK-----KSADEANNLAAVSLTNVEAVK---- 1294
Cdd:TIGR01612 1388 seklikkikddinleecksKIESTLDdkdidecikkikelknhiLSEESNidtyfKNADENNENVLLLFKNIEMADnksq 1467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1295 -IPSVDPKELRNDVAGVLEE-SENL---------VDSSVKENSANDELFDEVNRSVADARN-----ELQSSQDQQR---- 1354
Cdd:TIGR01612 1468 hILKIKKDNATNDHDFNINElKEHIdkskgckdeADKNAKAIEKNKELFEQYKKDVTELLNkysalAIKNKFAKTKkdse 1547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1355 ------------------VSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAK------IEKSRNDAVAEFA 1410
Cdd:TIGR01612 1548 iiikeikdahkkfileaeKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKflkisdIKKKINDCLKETE 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1411 GVEginqrlddiidaqdKRRNSLPIDKQfvidyrksaDVLLNETHALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEELT 1490
Cdd:TIGR01612 1628 SIE--------------KKISSFSIDSQ---------DTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIE 1684
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926425 1491 DSNENLQYYKKQAEDDkqmATEAVRKATLAKNSAIEANATILaeEDEIKKIINSLDT--MEEVN 1552
Cdd:TIGR01612 1685 KIEIDVDQHKKNYEIG---IIEKIKEIAIANKEEIESIKELI--EPTIENLISSFNTndLEGID 1743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1293-1611 |
1.54e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1293 VKIPSVDPKELRNDVAGV----------LEESENlVDSSVKENSAN-DELFDEVNRsVADARNELQSSQDQQRVSDQL-- 1359
Cdd:TIGR02169 148 ISMSPVERRKIIDEIAGVaefdrkkekaLEELEE-VEENIERLDLIiDEKRQQLER-LRREREKAERYQALLKEKREYeg 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1360 ------MLELEKSRERIVDSVSTADKTL-----------KDAEAALQVLEEFGAKIEKSRNDAVAEF----AGVEGINQR 1418
Cdd:TIGR02169 226 yellkeKEALERQKEAIERQLASLEEELeklteeiseleKRLEEIEQLLEELNKKIKDLGEEEQLRVkekiGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1419 LDDII--------DAQDKRRNS-LPIDKQF---------VIDYRKSADVLLNETHALADRYKDIIH--SDVD-----TRD 1473
Cdd:TIGR02169 306 LERSIaekereleDAEERLAKLeAEIDKLLaeieelereIEEERKRRDKLTEEYAELKEELEDLRAelEEVDkefaeTRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1474 STEAVQYDIEQLMEELTDSNENLqyykKQAEDDKQMATEAVRKatlAKNSAIEANATILAEEDEIKKIINSLDTMEEvnn 1553
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKREL----DRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEW--- 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 392926425 1554 aeldeleeeidRLDQLlaQAQLAKEvptYQQYRADEDvKVAQLKNDISELQKEVLNLE 1611
Cdd:TIGR02169 456 -----------KLEQL--AADLSKY---EQELYDLKE-EYDRVEKELSKLQRELAEAE 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1610 |
1.82e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1056 REKVKsldnTLQEIIENPAPVNDTKFDEKVKETSRAASEVWEAVKQKtkeggGTIKTKSKAIKDEIVAALEKLTSIDESV 1135
Cdd:COG4913 248 REQIE----LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL-----ELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1136 AQAKVGADAAENDmkRWEI---IIENARREIENvlhyLETEGEERAQiaynASQKYGEQSKRMSELASGTREE------- 1205
Cdd:COG4913 319 DALREELDELEAQ--IRGNggdRLEQLEREIER----LERELEERER----RRARLEALLAALGLPLPASAEEfaalrae 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1206 AEKHLKQASEIEQLSEQAIANATQANKEASDAIyggEQISKQIAELKEKQNQLNESIHRTLD-LAEEQKKSADE------ 1278
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRREL---RELEAEIASLERRKSNIPARLLALRDaLAEALGLDEAElpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1279 -----------------------------ANNLAAVsLTNVEAVK---------IPSVDPKELR-----NDVAGVLEese 1315
Cdd:COG4913 466 lievrpeeerwrgaiervlggfaltllvpPEHYAAA-LRWVNRLHlrgrlvyerVRTGLPDPERprldpDSLAGKLD--- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1316 nlvdssVKENSANDELFDEVNRS-----VADARnELQssQDQQRVSDQLMLELEKSRERIVDSVSTADKTL--KDAEAAL 1388
Cdd:COG4913 542 ------FKPHPFRAWLEAELGRRfdyvcVDSPE-ELR--RHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVlgFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1389 QVLEEFGAKIEKSRNDAVAEFagveginQRLDDIIDAQDKRRNSLpidkqfvidyrksadvllnetHALADRYKDiihsD 1468
Cdd:COG4913 613 AALEAELAELEEELAEAEERL-------EALEAELDALQERREAL---------------------QRLAEYSWD----E 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1469 VDTRDSTEAVQyDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKkiinslDTM 1548
Cdd:COG4913 661 IDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD------ELQ 733
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926425 1549 EEVNNAELDELEEEIDRLDQLLAQAQLAKevpTYQQYRADEDVKVAQLKNDISELQKEVLNL 1610
Cdd:COG4913 734 DRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEERIDALRARLNRAEEELERA 792
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
835-890 |
1.86e-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: 46.19 E-value: 1.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 835 CACSGNTDPNsiGNCDKITGECKkCIFNTHGFNCENCKPGYWGDaliePKGNCQSC 890
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGL----PSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1017-1606 |
2.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1017 ENVEGRRCDQCAEnrYGITQGCLPCDDCYTLIQSRVNVFREKVKSLDNTLQEIieNPApVNDTKFDEKVKE-TSRAASEV 1095
Cdd:PTZ00121 1022 QNFNIEKIEELTE--YGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGL--KPS-YKDFDFDAKEDNrADEATEEA 1096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1096 WEAVKQKTKEGGGTIKTKSKaiKDEIVAALEKLTSIDEsvaqakvgADAAEnDMKRweiiIENARREIENVLHYLETEGE 1175
Cdd:PTZ00121 1097 FGKAEEAKKTETGKAEEARK--AEEAKKKAEDARKAEE--------ARKAE-DARK----AEEARKAEDAKRVEIARKAE 1161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1176 E--RAQIAYNAsqkygEQSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAiyggeQISKQIAELKE 1253
Cdd:PTZ00121 1162 DarKAEEARKA-----EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA-----EDAKKAEAVKK 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1254 kqnqlnesihrtldlAEEQKKSADEANNLAAVSlTNVEAVKIPSVDPKELRNDVAGVLEESENLVDSSVK--ENSANDEL 1331
Cdd:PTZ00121 1232 ---------------AEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEA 1295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1332 FDEVNRSVADarnELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAG 1411
Cdd:PTZ00121 1296 KKAEEKKKAD---EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1412 VEGINQRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNE-----THALADRYKDIIHSDVDTRDSTEAVQYDIEQLM 1486
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAaakkkADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1487 EELTDSNENLQYY----------------KKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDTMEE 1550
Cdd:PTZ00121 1453 AEEAKKAEEAKKKaeeakkadeakkkaeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 1551 VNNAEldeleeeidrldqllaQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKE 1606
Cdd:PTZ00121 1533 AKKAD----------------EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
835-888 |
4.38e-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: 45.04 E-value: 4.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 392926425 835 CACSGNTDPNsiGNCDKITGECKkCIFNTHGFNCENCKPGYWGDALIepKGNCQ 888
Cdd:cd00055 2 CDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1211-1417 |
5.08e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1211 KQASEIEQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIhrtLDLAEEQKKSADEANNLAAVSLTNv 1290
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALYRS- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1291 eavkipsvdpkELRNDVAGVLEESENLVD-----SSVKE-NSANDELFDEVNRSVADARNELQSSQDQQRVSDQLMLELE 1364
Cdd:COG3883 99 -----------GGSVSYLDVLLGSESFSDfldrlSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392926425 1365 KSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQ 1417
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1049-1409 |
8.08e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1049 QSRVNVFREKVKSLDNTLQEIIENpapvNDTKFDEKVKETSRAASEVWEAVKQKTKegggtIKTKSKAIKDEIVAALEKL 1128
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRK----ALFELDKLQEELEQLREELEQAREELEQ-----LEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1129 TSIDESVAQAKVGADAAEN-------DMKRWEIIIENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELASg 1201
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEeleslqeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1202 TREEAEK--HLKQASEIEQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNEsihrtLDLAEEQKKSADEA 1279
Cdd:COG4372 162 LQEELAAleQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE-----AKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1280 NNLAAVSLTNVEAVKIPSVDPKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQ----SSQDQQRV 1355
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLaalsLIGALEDA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 392926425 1356 SDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEF 1409
Cdd:COG4372 317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1159-1554 |
1.04e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1159 ARREIENVLHYLETEGEERAQIAYNASQKYGEQskRMSELASgtREEAEKHLKQA-SEIEQLSEQAIANATQANKEASDA 1237
Cdd:COG3064 10 AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEE--RLAELEA--KRQAEEEAREAkAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1238 IYGGEqisKQIAELKEKQNQLNE---SIHRTLDLA-----EEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRNDVAG 1309
Cdd:COG3064 86 AAEAE---KKAAAEKAKAAKEAEaaaAAEKAAAAAekekaEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1310 VLEESEnlvdsSVKENSANDELFDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQ 1389
Cdd:COG3064 163 AAAAAA-----AAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1390 VLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNsLPIDKQFVIDYRKSADVLLNETHALADRYKDIIHSDV 1469
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLV-VVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1470 DTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDD--KQMATEAVRKATLAKNSAIEANATILAEEDEIKKIINSLDT 1547
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAgaGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAG 396
|
....*..
gi 392926425 1548 MEEVNNA 1554
Cdd:COG3064 397 GGGLLGL 403
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1048-1262 |
1.08e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 48.82 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1048 IQSRVNVFREKVKSLDNTLQEIIENPAPVNDTKfdEKVKETSRAASEVWEAVKQKTKEGGGTIKTKSKAIKD--EIVAAL 1125
Cdd:smart00283 16 QAEELEELAERMEELSASIEEVAANADEIAATA--QSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEEleESSDEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1126 EKLTS-IDESVAQ------------AKVG--------------------ADAAEndmkrwEI--IIENARREIENVLHYL 1170
Cdd:smart00283 94 GEIVSvIDDIADQtnllalnaaieaARAGeagrgfavvadevrklaersAESAK------EIesLIKEIQEETNEAVAAM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1171 E---TEGEERAQIAYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSeQAIANATQANKEASDAIyggEQISKQ 1247
Cdd:smart00283 168 EessSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVN-AAIDEIAQVTQETAAMS---EEISAA 243
|
250
....*....|....*
gi 392926425 1248 IAELKEKQNQLNESI 1262
Cdd:smart00283 244 AEELSGLAEELDELV 258
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1146-1614 |
1.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1146 ENDMKRWEIIIEnarrEIENVlHYleTEGEERAQI----AYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSE 1221
Cdd:PTZ00121 1039 DDVLKEKDIIDE----DIDGN-HE--GKAEAKAHVgqdeGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKA 1111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1222 QAIANATQANKEASDAiyggeqisKQIAELKEKqnqlnESIHRtldlAEEQKKSADEANNLAAVSLTnvEAVKIpsvdpk 1301
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDA--------RKAEEARKA-----EDARK----AEEARKAEDAKRVEIARKAE--DARKA------ 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1302 elrndvagvlEESENLVDSSVKENSANDElfdEVNRSvadarNELQSSQDQQRVSDQLMLE----LEKSR----ERIVDS 1373
Cdd:PTZ00121 1167 ----------EEARKAEDAKKAEAARKAE---EVRKA-----EELRKAEDARKAEAARKAEeerkAEEARkaedAKKAEA 1228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1374 VSTADKTLKDAEAALQVLEE-FGAKIEKSRNDAVAEFAgveginqRLDDIIDAQDKRRNSlpidkqfviDYRKSADVlln 1452
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFA-------RRQAAIKAEEARKAD---------ELKKAEEK--- 1289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1453 ethaladrykdiihsdvdtRDSTEAVQYDIEQLMEELTDSNENlqyyKKQAEDDKQMATEAVRKATLAKNSAIEANATIL 1532
Cdd:PTZ00121 1290 -------------------KKADEAKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1533 AEEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQL------LAQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKE 1606
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
....*...
gi 392926425 1607 VlnlEEIR 1614
Cdd:PTZ00121 1427 A---EEKK 1431
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1336-1633 |
1.48e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1336 NRSVADA-RNELQSSQ-DQQRVSDQLMLELEKSRERIVDSVST--------------ADKTLK---DAEAALQVLEEFGA 1396
Cdd:pfam05483 111 NRKIIEAqRKAIQELQfENEKVSLKLEEEIQENKDLIKENNATrhlcnllketcarsAEKTKKyeyEREETRQVYMDLNN 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1397 KIEKSRNdAVAEFAgVEGINQRLDDIIDAQDKRRNSLPIDKQF---VIDYRKSADVLLNETHALADRYKDIIHSDVDTRD 1473
Cdd:pfam05483 191 NIEKMIL-AFEELR-VQAENARLEMHFKLKEDHEKIQHLEEEYkkeINDKEKQVSLLLIQITEKENKMKDLTFLLEESRD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1474 STEAVQYDIEQLMEELTDSNENLQYYKKQAEDDK-QMATEAVRKATLAKNSAIeANATI--LAEEDEIKkiinsldtMEE 1550
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKmSLQRSMSTQKALEEDLQI-ATKTIcqLTEEKEAQ--------MEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1551 VNNAELDEL------EEEIDRLDQLLAQAQlakevptyQQYRADEDvkvaQLKNDISELQKEVLNLEEIrdnlpTKCFNV 1624
Cdd:pfam05483 340 LNKAKAAHSfvvtefEATTCSLEELLRTEQ--------QRLEKNED----QLKIITMELQKKSSELEEM-----TKFKNN 402
|
....*....
gi 392926425 1625 INLEQEGQK 1633
Cdd:pfam05483 403 KEVELEELK 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1246-1554 |
1.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1246 KQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVsLTNVEAVKIPSVDPKELRNDVAGVLEESENLvdssvkeN 1325
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEIDVASAEREIAELEAELERL-------D 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1326 SANDELfDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAkieKSRNDA 1405
Cdd:COG4913 682 ASSDDL-AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---EERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1406 VAEFAGVEGINQRLDDIIDAQDKRRNslpidkqfvidyrKSADVLLNETHALADRYKDIIhSDVDTrdSTEAVQyDIEQL 1485
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLN-------------RAEEELERAMRAFNREWPAET-ADLDA--DLESLP-EYLAL 820
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392926425 1486 MEELTdsNENLQYYKKQAEDdkqmateavRKATLAKNSAIEANATILAEEDEIKkiinslDTMEEVNNA 1554
Cdd:COG4913 821 LDRLE--EDGLPEYEERFKE---------LLNENSIEFVADLLSKLRRAIREIK------ERIDPLNDS 872
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
785-833 |
2.24e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 2.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 392926425 785 CPCPNDGPCILHAD-GDVICtECPNGYTGRRCDECSDGYFGNPKDGTECV 833
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1326-1537 |
2.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1326 SANDELfDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEfgaKIEKsRNDA 1405
Cdd:COG3883 13 FADPQI-QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEE-RREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1406 VAEFA-----------------GVEGIN------QRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYK 1462
Cdd:COG3883 88 LGERAralyrsggsvsyldvllGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926425 1463 diihsdvDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDE 1537
Cdd:COG3883 168 -------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1156-1409 |
2.75e-05 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 48.86 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1156 IENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKR-------MSELASGTREEAEkhlkQASEIEQLSEQAIANAT 1228
Cdd:COG0840 251 LRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASleetaaaMEELSATVQEVAE----NAQQAAELAEEASELAE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1229 QANKEASDAIYGGEQISKQIAELKEKQNQLNES---IHRTLDL----AE-----------------EQKKS----ADEAN 1280
Cdd:COG0840 327 EGGEVVEEAVEGIEEIRESVEETAETIEELGESsqeIGEIVDViddiAEqtnllalnaaieaaragEAGRGfavvADEVR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1281 NLA---AVSLTNVEAVkIpsvdpKELRNDVAGV---LEESENLVDSSVKENSANDELFDEVNRSVADARNELQ----SSQ 1350
Cdd:COG0840 407 KLAersAEATKEIEEL-I-----EEIQSETEEAveaMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQeiaaASE 480
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 392926425 1351 DQQRVSDQLMLELeksrERIVDSVSTADKTLKDAEAALQVLEEFGAKIeksrNDAVAEF 1409
Cdd:COG0840 481 EQSAGTEEVNQAI----EQIAAAAQENAASVEEVAAAAEELAELAEEL----QELVSRF 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1156-1494 |
3.45e-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: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1156 IENARREIENVLHYLETEGEERAQiAYNASQKYGEQSKRMSELAsgtreEAEKHLKQA-SEIEQLsEQAIANATQANKEA 1234
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYS-----WDEIDVASAeREIAEL-EAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1235 sdaiyggEQISKQIAELKEKQNQLNEsihrtlDLAEEQKKSADEANNLAAVsltnveavkipsvdpKELRNDVAGVLEES 1314
Cdd:COG4913 688 -------AALEEQLEELEAELEELEE------ELDELKGEIGRLEKELEQA---------------EEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1315 ENLVDSSVKENSanDELFDEVN--RSVADARNELQSSQDQQRvsdqlmLELEKSRERIV-----------DSVSTADKTL 1381
Cdd:COG4913 740 EDLARLELRALL--EERFAAALgdAVERELRENLEERIDALR------ARLNRAEEELEramrafnrewpAETADLDADL 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1382 KDAEAALQVLE--------EFGAKIEKSRNDA----VAEFAG-----VEGINQRLDDIIDA-QDKRRNSlpiDKQFVIDY 1443
Cdd:COG4913 812 ESLPEYLALLDrleedglpEYEERFKELLNENsiefVADLLSklrraIREIKERIDPLNDSlKRIPFGP---GRYLRLEA 888
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 1444 RKSADVLLNEthaladrYKDII-----HSDVDTRDSTEAVQYDIEQLMEELTDSNE 1494
Cdd:COG4913 889 RPRPDPEVRE-------FRQELravtsGASLFDEELSEARFAALKRLIERLRSEEE 937
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1190-1424 |
3.81e-05 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 47.28 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1190 EQSKRMSELASGTREEAEKhLKQ-ASEIEQLS---EQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIHRT 1265
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEE-LEElAERMEELSasiEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1266 LDLAEEQKKSADEANNLAAV-----SLTN-------VEAVkipsvdpkelRNDVAG-----VLEESENLVDSSvkENSAN 1328
Cdd:smart00283 80 VSAVEELEESSDEIGEIVSViddiaDQTNllalnaaIEAA----------RAGEAGrgfavVADEVRKLAERS--AESAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1329 D--ELFDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQ----VLEEFGAKIEKSR 1402
Cdd:smart00283 148 EieSLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDeqaaGSEEVNAAIDEIA 227
|
250 260 270
....*....|....*....|....*....|..
gi 392926425 1403 -----NDAVAE-----FAGVEGINQRLDDIID 1424
Cdd:smart00283 228 qvtqeTAAMSEeisaaAEELSGLAEELDELVE 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1222-1428 |
4.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1222 QAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVKipsvdpK 1301
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR------E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1302 ELRNDVAGVLEESENLVDSSVKENSAN-DELFDEVN--RSVADA-RNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTA 1377
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSalSKIADAdADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392926425 1378 DKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDK 1428
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1078-1276 |
5.66e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.56 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1078 DTKFDEKVKETSRAASEVWEAVKQKTKEGG--GTIKTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKrweiI 1155
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLEEAEKRAEKAEAevAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRK----V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1156 IENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSeLASGTREEAEKHLKQA-SEIEQLsEQAIANATQANK-- 1232
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLV-VVEGDLERAEERAELAeSKIVEL-EEELKVVGNNLKsl 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392926425 1233 EASDAIYGGEQISK--QIAELKEKqnqLNESIHRtldlAEEQKKSA 1276
Cdd:pfam00261 161 EASEEKASEREDKYeeQIRFLTEK---LKEAETR----AEFAERSV 199
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1300-1617 |
6.98e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1300 PKELRN---DVAGVL------EESEN-LvdSSVKENsandelfdeVNRsVADARNELqssqDQQRVSdqlmLELE----- 1364
Cdd:COG1196 154 PEERRAiieEAAGISkykerkEEAERkL--EATEEN---------LER-LEDILGEL----ERQLEP----LERQaekae 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1365 -----KSRERIVDSVSTADKtLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLpidkqf 1439
Cdd:COG1196 214 ryrelKEELKELEAELLLLK-LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA------ 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1440 vidyRKSADVLLNETHALAdryKDIIHSDVDTRDSTEavqyDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATL 1519
Cdd:COG1196 287 ----QAEEYELLAELARLE---QDIARLEERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1520 AKNSAIEANATILAEEDEIKKIINSLDTMEEvnnaeldeleeeiDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLKND 1599
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAE-------------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
330
....*....|....*...
gi 392926425 1600 ISELQKEVLNLEEIRDNL 1617
Cdd:COG1196 423 LEELEEALAELEEEEEEE 440
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1111-1294 |
7.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1111 KTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENV---LHYLETEGEERAQIAYNASQK 1187
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeIEERREELGERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1188 YG---------------EQSKRMSELASGTREEAEKHLKQASEIEQLS---EQAIANATQANKEASDAIyggEQISKQIA 1249
Cdd:COG3883 102 VSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKaelEAKLAELEALKAELEAAK---AELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 392926425 1250 ELKEKQNQLNE---SIHRTLDLAEEQKKSADEANNLAAVSLTNVEAVK 1294
Cdd:COG3883 179 EQEALLAQLSAeeaAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1083-1526 |
7.40e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.90 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1083 EKVKETSRAASEVWEAVK--QKTKEgggtikTKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEI--IIEN 1158
Cdd:NF041483 608 EAAEETERLRTEAAERIRtlQAQAE------QEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAqeSADR 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1159 ARREIENVLHYLETEGEEraqiAYNASQKYGEQSKRMSE-LASGTREEAEKHLKQASE------------IEQLSEQAIA 1225
Cdd:NF041483 682 VRAEAAAAAERVGTEAAE----ALAAAQEEAARRRREAEeTLGSARAEADQERERAREqseellasarkrVEEAQAEAQR 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1226 NATQANKEASDAIYGGEQISKQI----AELKEKQNQ--------LNESIHRT------------LDLAEEQKKSADEANN 1281
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQVrdsvAGLQEQAEEeiaglrsaAEHAAERTrteaqeeadrvrSDAYAERERASEDANR 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1282 LAAVSLTNVEAVKIPSvdpkelRNDVAGVLEESENL-VDSSVKENSANDELFDEV-------NRSVADAR---NELQSSQ 1350
Cdd:NF041483 838 LRREAQEETEAAKALA------ERTVSEAIAEAERLrSDASEYAQRVRTEASDTLasaeqdaARTRADARedaNRIRSDA 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1351 DQQrvSDQLMLELEKSRERIVDSVSTADKTLKD--AEAALQVLEEFGAKIEKSRNDAVAEfagvegiNQRL-----DDII 1423
Cdd:NF041483 912 AAQ--ADRLIGEATSEAERLTAEARAEAERLRDeaRAEAERVRADAAAQAEQLIAEATGE-------AERLraeaaETVG 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1424 DAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRDSTEAVQYDieQLMEELTDSNENL------Q 1497
Cdd:NF041483 983 SAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQAD--TLITEAAAEADQLtakaqeE 1060
|
490 500 510
....*....|....*....|....*....|....*....
gi 392926425 1498 YYKKQAEDDKQMAT-------EAVR---KATLAKNSAIE 1526
Cdd:NF041483 1061 ALRTTTEAEAQADTmvgaarkEAERivaEATVEGNSLVE 1099
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1149-1536 |
7.54e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1149 MKRWEIIIENARREIENVLHYLETEGEERAQIAYNASQKYGeqskrmselasgtreEAEKHLKQASEieqLSEQAIANAT 1228
Cdd:COG5022 812 YRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFG---------------RSLKAKKRFSL---LKKETIYLQS 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1229 QAN-KEASDAIYGGEQISKQIAELKEKQNQLNESIhrtLDLAEEQKKSADEANNLAAVSLTNVEA------VKIPSVDPK 1301
Cdd:COG5022 874 AQRvELAERQLQELKIDVKSISSLKLVNLELESEI---IELKKSLSSDLIENLEFKTELIARLKKllnnidLEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1302 ELRNDVAGVLEESENLVDSSVKENSA---NDELFDEVNRSVADARN---ELQSSQDQ----QRVSDQLmleleKSRERIV 1371
Cdd:COG5022 951 VKLPELNKLHEVESKLKETSEEYEDLlkkSTILVREGNKANSELKNfkkELAELSKQygalQESTKQL-----KELPVEV 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1372 DSVSTADKTLKDAEAALQVLeefgAKIEKSRNDAVAEFAGVEGinqrldDIIDAQDKRRNSLPIDKQFVIDYR------- 1444
Cdd:COG5022 1026 AELQSASKIISSESTELSIL----KPLQKLKGLLLLENNQLQA------RYKALKLRRENSLLDDKQLYQLEStenllkt 1095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1445 -KSADVLLNETHALADRYKDIIHSDvdtrdstEAVQYDIEQLMEELTDSN-ENLQYYKKQAEDDKQMATEAVRKATLAKN 1522
Cdd:COG5022 1096 iNVKDLEVTNRNLVKPANVLQFIVA-------QMIKLNLLQEISKFLSQLvNTLEPVFQKLSVLQLELDGLFWEANLEAL 1168
|
410
....*....|....
gi 392926425 1523 SAIEANATILAEED 1536
Cdd:COG5022 1169 PSPPPFAALSEKRL 1182
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
1083-1293 |
7.82e-05 |
|
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: 45.31 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1083 EKVKETSRAASEVWEAVKQKTKegggtiktKSKAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARR- 1161
Cdd:cd11386 5 ASIEEVAASADQVAETSQQAAE--------LAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1162 -EIENVLhyletegeeraqiAYNAS---QKYGEQSKRMSELASGTREEAEKHLKQASEIEQL---SEQAIANATQANKEA 1234
Cdd:cd11386 77 aEQTNLL-------------ALNAAieaARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELieeIQEQTEEAVEAMEET 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392926425 1235 SDAIyggEQISKQIAELKEkqnQLNESIHRTLDLAEEQKKSADEANNLAAVSLTNVEAV 1293
Cdd:cd11386 144 SEEV---EEGVELVEETGR---AFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAV 196
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1060-1612 |
8.02e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1060 KSLDNTL-QEIIENPAPVNDtkFDEKVKETSRAASEVWEAVKQktkegggTIKTKSKAIKDEIVAALEKLTSidesvaqa 1138
Cdd:TIGR01612 1011 KNKENMLyHQFDEKEKATND--IEQKIEDANKNIPNIEIAIHT-------SIYNIIDEIEKEIGKNIELLNK-------- 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1139 kvgadaaeNDMKRWEIIIENARREIENVLHYLETEGEERAQIaynasqKYGEQSKRMSELASGTREEAEKHLKQASEIEQ 1218
Cdd:TIGR01612 1074 --------EILEEAEINITNFNEIKEKLKHYNFDDFGKEENI------KYADEINKIKDDIKNLDQKIDHHIKALEEIKK 1139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1219 LSEQAI----ANATQANKEASDAIYggeqiSKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAvSLTNVEAVK 1294
Cdd:TIGR01612 1140 KSENYIdeikAQINDLEDVADKAIS-----NDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEK-DKTSLEEVK 1213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1295 -IPSVDPKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDS 1373
Cdd:TIGR01612 1214 gINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIIS 1293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1374 vSTADKTLKDA-EAALQVLEEFGAK-----IEKSRNDAVAEFAGVEG-INQRLDDI-----IDAQDKRRNSLPIDKQF-- 1439
Cdd:TIGR01612 1294 -KKHDENISDIrEKSLKIIEDFSEEsdindIKKELQKNLLDAQKHNSdINLYLNEIaniynILKLNKIKKIIDEVKEYtk 1372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1440 -VIDYRKSADVLLNETHALADRYKD---------IIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQM 1509
Cdd:TIGR01612 1373 eIEENNKNIKDELDKSEKLIKKIKDdinleecksKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENV 1452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1510 ateavrkATLAKNSAIEANAT--ILaeedEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRA 1587
Cdd:TIGR01612 1453 -------LLLFKNIEMADNKSqhIL----KIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKK 1521
|
570 580 590
....*....|....*....|....*....|....*..
gi 392926425 1588 DEDV------------KVAQLKNDISELQKEVLNLEE 1612
Cdd:TIGR01612 1522 DVTEllnkysalaiknKFAKTKKDSEIIIKEIKDAHK 1558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1109-1547 |
8.55e-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: 47.73 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1109 TIKTKSKAIKDEIVAALEKLTSIDESVAQAkVGADAAENDMKRWEIIIENARREI------ENVLHYLETEGEERAQ--- 1179
Cdd:TIGR00606 602 SLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKQRamlagaTAVYSQFITQLTDENQscc 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1180 -IAYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAiyggEQISKQIAELKEKQNQL 1258
Cdd:TIGR00606 681 pVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII----DLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1259 NESIHRTLDLAEEQKKSADEAN---NLAAVSLTNVEAVKIPSVDPKELRNDVAGVLEESENL-VDSSVKENSANDELFDE 1334
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMpeeESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQH 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1335 VNRSVADARNELQS-SQDQQRVSDQL---MLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFA 1410
Cdd:TIGR00606 837 ELDTVVSKIELNRKlIQDQQEQIQHLkskTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1411 GVEGINQRLDDIID--------AQDKrRNSLPIDKQFVIDYRKSadvLLNETHALADRYKdiihSDVDTRDSTEAVQYdi 1482
Cdd:TIGR00606 917 FLEKDQQEKEELISsketsnkkAQDK-VNDIKEKVKNIHGYMKD---IENKIQDGKDDYL----KQKETELNTVNAQL-- 986
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926425 1483 eqlmeeltdsNENLQYYKKQAEDDKQMATEAvrKATLAKNSAIEANATILAEEDEIKKIINSLDT 1547
Cdd:TIGR00606 987 ----------EECEKHQEKINEDMRLMRQDI--DTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
835-878 |
9.12e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 9.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 392926425 835 CACsgNTDPNSIGNCDKITGECKkCIFNTHGFNCENCKPGYWGD 878
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
287-338 |
1.20e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.18 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 392926425 287 CKCNGHASECVGSSSVDGenrlVCRCEHNTQGADCNECLPFYNDRPWRSGTS 338
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG----QCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1115-1428 |
1.24e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1115 KAIKDEIVAALEKLTSIDESVAQAKVGADAAENDmkrweiiIENARREIENVLHYLETEGEERAQIAynasqkygeqsKR 1194
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELE-----------ED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1195 MSELASGtREEAEKHLKQ-ASEIEQLSEQAIANATQANK-EASDAIYGGEQISKQIAELKEKQNQLNESIH--------R 1264
Cdd:TIGR02169 746 LSSLEQE-IENVKSELKElEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqklnrL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1265 TLDLAEEQKKSADEANNLAAVSLTNVEAVKIPSVDPKELRnDVAGVLEESENLV---DSSVKENSANDELFDEVNRSVAD 1341
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALrdlESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1342 ARNELQSSQDQQRVSDQLML-----------ELEKSRERIVdSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFA 1410
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKaklealeeelsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
330
....*....|....*...
gi 392926425 1411 GVEginQRLDDIIDAQDK 1428
Cdd:TIGR02169 983 EVL---KRLDELKEKRAK 997
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1244-1516 |
1.28e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1244 ISKQIAELKEKQNQLNESIhrtldlaEEQKKSADEANNLAAvSLTNVEAVKIPSVdpKELRNDVAGVLEESENLVDsSVK 1323
Cdd:COG1340 6 LSSSLEELEEKIEELREEI-------EELKEKRDELNEELK-ELAEKRDELNAQV--KELREEAQELREKRDELNE-KVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1324 ENSAN-DELFDEVNR---SVADARNELQSSQDQQRVSDQLMLELEK------------SRER-IVDSVSTADKTLKDAEA 1386
Cdd:COG1340 75 ELKEErDELNEKLNElreELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevlspEEEKeLVEKIKELEKELEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1387 ALQVLEefgaKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLPIDKQFVIDYRKSADvllnETHALADRYK---D 1463
Cdd:COG1340 155 ALEKNE----KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD----ELHKEIVEAQekaD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 392926425 1464 IIHSDVDtrdsteAVQYDIEQLMEELTdsnenlQYYKKQAEDDKQMATEAVRK 1516
Cdd:COG1340 227 ELHEEII------ELQKELRELRKELK------KLRKKQRALKREKEKEELEE 267
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1115-1289 |
1.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1115 KAIKDEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENAR---------REIENVLHYLETEGEERAQIaynas 1185
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYEALQKEIESLKRRISDL----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1186 qkygeqSKRMSELasgtREEAEKHLKQASEIEQLSEQAIANATQANKEASDAIyggEQISKQIAELKEKQNQLNESI-HR 1264
Cdd:COG1579 109 ------EDEILEL----MERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAEREELAAKIpPE 175
|
170 180
....*....|....*....|....*
gi 392926425 1265 TLDLAEEQKKSadeANNLAAVSLTN 1289
Cdd:COG1579 176 LLALYERIRKR---KNGLAVVPVEG 197
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1301-1554 |
1.54e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1301 KELRNDVAGVLEEsenlVDSSVKENSANDeLFDEVNrsvaDARNELQSSQDQqrvsdqlMLELEKSRERIVDSVSTADKT 1380
Cdd:PRK02224 179 ERVLSDQRGSLDQ----LKAQIEEKEEKD-LHERLN----GLESELAELDEE-------IERYEEQREQARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1381 LKDAEAALQVLEEFGAKIEKSRNDavaeFAGVEGINQRLDDIIDAQDKRRNSLPIDKQfviDYRKSADVLLNETHALADR 1460
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRET----IAETEREREELAEEVRDLRERLEELEEERD---DLLAEAGLDDADAEAVEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1461 YKDIIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEANATILAEEDEIKk 1540
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE- 394
|
250
....*....|....
gi 392926425 1541 iinslDTMEEVNNA 1554
Cdd:PRK02224 395 -----ELRERFGDA 403
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1425 |
1.97e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1184 ASQKYGEQSKRMSELASgTREEAEKHLKQA-SEIEQLSEQaIANATQANKEASDAIyggEQISKQIAELKEKQNQLNESI 1262
Cdd:COG3883 14 ADPQIQAKQKELSELQA-ELEAAQAELDALqAELEELNEE-YNELQAELEALQAEI---DKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1263 HRTLDLAEEQKKSAD------EANNLAAVsLTNVEAV-KIPSVDpKELRNDVAGVLEESENlvdssvKENSANDEL--FD 1333
Cdd:COG3883 89 GERARALYRSGGSVSyldvllGSESFSDF-LDRLSALsKIADAD-ADLLEELKADKAELEA------KKAELEAKLaeLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1334 EVNRSVADARNELQSSQDQQRvsdQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVE 1413
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQE---ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|..
gi 392926425 1414 GINQRLDDIIDA 1425
Cdd:COG3883 238 AAAAAAASAAGA 249
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1115-1381 |
3.24e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.23 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1115 KAIKDEIVAALEKLTSIDesVAQAKVGADAAENDMKRWEIIIE---NARREIENVLHYLETEGEERAQIAYNASQKYGE- 1190
Cdd:pfam06160 240 QQLEEQLEENLALLENLE--LDEAEEALEEIEERIDQLYDLLEkevDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERv 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1191 -QSKRMSELASGTREEAEKHLKQASEIEQLSEQAIANATQANKEASDAIyggEQISKQIAELKEKQNQLNESIHrtlDLA 1269
Cdd:pfam06160 318 qQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEEL---EEILEQLEEIEEEQEEFKESLQ---SLR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1270 EEQKKSADEANNLAAVSLT---NVEAVKIPSVdPKELRNDVAGVLEESENLVD--SSVKENsandelFDEVNRSVADARN 1344
Cdd:pfam06160 392 KDELEAREKLDEFKLELREikrLVEKSNLPGL-PESYLDYFFDVSDEIEDLADelNEVPLN------MDEVNRLLDEAQD 464
|
250 260 270
....*....|....*....|....*....|....*..
gi 392926425 1345 ELQssqdqqrvsdqlmlELEKSRERIVDSVSTADKTL 1381
Cdd:pfam06160 465 DVD--------------TLYEKTEELIDNATLAEQLI 487
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
347-405 |
4.21e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926425 347 CNCSQ---LSNRCYFdqqlfeetgHGGHCiDCQGNTQGVHCEQCIANHWRRPGENycvACGC 405
Cdd:pfam00053 1 CDCNPhgsLSDTCDP---------ETGQC-LCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1131-1264 |
7.64e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 44.24 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1131 IDESVAQAKVGADAaendmkrweiiIENARREIENVLHYLETEGEERAQIAyNASQkygEQSKRMSELASGTREeaekhl 1210
Cdd:COG0840 423 IEEIQSETEEAVEA-----------MEEGSEEVEEGVELVEEAGEALEEIV-EAVE---EVSDLIQEIAAASEE------ 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 1211 kQASEIEQLSE--QAIANATQANKEASdaiyggEQISKQIAELKEKQNQLNESIHR 1264
Cdd:COG0840 482 -QSAGTEEVNQaiEQIAAAAQENAASV------EEVAAAAEELAELAEELQELVSR 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1057-1615 |
7.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1057 EKVKSLDNTLQEIIENPapvnDTKFDEKVKETSRAaSEVWEAVKQKTKEGGGT---IKTKSKAIKD--EIVAALEK---- 1127
Cdd:PRK03918 158 DDYENAYKNLGEVIKEI----KRRIERLEKFIKRT-ENIEELIKEKEKELEEVlreINEISSELPElrEELEKLEKevke 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1128 LTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLHYLETEGEERAQIayNASQKYGEQSKRMSELASGTREEAE 1207
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1208 KHLKQASEIEQLSEQAIANATQANKEASDAiyggEQISKQIAELKEKQNQLNESiHRTLDLAEEQKKSADE-ANNLAAVS 1286
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRLEELEER-HELYEEAKAKKEELERlKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1287 LTNVEAvKIPSVD--PKELRNDVAGVLEESENLvDSSVKENSANDELFDEVNRSVADARNELqSSQDQQRVSDQLMLELE 1364
Cdd:PRK03918 386 PEKLEK-ELEELEkaKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKAKGKCPVCGREL-TEEHRKELLEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1365 KSRERIvdsvSTADKTLKDAEAALQVLEEFGAKIEK-SRNDAVAEFagVEGINQRLDDIiDAQDKRRNSLpidkqfviDY 1443
Cdd:PRK03918 463 RIEKEL----KEIEEKERKLRKELRELEKVLKKESElIKLKELAEQ--LKELEEKLKKY-NLEELEKKAE--------EY 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1444 RKSADvLLNETHALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNS 1523
Cdd:PRK03918 528 EKLKE-KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1524 AIEANATILAEEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLlaqaqlaKEVPTYQQYRADEDvKVAQLKNDISEL 1603
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL-------EKKYSEEEYEELRE-EYLELSRELAGL 678
|
570
....*....|..
gi 392926425 1604 QKEVLNLEEIRD 1615
Cdd:PRK03918 679 RAELEELEKRRE 690
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
763-1042 |
8.14e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 43.80 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 763 CERCARGYYGDALQGTEEDCQKCPCPNDGPCIlhADGDVICTECPNGYTGRRCDECSDgyfgnpkdgtecvECACSGNTD 842
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSAPCKTENCKACS--NDKREVCEECNSNNYLTPTSQCID-------------DCAKIGNYY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 843 PNSIGNCDKITGECK--KCIFNTHGFNCENCKPGYW--GDALIEPKGNCQSCG---------CFAAGTRRPNNDYTLLEC 909
Cdd:pfam03302 66 YTTNANNKKICKECTvaNCKTCEDQGQCQACNDGFYksGDACSPCHESCKTCSggtasdcteCLTGKALRYGNDGTKGTC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 910 NQQdgqcdCLPNVIGIQCDQCAhgfYNITSGLGCQECNCDPLGSEGNTCDVNTGQCQ--CKPG-VTGQRCDRCADYHFGF 986
Cdd:pfam03302 146 GEG-----CTTGTGAGACKTCG---LTIDGTSYCSECATETEYPQNGVCTSTAARATatCKASsVANGMCSSCANGYFRM 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926425 987 -----------------SANGCQPCDCEYIGSENQQCDVNSGQCLCKENVEGRRCDQCAENRYGITQGCLPCD 1042
Cdd:pfam03302 218 nggcyettkfpgksvceEANSGGTCQKEAPGYKLNNGDLVTCSPGCKTCTSNTVCTTCMDGYVKTSDSCTKCD 290
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1190-1400 |
1.02e-03 |
|
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: 42.66 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1190 EQSKRMSELASgTREEAEKHLKQASEI----EQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIHRT 1265
Cdd:smart00283 29 ELSASIEEVAA-NADEIAATAQSAAEAaeegREAVEDAITAMDQIREVVEEAVSAVEELEESSDEIGEIVSVIDDIADQT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1266 --LDL--------AEEQKKS----ADEANNLA---AVSLTNVEAVkIPSVdpKELRNDVAGVLEESENLVDSSVKENSAN 1328
Cdd:smart00283 108 nlLALnaaieaarAGEAGRGfavvADEVRKLAersAESAKEIESL-IKEI--QEETNEAVAAMEESSSEVEEGVELVEET 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 1329 DELFDEVNRSVADARNELQ----SSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEK 1400
Cdd:smart00283 185 GDALEEIVDSVEEIADLVQeiaaATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1118-1283 |
1.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1118 KDEIVAALEKLTSIDESVAQAkvgaDAAENDMKrweiiIENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSE 1197
Cdd:COG4717 336 PEELLELLDRIEELQELLREA----EELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1198 LASGTREEAE--KHLKQASEIEQLsEQAIANATQANKEASDAIyggEQISKQIAELKEKQNQLNESihRTLDLAEEQKKS 1275
Cdd:COG4717 407 LEEQLEELLGelEELLEALDEEEL-EEELEELEEELEELEEEL---EELREELAELEAELEQLEED--GELAELLQELEE 480
|
....*....
gi 392926425 1276 A-DEANNLA 1283
Cdd:COG4717 481 LkAELRELA 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1177-1617 |
1.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1177 RAQIAYNASQKYGEQSKRMSELASGTRE--EAEKHLKQAS-EIEQLsEQAIANATQ------ANKEASDAIYGGEQISKQ 1247
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEeELEEL-EAELEELREelekleKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1248 IAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSltnVEAVKIPSVDPKELRNDVAGVLEESENLVDSSVKENSA 1327
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1328 NDELFDEVNRSVADARNELQSSQDQQRVSDQ--------LMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIE 1399
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEArlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1400 KSRNDAVAEFAGVEGINQRLDDIIDAQ-DKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKDIihsdvdtrdSTEAV 1478
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELlAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL---------QLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1479 QYDIEQLMEELTDSNENlQYYKKQAEDDKQMATEAvRKATL-----AKNSAIEANATILaEEDEIKKIINSLDTMEEVNN 1553
Cdd:COG4717 369 EQEIAALLAEAGVEDEE-ELRAALEQAEEYQELKE-ELEELeeqleELLGELEELLEAL-DEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926425 1554 AELDELEEEIDRLDQLLAQAQLAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNL 1617
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1057-1614 |
1.58e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1057 EKVKSLDNTLQ---EIIENPAPVNDTKFDEKVKETS-----RAASEVWEAVKQKTKegggtIKTKSKAIKDEIVAALEKL 1128
Cdd:TIGR00618 341 EEQRRLLQTLHsqeIHIRDAHEVATSIREISCQQHTltqhiHTLQQQKTTLTQKLQ-----SLCKELDILQREQATIDTR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1129 TSIDESVAQAKVGADAAENDMKRWEIIIENArreIENVlhYLETEGEERAQIayNASQKYGEQSKRMSELASGTREEAEK 1208
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAA---ITCT--AQCEKLEKIHLQ--ESAQSLKEREQQLQTKEQIHLQETRK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1209 HLKQASEIEQLSEQ-----------------------------AIANATQANKEASDAIYG-GEQISKQIAELKEkqnQL 1258
Cdd:TIGR00618 489 KAVVLARLLELQEEpcplcgscihpnparqdidnpgpltrrmqRGEQTYAQLETSEEDVYHqLTSERKQRASLKE---QM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1259 NESIHRTLDLAEEQKKSADEANNlaavsltnveavkipsvdpkeLRNDVAGVLEESENLVDSSVKENSANDELFDEVNRS 1338
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPN---------------------LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1339 VADARNELQSSQDQQRVS------DQLMLELEKSRERIVDSVSTADKTLKDA--EAALQVLEefgakiekSRNDAVAEFA 1410
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELAlkltalHALQLTLTQERVREHALSIRVLPKELLAsrQLALQKMQ--------SEKEQLTYWK 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1411 gvEGINQR------LDDIIDAQDKRRNSLPIDKQFVIDYRKSADVLLNETHALADRYKD--IIHSDVDTRDSTEAVQYDI 1482
Cdd:TIGR00618 697 --EMLAQCqtllreLETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvLKARTEAHFNNNEEVTAAL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1483 eQLMEELTDSNENLQYYKKQAEDDKQMAteavrkatlaknsaieanATILAEedeikkIINSLDTMEEVNNAELDELEEE 1562
Cdd:TIGR00618 775 -QTGAELSHLAAEIQFFNRLREEDTHLL------------------KTLEAE------IGQEIPSDEDILNLQCETLVQE 829
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 392926425 1563 IDRLDQLLAQ-AQLAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIR 1614
Cdd:TIGR00618 830 EEQFLSRLEEkSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1156-1392 |
1.71e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 42.22 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1156 IENARREIENVLHY----LETEGEERAQiaynASQKYGEQSKRM--SELASGTREEAEKH---LKQASEIEQL------- 1219
Cdd:pfam13949 29 LPKLKQRNREILDEaeklLDEEESEDEQ----LRAKYGTRWTRPpsSELTATLRAEIRKYreiLEQASESDSQvrskfre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1220 SEQAIANATQANKEASDAI------YGGEQISKQIAELKEKQNQLNEsihrtldLAEEQKKSADEANNLAAvsltnveav 1293
Cdd:pfam13949 105 HEEDLELLSGPDEDLEAFLpssrraKNSPSVEEQVAKLRELLNKLNE-------LKREREQLLKDLKEKAR--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1294 kipsvdpkelRNDVAGVL-EESENLVDSSVKENSANDEL--FDEVnrsvadaRNELQSSQDQQrvsDQLMLELEKSRERI 1370
Cdd:pfam13949 169 ----------NDDISPKLlLEKARLIAPNQEEQLFEEELekYDPL-------QNRLEQNLHKQ---EELLKEITEANNEF 228
|
250 260
....*....|....*....|..
gi 392926425 1371 VDSVSTADKTLKDAEAALQVLE 1392
Cdd:pfam13949 229 LQDKRVDSEKQRQREEALQKLE 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1178-1411 |
1.85e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1178 AQIAYNASQKYGEQSKRMSELASGTREEAEKHLKQASEIEQLsEQAIANATQANKEASDAIYGGEQ----ISKQIAELKE 1253
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1254 KQNQLNESIHRTLDLAEEQKK--------SADEANNlAAVSLTNVEAVKipsvdpKELRNDVAGVLEESENLvdssvken 1325
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplalllSPEDFLD-AVRRLQYLKYLA------PARREQAEELRADLAEL-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1326 sandelfDEVNRSVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQV----LEEFGAKIEKS 1401
Cdd:COG4942 163 -------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQeaeeLEALIARLEAE 235
|
250
....*....|
gi 392926425 1402 RNDAVAEFAG 1411
Cdd:COG4942 236 AAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1338-1606 |
1.88e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1338 SVADARNELQSSQDQQRVSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKsrndavaefaGVEGINQ 1417
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----------ELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1418 RLDDIIDAQDKRRNSLpiDKQFVIDYRKSAdvllnethalADRYKDIIHSdvdtrdsteavqydieqlmEELTDSNENLQ 1497
Cdd:COG4942 91 EIAELRAELEAQKEEL--AELLRALYRLGR----------QPPLALLLSP-------------------EDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1498 YYKKQAEDDKQMATEavrkatlaknsaIEANATILAE-EDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLaqAQLA 1576
Cdd:COG4942 140 YLKYLAPARREQAEE------------LRADLAELAAlRAELEAERAELEALLAELEEERAALEALKAERQKLL--ARLE 205
|
250 260 270
....*....|....*....|....*....|
gi 392926425 1577 KEVPTYQQYRADEDVKVAQLKNDISELQKE 1606
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1241-1398 |
2.33e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1241 GEQISKQIAELKEKQNQLNESIH------RTLDLAEEQKKSADEANNLAAVSLTnveavkipsvDPKELRNDVAGVLEES 1314
Cdd:pfam04108 118 RDALKELIDELQAAQESLDSDLKrfdddlRDLQKELESLSSPSESISLIPTLLK----------ELESLEEEMASLLESL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1315 ENLVDSSVK----ENSANDELFDEV---NRSVADARNELQSSQDqqrvsdqlmlELEKSRERIVDSVSTADKTLKDAEAA 1387
Cdd:pfam04108 188 TNHYDQCVTavklTEGGRAEMLEVLendARELDDVVPELQDRLD----------EMENNYERLQKLLEQKNSLIDELLSA 257
|
170
....*....|.
gi 392926425 1388 LQVLEEFGAKI 1398
Cdd:pfam04108 258 LQLIAEIQSRL 268
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
785-828 |
2.34e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.33 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 392926425 785 CPCPNDGP----CILHadgDVICtECPNGYTGRRCDECSDGYFGNPKD 828
Cdd:pfam00053 1 CDCNPHGSlsdtCDPE---TGQC-LCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1121-1250 |
3.15e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.34 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1121 IVAALEKLT-SIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLhyleTEGEERAQiaynasqkygEQSKRMSELA 1199
Cdd:cd06503 24 ILKALDEREeKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEII----EEARKEAE----------KIKEEILAEA 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 392926425 1200 sgtREEAEKHLKQA-SEIEQLSEQAIAnatQANKEASDaiyggeqISKQIAE 1250
Cdd:cd06503 90 ---KEEAERILEQAkAEIEQEKEKALA---ELRKEVAD-------LAVEAAE 128
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
785-829 |
3.51e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392926425 785 CPCPNDG----PCILHadgDVICtECPNGYTGRRCDECSDGYFGNPKDG 829
Cdd:smart00180 1 CDCDPGGsasgTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1110-1257 |
3.81e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1110 IKTKSKAIKDEIVAALEKLTSIDESVAQA-KVGADA-AENDMKRWEIIIENARREIENVLHYLETEgEERAQIAynASQK 1187
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQAnREAEEAeLEQEREIETARIAEAEAELAKKKAEERRE-AETARAE--AEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1188 YGEQS-------KRMSELASGTRE----EAEKHLKQASEIEQLSEQAIANATQANKEAS---DAIyggEQISKQIAELKE 1253
Cdd:COG2268 268 YEIAEanaerevQRQLEIAEREREielqEKEAEREEAELEADVRKPAEAEKQAAEAEAEaeaEAI---RAKGLAEAEGKR 344
|
....
gi 392926425 1254 KQNQ 1257
Cdd:COG2268 345 ALAE 348
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1049-1258 |
3.94e-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: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1049 QSRVNVFREKVKSLDNTLQEiienpapvndtkFDEKVKETSRAASEVWEAVKQKTKEGGGTIKTkSKAIKDEIVAALEKL 1128
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDE------------LRAELTLLNEEAANLRERLESLERRIAATERR-LEDLEEQIEELSEDI 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1129 TSIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLHYLETEGEERAQIAYNASQKYGEQSKRMSELASGTREEAEK 1208
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392926425 1209 HLKQASEIEQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQL 1258
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1062-1628 |
4.04e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1062 LDNTLQeIIENPAPVNDTK--FDEKVKEtsraasevweaVKQKTKEGGGTIKTKSKAIKDEIVAALEKLTSIDESVaqaK 1139
Cdd:PTZ00440 169 LDNLII-VLENPEKYNVRKtlYDEKFNE-----------YKNKKEAFYNCLKNKKEDYDKKIKKINNEIRKLLKNI---K 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1140 VGADAAENDMkrWEIIIEnarreienvlHYLETEGEeraqIAYNASQKYGEQSKRMSELASGTREEAEKHL---KQASEI 1216
Cdd:PTZ00440 234 CTGNMCKTDT--YVDMVE----------LYLLRVNE----VPSNNYDNYLNRAKELLESGSDLINKIKKELgdnKTIYSI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1217 EQLSEQAIANATQANKEASDAIYGGEQISKQIAELKEKQNQLNESIHRTLDLAE---EQKKSADEANNLAAVSLTNVEAV 1293
Cdd:PTZ00440 298 NFIQEEIGDIIKRYNFHLKKIEKGKEYIKRIQNNNIPPQVKKDELKKKYFESAKhyaSFKFSLEMLSMLDSLLIKKEKIL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1294 -------------KIPS-VDPKELRNDVAGVLEESENLVDSSVKENSANDELFDEVNRSVADARNELQSSQDQQRVS--- 1356
Cdd:PTZ00440 378 nnlfnklfgdlkeKIETlLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEIIEIKKKYDEKINElkk 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1357 --DQL------------MLELEK-SRERIVDSVSTADKTLKDAEAALQVLEEFGAKIEKSRNDAV---AEFAGVEGINQR 1418
Cdd:PTZ00440 458 siNQLktlisimksfydLIISEKdSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKnieDYYITIEGLKNE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1419 LDDIIDAQDKRRNSLpidkQFVIDYRKSADVLLNETHALADRYKDIIHSDVDTRDSTEAVQYDIEQLMEELTDSNENLQY 1498
Cdd:PTZ00440 538 IEGLIELIKYYLQSI----ETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1499 YKKQAEDDKQMATEAVRKatLAKNSAIEANATILAEEDEIKKIINSLDTMEEvnnaeldeleeeidrLDQLLAQAQlake 1578
Cdd:PTZ00440 614 FINEKNDLQEKVKYILNK--FYKGDLQELLDELSHFLDDHKYLYHEAKSKED---------------LQTLLNTSK---- 672
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 392926425 1579 vptyQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDNLPTKCFNVINLE 1628
Cdd:PTZ00440 673 ----NEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLNNIEQD 718
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1121-1266 |
4.84e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.39 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1121 IVAALEKLT-SIDESVAQAKVGADAAENDMKRWEIIIENARREIENVLHYLETEGEERAQiaynasqkygeqskrmsELA 1199
Cdd:COG0711 25 ILKALDERQeKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAE-----------------EAK 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1200 SGTREEAEKHLKQA-SEIEQLSEQAIAnatQANKEASDaiyggeqISKQIAE--LKEKqnqLNESIHRTL 1266
Cdd:COG0711 88 AEAEAEAERIIAQAeAEIEQERAKALA---ELRAEVAD-------LAVAIAEkiLGKE---LDAAAQAAL 144
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1120-1252 |
4.92e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1120 EIVAALEKLTSIDESVAQAkvgADAAENDMkrweIIIENARREIENVLHYLET------EGEERAQIAYNASQKYG---- 1189
Cdd:COG0497 248 QALRALERLAEYDPSLAEL---AERLESAL----IELEEAASELRRYLDSLEFdperleEVEERLALLRRLARKYGvtve 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392926425 1190 -------EQSKRMSELASGtrEEAEKHLKQasEIEQLSEQAIANA---TQANKEASDAIygGEQISKQIAELK 1252
Cdd:COG0497 321 ellayaeELRAELAELENS--DERLEELEA--ELAEAEAELLEAAeklSAARKKAAKKL--EKAVTAELADLG 387
|
|
| Prominin |
pfam05478 |
Prominin; The prominins are an emerging family of proteins that among the multispan membrane ... |
1178-1396 |
5.52e-03 |
|
Prominin; The prominins are an emerging family of proteins that among the multispan membrane proteins display a novel topology. Mouse prominin and human prominin (mouse)-like 1 (PROML1) are predicted to contain five membrane spanning domains, with an N-terminal domain exposed to the extracellular space followed by four, alternating small cytoplasmic and large extracellular, loops and a cytoplasmic C-terminal domain. The exact function of prominin is unknown although in humans defects in PROM1, the gene coding for prominin, cause retinal degeneration.
Pssm-ID: 461660 [Multi-domain] Cd Length: 799 Bit Score: 41.46 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1178 AQIAYNASQKYGEQSKRMSELASGtreeAEKHLkqASEIEQLSEQAIANA-------TQANKEASDAIyggEQISKQIAE 1250
Cdd:pfam05478 194 QHIDHVLVQNYSELQDHVSDDLDD----AGKHI--GLDIHDTLESNVYPAlaeleriLQNMPEAKDLL---EQVNALLKD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1251 LKEKQNQLN-------ESIHRTLDLAEEQKKSADEAN-NLAAVSL-TNVEAVKIPSVDpkELRNDVAGVLEESenlVDSS 1321
Cdd:pfam05478 265 LRFYGTQLRdglrgvkRDLNYALSNPLCTTQECDKFLsSLSIEFLdTSACLDQLPNVD--EFLENVKGVIETN---LSSI 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392926425 1322 VKE-NSANDELFDEVNRSVADARNELQSSQDQQRvSDQLMLELEKSRERIVDSVSTADKTLKDAEAALQVLEEFGA 1396
Cdd:pfam05478 340 VQEgLDRFNNIPEKVKNQTAGVVPPLKRALAQIR-EQIRTLATDIPRDALSAVSSDIHNTERSSRTFLDVVEKYGS 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1119-1260 |
6.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1119 DEIVAALEKLTSIDESVAQAKVGADAAENDMKRWEIIIENARREIENVL------HYLETEGEERAQIAyNASQKYGEQS 1192
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQLAELEAELA-ELSARYTPNH 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926425 1193 KRMSELASgTREEAEKHLKQasEIEQLSEQAIANATQANKEAsdaiyggEQISKQIAELKEKQNQLNE 1260
Cdd:COG3206 291 PDVIALRA-QIAALRAQLQQ--EAQRILASLEAELEALQARE-------ASLQAQLAQLEARLAELPE 348
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1152-1324 |
6.52e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.38 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1152 WEIIIENARREIENVLHYLETEGEERA-QIAYNASQKYGEQSKRMSELASG----TREEAEKHLKQA-SEIEQLSEQAIA 1225
Cdd:PRK06669 42 EEEQVEQLREEANDEAKEIIEEAEEDAfEIVEAAEEEAKEELLKKTDEASSiiekLQMQIEREQEEWeEELERLIEEAKA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1226 NATQANKEASDAiyggeqisKQIAELKEKQNQLNESIHRTLDLAEEQKKSADEANNLAAVSLtnveAVKIpsvdpkelrn 1305
Cdd:PRK06669 122 EGYEEGYEKGRE--------EGLEEVRELIEQLNKIIEKLIKKREEILESSEEEIVELALDI----AKKV---------- 179
|
170
....*....|....*....
gi 392926425 1306 dVAGVLEESENLVDSSVKE 1324
Cdd:PRK06669 180 -IKEISENSKEIALALVKE 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1389-1618 |
6.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1389 QVLEEF--GAKIEksrnDAVAEFAGVEGINQRLDDiidAQDKRRNSLPIDKQFViDYRKSAdvllnETHALADRYKDIIH 1466
Cdd:COG4913 216 YMLEEPdtFEAAD----ALVEHFDDLERAHEALED---AREQIELLEPIRELAE-RYAAAR-----ERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1467 SDVDTRdSTEAVQYDIEQLMEELTDSNENLQyykkQAEDDKQMATEAVRKATLAKNSA----IEA-NATILAEEDEIKKI 1541
Cdd:COG4913 283 LWFAQR-RLELLEAELEELRAELARLEAELE----RLEARLDALREELDELEAQIRGNggdrLEQlEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1542 INSLDTMEEVNNAELDELEEEIDRLDQLLAQAQ-----LAKEVPTYQQYRADEDVKVAQLKNDISELQKEVLNLEEIRDN 1616
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
..
gi 392926425 1617 LP 1618
Cdd:COG4913 438 IP 439
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1300-1620 |
7.80e-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: 41.20 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1300 PKELRN---DVAGVL------EESENlvdssvKENSANDELfdevNRsVADARNELQSSQD---QQRVSDQLMLELEKSR 1367
Cdd:TIGR02168 154 PEERRAifeEAAGISkykerrKETER------KLERTRENL----DR-LEDILNELERQLKsleRQAEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1368 ERIVDSVSTADktLKDAEAALQVLEEFGAKIEKSRNDAVAEFAGVEGINQRLDDIIDAQDKRRNSLpidkqfvidyrksa 1447
Cdd:TIGR02168 223 RELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-------------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1448 dvllneTHALADRYKDIihSDVDTRdsteavqydIEQLMEELTDSNENLQYYKKQAEDDKQMATEAVRKATLAKNSAIEA 1527
Cdd:TIGR02168 287 ------QKELYALANEI--SRLEQQ---------KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926425 1528 NATILAEEDEIKKIINSLDTMEEVNNAELDELEEEIDRLDQLLAQ-AQLAKEVPTYQQYRADEDVKVAQLKNDISELQKE 1606
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
330
....*....|....*.
gi 392926425 1607 V--LNLEEIRDNLPTK 1620
Cdd:TIGR02168 430 LeeAELKELQAELEEL 445
|
|
| |
