|
Name |
Accession |
Description |
Interval |
E-value |
| LamB |
smart00281 |
Laminin B domain; |
308-433 |
3.79e-41 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 147.41 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 308 RLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVD--RGGRHPSAHDVILEGAGLRITAPLMplGKTLPCGLTK-TYTFRLNE 384
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHPAE--GPPLPDELTTvEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 385 HPSNNWSPQLSYfEYRRLLRNLTALRIRATYGEYSTG-YIDNVTLISARP 433
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
313-443 |
3.77e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 136.25 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 313 YFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAH---DVILEGAGLRITAPLMPLGKTLPcGLTKTYTFRLNEHpsnN 389
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNsepDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEE---N 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 390 W----SPQLSYFEYRRLLRNLTALRIRATYGEYSTG-YIDNVTLISARP-VSGAPAPWVE 443
Cdd:pfam00052 77 WrdsdGAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPgGSGPPASWVE 136
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
677-1216 |
5.30e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.08 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMdqFMQQLQ-RMEALISKAQggdgvvpdTELEGRMQQAEQAlqdilrdaqisEGASRSLGLQLA----KVRSQE 751
Cdd:pfam15921 254 SQNKIEL--LLQQHQdRIEQLISEHE--------VEITGLTEKASSA-----------RSQANSIQSQLEiiqeQARNQN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 752 NSYQSRLDDLKMTVERVRA----LGSQYQNRVRDTHRlitqmQLSLAESEASLGNTNipaSDHYVGPNGF------KSLA 821
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSelreAKRMYEDKIEELEK-----QLVLANSELTEARTE---RDQFSQESGNlddqlqKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 822 QEATRLAESHVESASN-------------MEQLTRETEDYSK--QALSLVRKALHEGVgSGSGSPDGAVVQGLVEKLEKT 886
Cdd:pfam15921 385 DLHKREKELSLEKEQNkrlwdrdtgnsitIDHLRRELDDRNMevQRLEALLKAMKSEC-QGQMERQMAAIQGKNESLEKV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 887 KSLAQQL--TREATQAEIEADRSYQHSLRlldsvSRLQGVSDQSFQVEEAKR-IKQKADSLSSLVTR------HMDEFKR 957
Cdd:pfam15921 464 SSLTAQLesTKEMLRKVVEELTAKKMTLE-----SSERTVSDLTASLQEKERaIEATNAEITKLRSRvdlklqELQHLKN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 958 TQKNLGNWKEEAQQL-LQngKSGREKSDQLLSRA--NLAKSRAQEALSMGnatfyeveSILKNLREFDLQVDNRKAEAEE 1034
Cdd:pfam15921 539 EGDHLRNVQTECEALkLQ--MAEKDKVIEILRQQieNMTQLVGQHGRTAG--------AMQVEKAQLEKEINDRRLELQE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1035 aMKRLsyisqkvsdaSDKTQQAERALGSAAADAQRAK----NGAGEALEISSEIEQEIGSLNLEANVTadgalamEKGLA 1110
Cdd:pfam15921 609 -FKIL----------KDKKDAKIRELEARVSDLELEKvklvNAGSERLRAVKDIKQERDQLLNEVKTS-------RNELN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1111 SLKSEMREVEGELERKELEFDTNMDAVQMVITEAQK--------------VDTRAKNAGVTIQDTLNTLDGLLHLMDQPL 1176
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSeleqtrntlksmegSDGHAMKVAMGMQKQITAKRGQIDALQSKI 750
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1177 SVDEEGLV--------LLEQ--KLSRAKTQINSQLRPMMSELEERARQQR 1216
Cdd:pfam15921 751 QFLEEAMTnankekhfLKEEknKLSQELSTVATEKNKMAGELEVLRSQER 800
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
146-190 |
1.72e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 1.72e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2462509082 146 PCNCNSKGSLSARCD-NSGRCSCKPGVTGARCDRCLPGFHMLTDAG 190
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
147-191 |
4.23e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 4.23e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2462509082 147 CNCNSKGSLSARCD-NSGRCSCKPGVTGARCDRCLPGFHMLTDAGC 191
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
677-1236 |
6.77e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMDQFMQQLQRMEALIskaqggdgvvpdTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQS 756
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAEL------------EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 757 RLDDLKMTVER----VRALGSQYQ-NRVRDTHRLIT---QMQLSLAESEASLGNTNIPASDHYVgpngfksLAQEATRLA 828
Cdd:TIGR02168 408 RLERLEDRRERlqqeIEELLKKLEeAELKELQAELEeleEELEELQEELERLEEALEELREELE-------EAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 829 ESHVESASN----MEQLTRETEDYSKQalslVRKALHEGvgSGSGSPDGAVVQGLV--EKLEKTKSLA-----QQL---T 894
Cdd:TIGR02168 481 ERELAQLQArldsLERLQENLEGFSEG----VKALLKNQ--SGLSGILGVLSELISvdEGYEAAIEAAlggrlQAVvveN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 895 REATQAEIEADRsyQHSLRLLdSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVtRHMDEFKRTQKNLGNW--------- 965
Cdd:TIGR02168 555 LNAAKKAIAFLK--QNELGRV-TFLPLDSIKGTEIQGNDREILKNIEGFLGVAK-DLVKFDPKLRKALSYLlggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 966 KEEAQQLL----------------------QNGKSGREKSDQLLSRANLAKSRAQ-----EALSMGNATFYEVESILKNL 1018
Cdd:TIGR02168 631 LDNALELAkklrpgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKieeleEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1019 REFDLQVDNRKAEAE----EAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLE 1094
Cdd:TIGR02168 711 EEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1095 ANVTADGALAMEKGLASLKSEMREVEGEL-----ERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVT-----IQDTLNT 1164
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAaeieeLEELIEE 870
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509082 1165 L-DGLLHLMDQpLSVDEEGLVLLEQKLSRAKTQINSqLRPMMSELEERARQQRGHLHLLETSIDGILADVKNL 1236
Cdd:TIGR02168 871 LeSELEALLNE-RASLEEALALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
202-247 |
8.67e-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: 60.83 E-value: 8.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462509082 202 CDCDPAGIAGP-CDA--GRCVCKPAVTGERCDRCRSGYYNLDGGNPEGC 247
Cdd:pfam00053 1 CDCNPHGSLSDtCDPetGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
147-186 |
1.00e-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: 60.83 E-value: 1.00e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2462509082 147 CNCNSKGSLSARCD-NSGRCSCKPGVTGARCDRCLPGFHML 186
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
579-628 |
1.17e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 1.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 579 PCQCNNNvdPSASGNCDRLTGRCLkCIHNTAGIYCDQCKAGYFGDPLAPN 628
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
710-1223 |
3.00e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 710 TELEGRMQ----QAEQA-----LQDILRDAQISEGAS--RSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNR 778
Cdd:COG1196 196 GELERQLEplerQAEKAeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 779 VRDTHRLITQMQLSLAESEASLGNTNipasdhyvgpNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRK 858
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLE----------QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 859 ALHEgvgsgsgspdGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAK--- 935
Cdd:COG1196 346 LEEA----------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALler 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 936 --RIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVES 1013
Cdd:COG1196 416 leRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1014 ILKNLREFDLQVDNRKAEAEEAMKRLsyISQKVSDASDKTQQAERALgsAAADAQRAKNGAGEALEISSEIEQEIGSLNL 1093
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRG--LAGAVAVLIGVEAAYEAAL--EAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1094 EAnVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMD 1173
Cdd:COG1196 572 GR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1174 QPLSVDEEGLVLLEQKLSRAKTQINSQLRpMMSELEERARQQRGHLHLLE 1223
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEA-ELEELAERLAEEELELEEAL 699
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
202-247 |
4.18e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 4.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462509082 202 CDCDPAGIAGP-CDA--GRCVCKPAVTGERCDRCRSGYYnldGGNPEGC 247
Cdd:smart00180 1 CDCDPGGSASGtCDPdtGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
580-627 |
5.69e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.82 E-value: 5.69e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462509082 580 CQCNNNVdpSASGNCDRLTGRCLkCIHNTAGIYCDQCKAGYFGDPLAP 627
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
202-248 |
3.23e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 3.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 202 CDCDPAGIAGP-CDA--GRCVCKPAVTGERCDRCRSGYYNLDgGNPEGCT 248
Cdd:cd00055 2 CDCNGHGSLSGqCDPgtGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1243 |
3.33e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRdaQISEGAS--RSLGLQLAKVRSQensYQsRLDDLKMTVERVRALGSQYQNRVRDTHRLITQ 788
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR--EINEISSelPELREELEKLEKE---VK-ELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 789 MQLSLAESEASLgntnipasdhyvgpngfKSLAQEATRLAESHvESASNMEQLTRETEDYsKQALSLVRKALhegvgsGS 868
Cdd:PRK03918 264 LEERIEELKKEI-----------------EELEEKVKELKELK-EKAEEYIKLSEFYEEY-LDELREIEKRL------SR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 869 GSPDGAVVQGLVEKLEKTKSLAQQLTREATQ-----AEIEAD-RSYQHSLRLLDSVSRLQgvsdQSFQVEEAKRIKQKAD 942
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKElekrlEELEERhELYEEAKAKKEELERLK----KRLTGLTPEKLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 943 SLSSLVTRHMDEFKRTQKNLGNWKEEAQQL------LQNGKS-----GREKSDQllSRANL-AKSRAqealsmgnatfyE 1010
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELkkaieeLKKAKGkcpvcGRELTEE--HRKELlEEYTA------------E 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1011 VESILKNLREFDLQVDNRKAEAEEAMKRLSYISQ--KVSDASDKTQQAERALGS-AAADAQRAKNGAGEALEISSEIEQE 1087
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1088 IGSLNLEANVTADgalaMEKGLASLKSEMREVEGEL-----ERKELEFDTnMDAVQMVITEAQKVDTR---AKNAGVTIQ 1159
Cdd:PRK03918 541 IKSLKKELEKLEE----LKKKLAELEKKLDELEEELaellkELEELGFES-VEELEERLKELEPFYNEyleLKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1160 DTLNTLDGLlhlmDQPLSVDEEGLVLLEQKLSRAKTQINS-----------QLRPMMSELEERARQQRGHLHLLETSIDG 1228
Cdd:PRK03918 616 REEKELKKL----EEELDKAFEELAETEKRLEELRKELEElekkyseeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
570
....*....|....*
gi 2462509082 1229 ILADVKNLENIRDNL 1243
Cdd:PRK03918 692 IKKTLEKLKEELEER 706
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
580-624 |
5.99e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 5.99e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2462509082 580 CQCNnnVDPSASGNCDRLTGRCLkCIHNTAGIYCDQCKAGYFGDP 624
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-572 |
1.14e-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: 46.58 E-value: 1.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462509082 524 PCPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGYFGDPFGEHG 572
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
823-1169 |
2.03e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.52 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 823 EATRLAESHV-ESASNMEQLTRETEdysKQALSLVRKALHEGvgsgsgspDGAVVQGLVEKLEKTKSLAQQLTREATQAE 901
Cdd:NF041483 138 ERRQTVESHVnENVAWAEQLRARTE---SQARRLLDESRAEA--------EQALAAARAEAERLAEEARQRLGSEAESAR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 902 IEAD----RSYQHSLRLLDSVS-RLQGVSDQSFQ-----VEEAKRIKQKADSLSSLVTRHMDEFKR--------TQKNLG 963
Cdd:NF041483 207 AEAEailrRARKDAERLLNAAStQAQEATDHAEQlrsstAAESDQARRQAAELSRAAEQRMQEAEEalrearaeAEKVVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 964 NWKEEAQQLLQNGKSGREKsdqllsRANLAKSR----AQEALSMGNATFYEVESILKNLREfdlQVDNRKAEAEEAmKRL 1039
Cdd:NF041483 287 EAKEAAAKQLASAESANEQ------RTRTAKEEiarlVGEATKEAEALKAEAEQALADARA---EAEKLVAEAAEK-ART 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1040 SYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALE-ISSEIEQEIGSLNLEANVTADGAlameKGLA-------- 1110
Cdd:NF041483 357 VAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAErIRREAEAEADRLRGEAADQAEQL----KGAAkddtkeyr 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462509082 1111 ----SLKSEMREVEGELERKELEfdtnmdavqmVITEAQKVDTRAKNAGVT-IQDTLNTLDGLL 1169
Cdd:NF041483 433 aktvELQEEARRLRGEAEQLRAE----------AVAEGERIRGEARREAVQqIEEAARTAEELL 486
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
635-667 |
6.69e-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: 44.27 E-value: 6.69e-06
10 20 30
....*....|....*....|....*....|....
gi 2462509082 635 ACNCNPMGSEPVGC-RSDGTCVCKPGFGGPNCEH 667
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDR 34
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-571 |
7.03e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 7.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2462509082 525 CPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGYFGDPFGEH 571
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
636-667 |
2.12e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.11 E-value: 2.12e-05
10 20 30
....*....|....*....|....*....|...
gi 2462509082 636 CNCNPMGSEPVGC-RSDGTCVCKPGFGGPNCEH 667
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDR 33
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
636-667 |
4.97e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 4.97e-05
10 20 30
....*....|....*....|....*....|...
gi 2462509082 636 CNCNPMGSEPVGCRSD-GTCVCKPGFGGPNCEH 667
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDR 33
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
884-1154 |
1.28e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 884 EKTKSLAQQLTREATQAEIEADR---------------------SYQ-HSLRLLDSVSRLQGVSDQ--SFQVEEAKRIKQ 939
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADRlrgeaadqaeqlkgaakddtkEYRaKTVELQEEARRLRGEAEQlrAEAVAEGERIRG 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 940 KAdslSSLVTRHMDEFKRTQKN-LGNWKEEAQQLLQNGKSGREK-SDQLLSRAN---------LAKSRAQ------EALS 1002
Cdd:NF041483 466 EA---RREAVQQIEEAARTAEElLTKAKADADELRSTATAESERvRTEAIERATtlrrqaeetLERTRAEaerlraEAEE 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1003 MGNATFYEVESILKNLR-EFDLQVDNRKAEAEEAMKRLSyisqkvSDASDKTQQAERALGSAAADAQRAKNGAGEALE-- 1079
Cdd:NF041483 543 QAEEVRAAAERAARELReETERAIAARQAEAAEELTRLH------TEAEERLTAAEEALADARAEAERIRREAAEETErl 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1080 ----------ISSEIEQEIGSLNLEANVTADGALAMEKGLA-SLKSemrEVEGELERKELEFDTNMDAVQM-VITEAQKV 1147
Cdd:NF041483 617 rteaaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAvRLRS---EAAAEAERLKSEAQESADRVRAeAAAAAERV 693
|
....*..
gi 2462509082 1148 DTRAKNA 1154
Cdd:NF041483 694 GTEAAEA 700
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
547-572 |
2.30e-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: 2.30e-03
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
91-149 |
3.47e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 3.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462509082 91 CDCNG---KSRQCifdrelHRQTGngfRCLnCNDNTDGIHCEKCKNGFYRHRerdRCLPCNC 149
Cdd:pfam00053 1 CDCNPhgsLSDTC------DPETG---QCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
91-141 |
3.89e-03 |
|
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: 36.56 E-value: 3.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462509082 91 CDCNG---KSRQCifdrelHRQTGngfRCLnCNDNTDGIHCEKCKNGFYRHRER 141
Cdd:cd00055 2 CDCNGhgsLSGQC------DPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
954-1174 |
7.30e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.35 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 954 EFKRTQKNLGNWKEEAQQLLQNGKSGREKSdqllsranlaksraqealsmgnatfyEVESILKNLREFDLQVDNRK---- 1029
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLE--------------------------SVEALLKKHEALEAELAAHEerve 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1030 ---AEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLN-LEANVTADGALAM 1105
Cdd:cd00176 58 alnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEeKEAALASEDLGKD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509082 1106 EKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAgvTIQDTLNTLDGLLHLMDQ 1174
Cdd:cd00176 138 LESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEE--KLEELNERWEELLELAEE 204
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamB |
smart00281 |
Laminin B domain; |
308-433 |
3.79e-41 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 147.41 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 308 RLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVD--RGGRHPSAHDVILEGAGLRITAPLMplGKTLPCGLTK-TYTFRLNE 384
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDgrRGGTHVSAPDVILEGNGLRISHPAE--GPPLPDELTTvEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 385 HPSNNWSPQLSYfEYRRLLRNLTALRIRATYGEYSTG-YIDNVTLISARP 433
Cdd:smart00281 79 WQYYGGRPVTRE-DLMMVLANLTAILIRATYSQQMAGsRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
313-443 |
3.77e-37 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 136.25 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 313 YFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAH---DVILEGAGLRITAPLMPLGKTLPcGLTKTYTFRLNEHpsnN 389
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNsepDVILEGNGLRLSYSSPDQPPPDP-GQEQTYSVRLHEE---N 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 390 W----SPQLSYFEYRRLLRNLTALRIRATYGEYSTG-YIDNVTLISARP-VSGAPAPWVE 443
Cdd:pfam00052 77 WrdsdGAPVSREDFMMVLANLTAILIRATYSTGSGQvSLSNVSLDSAVPgGSGPPASWVE 136
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
677-1216 |
5.30e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.08 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMdqFMQQLQ-RMEALISKAQggdgvvpdTELEGRMQQAEQAlqdilrdaqisEGASRSLGLQLA----KVRSQE 751
Cdd:pfam15921 254 SQNKIEL--LLQQHQdRIEQLISEHE--------VEITGLTEKASSA-----------RSQANSIQSQLEiiqeQARNQN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 752 NSYQSRLDDLKMTVERVRA----LGSQYQNRVRDTHRlitqmQLSLAESEASLGNTNipaSDHYVGPNGF------KSLA 821
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSelreAKRMYEDKIEELEK-----QLVLANSELTEARTE---RDQFSQESGNlddqlqKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 822 QEATRLAESHVESASN-------------MEQLTRETEDYSK--QALSLVRKALHEGVgSGSGSPDGAVVQGLVEKLEKT 886
Cdd:pfam15921 385 DLHKREKELSLEKEQNkrlwdrdtgnsitIDHLRRELDDRNMevQRLEALLKAMKSEC-QGQMERQMAAIQGKNESLEKV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 887 KSLAQQL--TREATQAEIEADRSYQHSLRlldsvSRLQGVSDQSFQVEEAKR-IKQKADSLSSLVTR------HMDEFKR 957
Cdd:pfam15921 464 SSLTAQLesTKEMLRKVVEELTAKKMTLE-----SSERTVSDLTASLQEKERaIEATNAEITKLRSRvdlklqELQHLKN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 958 TQKNLGNWKEEAQQL-LQngKSGREKSDQLLSRA--NLAKSRAQEALSMGnatfyeveSILKNLREFDLQVDNRKAEAEE 1034
Cdd:pfam15921 539 EGDHLRNVQTECEALkLQ--MAEKDKVIEILRQQieNMTQLVGQHGRTAG--------AMQVEKAQLEKEINDRRLELQE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1035 aMKRLsyisqkvsdaSDKTQQAERALGSAAADAQRAK----NGAGEALEISSEIEQEIGSLNLEANVTadgalamEKGLA 1110
Cdd:pfam15921 609 -FKIL----------KDKKDAKIRELEARVSDLELEKvklvNAGSERLRAVKDIKQERDQLLNEVKTS-------RNELN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1111 SLKSEMREVEGELERKELEFDTNMDAVQMVITEAQK--------------VDTRAKNAGVTIQDTLNTLDGLLHLMDQPL 1176
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSeleqtrntlksmegSDGHAMKVAMGMQKQITAKRGQIDALQSKI 750
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1177 SVDEEGLV--------LLEQ--KLSRAKTQINSQLRPMMSELEERARQQR 1216
Cdd:pfam15921 751 QFLEEAMTnankekhfLKEEknKLSQELSTVATEKNKMAGELEVLRSQER 800
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
146-190 |
1.72e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 1.72e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2462509082 146 PCNCNSKGSLSARCD-NSGRCSCKPGVTGARCDRCLPGFHMLTDAG 190
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
147-191 |
4.23e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 4.23e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2462509082 147 CNCNSKGSLSARCD-NSGRCSCKPGVTGARCDRCLPGFHMLTDAGC 191
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
677-1236 |
6.77e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMDQFMQQLQRMEALIskaqggdgvvpdTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQS 756
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAEL------------EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 757 RLDDLKMTVER----VRALGSQYQ-NRVRDTHRLIT---QMQLSLAESEASLGNTNIPASDHYVgpngfksLAQEATRLA 828
Cdd:TIGR02168 408 RLERLEDRRERlqqeIEELLKKLEeAELKELQAELEeleEELEELQEELERLEEALEELREELE-------EAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 829 ESHVESASN----MEQLTRETEDYSKQalslVRKALHEGvgSGSGSPDGAVVQGLV--EKLEKTKSLA-----QQL---T 894
Cdd:TIGR02168 481 ERELAQLQArldsLERLQENLEGFSEG----VKALLKNQ--SGLSGILGVLSELISvdEGYEAAIEAAlggrlQAVvveN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 895 REATQAEIEADRsyQHSLRLLdSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVtRHMDEFKRTQKNLGNW--------- 965
Cdd:TIGR02168 555 LNAAKKAIAFLK--QNELGRV-TFLPLDSIKGTEIQGNDREILKNIEGFLGVAK-DLVKFDPKLRKALSYLlggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 966 KEEAQQLL----------------------QNGKSGREKSDQLLSRANLAKSRAQ-----EALSMGNATFYEVESILKNL 1018
Cdd:TIGR02168 631 LDNALELAkklrpgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKieeleEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1019 REFDLQVDNRKAEAE----EAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLE 1094
Cdd:TIGR02168 711 EEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1095 ANVTADGALAMEKGLASLKSEMREVEGEL-----ERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVT-----IQDTLNT 1164
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAaeieeLEELIEE 870
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509082 1165 L-DGLLHLMDQpLSVDEEGLVLLEQKLSRAKTQINSqLRPMMSELEERARQQRGHLHLLETSIDGILADVKNL 1236
Cdd:TIGR02168 871 LeSELEALLNE-RASLEEALALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
202-247 |
8.67e-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: 60.83 E-value: 8.67e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462509082 202 CDCDPAGIAGP-CDA--GRCVCKPAVTGERCDRCRSGYYNLDGGNPEGC 247
Cdd:pfam00053 1 CDCNPHGSLSDtCDPetGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
147-186 |
1.00e-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: 60.83 E-value: 1.00e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2462509082 147 CNCNSKGSLSARCD-NSGRCSCKPGVTGARCDRCLPGFHML 186
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
711-1237 |
3.27e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQ 790
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 791 LSLAESEASLGNTNipASDHYVGPNgFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRK--ALHEGVGSGS 868
Cdd:TIGR02168 323 AQLEELESKLDELA--EELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 869 G--SPDGAVVQGLVEKLEKTKSLAQQLTRE-------ATQAEIEADRSYQHSL--RLLDSVSRLQGVSDQSFQVEEA--- 934
Cdd:TIGR02168 400 NeiERLEARLERLEDRRERLQQEIEELLKKleeaelkELQAELEELEEELEELqeELERLEEALEELREELEEAEQAlda 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 935 -----KRIKQKADSLSSLVTRHMDEFK--RTQKNLGNWKEEAQQLLQNGKSGREK------------SDQLLSRANLAKS 995
Cdd:TIGR02168 480 aerelAQLQARLDSLERLQENLEGFSEgvKALLKNQSGLSGILGVLSELISVDEGyeaaieaalggrLQAVVVENLNAAK 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 996 RAQEAL---SMGNATFYEVESIlknlREFDLQVDNRKAEAEEAmKRLSYISQKVSDASdktqQAERALGSAAADAQRAKN 1072
Cdd:TIGR02168 560 KAIAFLkqnELGRVTFLPLDSI----KGTEIQGNDREILKNIE-GFLGVAKDLVKFDP----KLRKALSYLLGGVLVVDD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1073 GAgEALEISSEIEQEigslnlEANVTADGALAMEKGLASLKSEMRE---VEGELERKELEfdTNMDAVQMVITEAQKVDT 1149
Cdd:TIGR02168 631 LD-NALELAKKLRPG------YRIVTLDGDLVRPGGVITGGSAKTNssiLERRREIEELE--EKIEELEEKIAELEKALA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1150 RAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAkTQINSQLRPMMSELEERARQQRGHLHLLETSIDGI 1229
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
....*...
gi 2462509082 1230 LADVKNLE 1237
Cdd:TIGR02168 781 EAEIEELE 788
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
579-628 |
1.17e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 1.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 579 PCQCNNNvdPSASGNCDRLTGRCLkCIHNTAGIYCDQCKAGYFGDPLAPN 628
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
710-1223 |
3.00e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 710 TELEGRMQ----QAEQA-----LQDILRDAQISEGAS--RSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNR 778
Cdd:COG1196 196 GELERQLEplerQAEKAeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 779 VRDTHRLITQMQLSLAESEASLGNTNipasdhyvgpNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRK 858
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLE----------QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 859 ALHEgvgsgsgspdGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAK--- 935
Cdd:COG1196 346 LEEA----------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALler 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 936 --RIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVES 1013
Cdd:COG1196 416 leRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1014 ILKNLREFDLQVDNRKAEAEEAMKRLsyISQKVSDASDKTQQAERALgsAAADAQRAKNGAGEALEISSEIEQEIGSLNL 1093
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRG--LAGAVAVLIGVEAAYEAAL--EAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1094 EAnVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMD 1173
Cdd:COG1196 572 GR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1174 QPLSVDEEGLVLLEQKLSRAKTQINSQLRpMMSELEERARQQRGHLHLLE 1223
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEA-ELEELAERLAEEELELEEAL 699
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
202-247 |
4.18e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 4.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462509082 202 CDCDPAGIAGP-CDA--GRCVCKPAVTGERCDRCRSGYYnldGGNPEGC 247
Cdd:smart00180 1 CDCDPGGSASGtCDPdtGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
580-627 |
5.69e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.82 E-value: 5.69e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2462509082 580 CQCNNNVdpSASGNCDRLTGRCLkCIHNTAGIYCDQCKAGYFGDPLAP 627
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDP 45
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
677-1138 |
8.62e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMDQFMQQLQRMEALISKAQggdgvvpdTELEGRMQQAEQALQdilrdaqiseGASRSLglqlAKVRSQENSYQS 756
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMK--------SECQGQMERQMAAIQ----------GKNESL----EKVSSLTAQLES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 757 RLDDLKMTVERVRALGSQYQNrvrdTHRLITQMQLSLAESEASLGNTNIPA----SDHYVGPNGFKSLAQEATRLaeSHV 832
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLES----SERTVSDLTASLQEKERAIEATNAEItklrSRVDLKLQELQHLKNEGDHL--RNV 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 833 ESASNMEQLTRETEDYSKQALSLVRKALHEGVGSgSGSPDGAVvqgLVEKLEKTKSLAQQlTREATQAEIEADRSyQHSL 912
Cdd:pfam15921 547 QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ-HGRTAGAM---QVEKAQLEKEINDR-RLELQEFKILKDKK-DAKI 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 913 RLLDS------VSRLQGVSDQSFQVEEAKRIKQKADSLsslvtrhMDEFKRTQKNLGNWKEEAQQLLQNGksgREKSDQL 986
Cdd:pfam15921 621 RELEArvsdleLEKVKLVNAGSERLRAVKDIKQERDQL-------LNEVKTSRNELNSLSEDYEVLKRNF---RNKSEEM 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 987 LSRANLAKSRAQEALSmgnatfyEVESILKNLREFDlQVDNRKAEAEEAM-KRLSYISQKVSDASDKTQQAERALGSAAA 1065
Cdd:pfam15921 691 ETTTNKLKMQLKSAQS-------ELEQTRNTLKSME-GSDGHAMKVAMGMqKQITAKRGQIDALQSKIQFLEEAMTNANK 762
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509082 1066 DAQRAKngagealEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQ 1138
Cdd:pfam15921 763 EKHFLK-------EEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
891-1241 |
2.70e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 891 QQLTREATQAEiEAdRSYQHSLRLLDSvsRLQGVSDQSFQvEEAKRIKQKADSLSSLvtrhmdefkrtqknlgnwKEEAQ 970
Cdd:COG1196 203 EPLERQAEKAE-RY-RELKEELKELEA--ELLLLKLRELE-AELEELEAELEELEAE------------------LEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 971 QLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLsyiSQKVSDAS 1050
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1051 DKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEF 1130
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1131 DTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQplsvDEEGLVLLEQKLSRAKTQINSQLRPmmselEE 1210
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEE-----LA 487
|
330 340 350
....*....|....*....|....*....|.
gi 2462509082 1211 RARQQRGHLHLLETSIDGILADVKNLENIRD 1241
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
202-248 |
3.23e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 3.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 202 CDCDPAGIAGP-CDA--GRCVCKPAVTGERCDRCRSGYYNLDgGNPEGCT 248
Cdd:cd00055 2 CDCNGHGSLSGqCDPgtGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
976-1238 |
3.29e-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: 61.62 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 976 GKSGREKSDQLLSRANLAKSRAQEAlsmgnatfyEVESiLKNLREFdLQVDNRKAEaeeamKRLSYISQKVSDASDKTQQ 1055
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAELQRLRE---------RLEG-LKRELSS-LQSELRRIE-----NRLDELSQELSDASRKIGE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1056 AERALGSAAADAQRAKngagealEISSEIEQEIGSLnleanvtadgalamEKGLASLKSEMREVEGELERKE-------- 1127
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLK-------ERLEELEEDLSSL--------------EQEIENVKSELKELEARIEELEedlhklee 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1128 ----LEFDTNMDAVQMVITEAQKV-DTRAKNAGVT--IQDTLNTLDGLLHLMDQPLSVDEEGLVLLE-QKLSRAKTQINS 1199
Cdd:TIGR02169 780 alndLEARLSHSRIPEIQAELSKLeEEVSRIEARLreIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENL 859
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462509082 1200 QLRpmMSELEERARQQRGHLHLLETSIDGILADVKNLEN 1238
Cdd:TIGR02169 860 NGK--KEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1243 |
3.33e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRdaQISEGAS--RSLGLQLAKVRSQensYQsRLDDLKMTVERVRALGSQYQNRVRDTHRLITQ 788
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR--EINEISSelPELREELEKLEKE---VK-ELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 789 MQLSLAESEASLgntnipasdhyvgpngfKSLAQEATRLAESHvESASNMEQLTRETEDYsKQALSLVRKALhegvgsGS 868
Cdd:PRK03918 264 LEERIEELKKEI-----------------EELEEKVKELKELK-EKAEEYIKLSEFYEEY-LDELREIEKRL------SR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 869 GSPDGAVVQGLVEKLEKTKSLAQQLTREATQ-----AEIEAD-RSYQHSLRLLDSVSRLQgvsdQSFQVEEAKRIKQKAD 942
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKElekrlEELEERhELYEEAKAKKEELERLK----KRLTGLTPEKLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 943 SLSSLVTRHMDEFKRTQKNLGNWKEEAQQL------LQNGKS-----GREKSDQllSRANL-AKSRAqealsmgnatfyE 1010
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELkkaieeLKKAKGkcpvcGRELTEE--HRKELlEEYTA------------E 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1011 VESILKNLREFDLQVDNRKAEAEEAMKRLSYISQ--KVSDASDKTQQAERALGS-AAADAQRAKNGAGEALEISSEIEQE 1087
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1088 IGSLNLEANVTADgalaMEKGLASLKSEMREVEGEL-----ERKELEFDTnMDAVQMVITEAQKVDTR---AKNAGVTIQ 1159
Cdd:PRK03918 541 IKSLKKELEKLEE----LKKKLAELEKKLDELEEELaellkELEELGFES-VEELEERLKELEPFYNEyleLKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1160 DTLNTLDGLlhlmDQPLSVDEEGLVLLEQKLSRAKTQINS-----------QLRPMMSELEERARQQRGHLHLLETSIDG 1228
Cdd:PRK03918 616 REEKELKKL----EEELDKAFEELAETEKRLEELRKELEElekkyseeeyeELREEYLELSRELAGLRAELEELEKRREE 691
|
570
....*....|....*
gi 2462509082 1229 ILADVKNLENIRDNL 1243
Cdd:PRK03918 692 IKKTLEKLKEELEER 706
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
703-1215 |
1.53e-08 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 58.99 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 703 GDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSR-LDDLKMTVERVRAL-GSQYQNRVR 780
Cdd:pfam07111 16 GHQDVLERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRqLQELRRLEEEVRLLrETSLQQKMR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 781 DTHRLITQMQLSLAESEASLGNTNIPASdhYVGPNGFKSLAQEATRLAESHVESAsNMEQLTRETEDYSKQALSLVRKA- 859
Cdd:pfam07111 96 LEAQAMELDALAVAEKAGQAEAEGLRAA--LAGAEMVRKNLEEGSQRELEEIQRL-HQEQLSSLTQAHEEALSSLTSKAe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 860 -LHEGVGSGSGSPDGAVVQgLVEKLEKTKSLAQQLTReaTQAEIEADRSYQHSLR----------------------LLD 916
Cdd:pfam07111 173 gLEKSLNSLETKRAGEAKQ-LAEAQKEAELLRKQLSK--TQEELEAQVTLVESLRkyvgeqvppevhsqtwelerqeLLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 917 SVSRLQ-------------GVSDQS------FQVEEAKRIKQKADSLSSlvtrhmdEF-KRTQKNLGNWKE--------- 967
Cdd:pfam07111 250 TMQHLQedradlqatvellQVRVQSlthmlaLQEEELTRKIQPSDSLEP-------EFpKKCRSLLNRWREkvfalmvql 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 968 EAQQL---------------LQNGKSGREKSDQLLSRA------------------NLAKSRAQEALSMGNATFYEVESI 1014
Cdd:pfam07111 323 KAQDLehrdsvkqlrgqvaeLQEQVTSQSQEQAILQRAlqdkaaevevermsakglQMELSRAQEARRRQQQQTASAEEQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1015 LK----NLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGA---GEALEISSEIEQE 1087
Cdd:pfam07111 403 LKfvvnAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCpppPPAPPVDADLSLE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1088 IGSLNLEANvTADGALAMEKGLASLKSEMREVEGELERKELefdtnmdavqmvITEAQKVDTRAKNAgvtiQDTLNTLDG 1167
Cdd:pfam07111 483 LEQLREERN-RLDAELQLSAHLIQQEVGRAREQGEAERQQL------------SEVAQQLEQELQRA----QESLASVGQ 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2462509082 1168 LLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQ 1215
Cdd:pfam07111 546 QLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQ 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
711-1199 |
3.87e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLkmtVERVRALGSQYQNRVRDTHRLITQmQ 790
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQ-L 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 791 LSLAESEASLgntnipasdhyvgpngfkslAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEgvgsgsgs 870
Cdd:COG1196 403 EELEEAEEAL--------------------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-------- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 871 pdgavvQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTR 950
Cdd:COG1196 455 ------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 951 HMDEFKRTQKNLGnwkEEAQQLLQNGksGREKSDQLLSRANLAKSRAQealsmGNATFYEVESI------------LKNL 1018
Cdd:COG1196 529 LIGVEAAYEAALE---AALAAALQNI--VVEDDEVAAAAIEYLKAAKA-----GRATFLPLDKIraraalaaalarGAIG 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1019 REFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVT 1098
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1099 ADGALAMEKgLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSV 1178
Cdd:COG1196 679 AELEELAER-LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
490 500
....*....|....*....|.
gi 2462509082 1179 DEEGLVLLEQKLSRAKTQINS 1199
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
580-624 |
5.99e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 5.99e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2462509082 580 CQCNnnVDPSASGNCDRLTGRCLkCIHNTAGIYCDQCKAGYFGDP 624
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
815-1102 |
1.36e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.73 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 815 NGFKSL--AQEATRLAESHVESASNMEQLTRETEDYSKQaLSLVRKALHEGVGSGSGSpdgavVQGLVEKLEKTKSLAQQ 892
Cdd:COG5185 347 QGQESLteNLEAIKEEIENIVGEVELSKSSEELDSFKDT-IESTKESLDEIPQNQRGY-----AQEILATLEDTLKAADR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 893 lTREATQAEIE-ADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSlvtrhmdefkRTQKNLGNWKEEAQQ 971
Cdd:COG5185 421 -QIEELQRQIEqATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR----------SVRSKKEDLNEELTQ 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 972 LLQNGKSGREKSDQLlsRANLAKSraqealsmgnatfyeVESILKNLREFDLQVDNRKAEAEEAMKRLsyISQKVSDASD 1051
Cdd:COG5185 490 IESRVSTLKATLEKL--RAKLERQ---------------LEGVRSKLDQVAESLKDFMRARGYAHILA--LENLIPASEL 550
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462509082 1052 KTQQAERALGSAAADAQRAKNGAGEALEIsseieqeIGSLNLEANVTADGA 1102
Cdd:COG5185 551 IQASNAKTDGQAANLRTAVIDELTQYLST-------IESQQAREDPIPDQA 594
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
711-1162 |
2.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRDAQISEGASRSLGL--QLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDthrlITQ 788
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAE----LAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 789 MQLSLAESEASLGNTNipasdhyvgPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEgvgsgs 868
Cdd:COG4717 175 LQEELEELLEQLSLAT---------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA------ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 869 gspdgavvqglvEKLEKTKSLAQQLTREATQAEIEADrsyqhSLRLLDSVSRLQGVsdqsfqveeakrikqkADSLSSLV 948
Cdd:COG4717 240 ------------ALEERLKEARLLLLIAAALLALLGL-----GGSLLSLILTIAGV----------------LFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 949 TRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSR----ANLAKSRAQEALSMGNATFYEVESILKNLREFDLQ 1024
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglpPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1025 V---------DNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEAleissEIEQEIGSLNLEA 1095
Cdd:COG4717 367 EleqeiaallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEEL 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509082 1096 NVTADGALAMEKGLASLKSEMREVE--GELERKELEFDTnmdaVQMVITEAQKVDTRAKNAGVTIQDTL 1162
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEedGELAELLQELEE----LKAELRELAEEWAALKLALELLEEAR 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
879-1152 |
9.26e-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: 53.52 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 879 LVEKLEKTKSLAQQLTRE---------ATQAEIEADRSYQHSL--RLLDSVSRLQG-VSDQSFQVEEAKRIKQKADSLSs 946
Cdd:TIGR02168 237 LREELEELQEELKEAEEEleeltaelqELEEKLEELRLEVSELeeEIEELQKELYAlANEISRLEQQKQILRERLANLE- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 947 lvtrhmDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEAlsmgNATFYEVESILKNLREFDLQVD 1026
Cdd:TIGR02168 316 ------RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL----EAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1027 NRKAEAEE----AMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAkngagEALEISSEIEQEigslnleanvtadga 1102
Cdd:TIGR02168 386 SKVAQLELqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA-----ELKELQAELEEL--------------- 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1103 lamEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAK 1152
Cdd:TIGR02168 446 ---EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
524-572 |
1.14e-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: 46.58 E-value: 1.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462509082 524 PCPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGYFGDPFGEHG 572
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
953-1255 |
1.18e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 953 DEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEA 1032
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1033 EEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAgEALEIS------SEIEQEIGSLNLEANVTADGALAME 1106
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQElqalseAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1107 KGLaslksEMREVEGELERKELEFDTNMDAVQMVITE-AQKVDTRAKNAGVTI--QDTLNTLDGLLHLMDQPLSVDEEGL 1183
Cdd:COG4372 204 EAE-----KLIESLPRELAEELLEAKDSLEAKLGLALsALLDALELEEDKEELleEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462509082 1184 VLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQ 1255
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
711-1099 |
1.49e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRDAQISEgasRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQ 790
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFEL---DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 791 LSLAESEASLgntnipasdhyvgpngfKSLAQEATRLAEShvesasnMEQLTREtedysKQALSLVRKALHEGVgsgsgs 870
Cdd:COG4372 94 AELAQAQEEL-----------------ESLQEEAEELQEE-------LEELQKE-----RQDLEQQRKQLEAQI------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 871 pdGAVVQGLVEKLEKTKSLAQQLTReaTQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTR 950
Cdd:COG4372 139 --AELQSEIAEREEELKELEEQLES--LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 951 HMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFD----LQVD 1026
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEaleeAALE 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462509082 1027 NRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAAD--AQRAKNGAGEALEISSEIEQEIGSLNLEANVTA 1099
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIllAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
823-1169 |
2.03e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.52 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 823 EATRLAESHV-ESASNMEQLTRETEdysKQALSLVRKALHEGvgsgsgspDGAVVQGLVEKLEKTKSLAQQLTREATQAE 901
Cdd:NF041483 138 ERRQTVESHVnENVAWAEQLRARTE---SQARRLLDESRAEA--------EQALAAARAEAERLAEEARQRLGSEAESAR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 902 IEAD----RSYQHSLRLLDSVS-RLQGVSDQSFQ-----VEEAKRIKQKADSLSSLVTRHMDEFKR--------TQKNLG 963
Cdd:NF041483 207 AEAEailrRARKDAERLLNAAStQAQEATDHAEQlrsstAAESDQARRQAAELSRAAEQRMQEAEEalrearaeAEKVVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 964 NWKEEAQQLLQNGKSGREKsdqllsRANLAKSR----AQEALSMGNATFYEVESILKNLREfdlQVDNRKAEAEEAmKRL 1039
Cdd:NF041483 287 EAKEAAAKQLASAESANEQ------RTRTAKEEiarlVGEATKEAEALKAEAEQALADARA---EAEKLVAEAAEK-ART 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1040 SYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALE-ISSEIEQEIGSLNLEANVTADGAlameKGLA-------- 1110
Cdd:NF041483 357 VAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAErIRREAEAEADRLRGEAADQAEQL----KGAAkddtkeyr 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462509082 1111 ----SLKSEMREVEGELERKELEfdtnmdavqmVITEAQKVDTRAKNAGVT-IQDTLNTLDGLL 1169
Cdd:NF041483 433 aktvELQEEARRLRGEAEQLRAE----------AVAEGERIRGEARREAVQqIEEAARTAEELL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
711-1059 |
4.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDiLRDAQisegasRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQ 790
Cdd:TIGR02168 688 ELEEKIAELEKALAE-LRKEL------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 791 LSLAESEAslgntnipasdhyvgpngfkSLAQEATRLAESHVESASNMEQLTRETEDYS--KQALSLVRKALHEgvgsgs 868
Cdd:TIGR02168 761 AEIEELEE--------------------RLEEAEEELAEAEAEIEELEAQIEQLKEELKalREALDELRAELTL------ 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 869 gspdgavvqgLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGV--------SDQSFQVEEAKRIKQK 940
Cdd:TIGR02168 815 ----------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeleeliEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 941 ADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLRE 1020
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509082 1021 FDLQVDNRK-------------------AEAEEAMKRLSYISQKVSDASDKTQQAERA 1059
Cdd:TIGR02168 965 DDEEEARRRlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
914-1125 |
6.25e-06 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 48.52 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 914 LLDSVSRL--QGVSDQSFQVEEAKRIKQKAdslsslvTRHMdefkrtQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRAN 991
Cdd:pfam04012 1 IFKRLGRLvrANIHEGLDKAEDPEKMLEQA-------IRDM------QSELVKARQALAQTIARQKQLERRLEQQTEQAK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 992 LAKSRAQEALSMGN-----ATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQ----QAERALGS 1062
Cdd:pfam04012 68 KLEEKAQAALTKGNeelarEALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNllkaRLKAAKAQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509082 1063 AAADAQRAKNGAGEALEISSEIEQEIgsLNLEANVTADGALAMEKGL----ASLKSEMREVEGELER 1125
Cdd:pfam04012 148 EAVQTSLGSLSTSSATDSFERIEEKI--EEREARADAAAELASAVDLdaklEQAGIQMEVSEDVLAR 212
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
635-667 |
6.69e-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: 44.27 E-value: 6.69e-06
10 20 30
....*....|....*....|....*....|....
gi 2462509082 635 ACNCNPMGSEPVGC-RSDGTCVCKPGFGGPNCEH 667
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDR 34
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
525-571 |
7.03e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 7.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2462509082 525 CPCHNGFSCSVMPETEEVVCNnCPPGVTGARCELCADGYFGDPFGEH 571
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
500-580 |
7.87e-06 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 47.01 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 500 NPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPE----TEEVVCnNCPPGVT-------GARCELCADGYFGDpf 568
Cdd:cd13406 31 TQDTVCSPCEPGFYNEAVNYEPCKPCTQCNQRSGSEEKQkctkTSDTVC-RCRPGTQpldsykpGVDCVPCPPGHFSR-- 107
|
90
....*....|..
gi 2462509082 569 GEHGPVRPCQPC 580
Cdd:cd13406 108 GDNQACKPWTNC 119
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
732-1210 |
8.79e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 732 ISEGASRSLGLQLAK----VRSQENSYQSRLDDLKMTVERVRALGSQYQnrvrDTHRLITqmqlslaESeaslgnTNIPA 807
Cdd:PRK04863 209 ISSAITRSLRDYLLPensgVRKAFQDMEAALRENRMTLEAIRVTQSDRD----LFKHLIT-------ES------TNYVA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 808 SDHYVGPNGFKSLAQEATRL--------------AESHVESASNMEQLTRE----TEDY--SKQALSLVRKAL--HEGVG 865
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELrrelytsrrqlaaeQYRLVEMARELAELNEAesdlEQDYqaASDHLNLVQTALrqQEKIE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 866 SGSGSpdgavVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLR----LLDSVSRLQGVSDQSFQVEEAKRIKQKA 941
Cdd:PRK04863 352 RYQAD-----LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDElksqLADYQQALDVQQTRAIQYQQAVQALERA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 942 DSLSSLvtrhmDEFkrTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVE-SILKNL-R 1019
Cdd:PRK04863 427 KQLCGL-----PDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrSEAWDVaR 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1020 EFDLQVDNRKAEAEeamkRLSYISQKVSDA---SDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEAN 1096
Cdd:PRK04863 500 ELLRRLREQRHLAE----QLQQLRMRLSELeqrLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1097 VTADGALAMEKGLASLKSEMRevegELERKELEFDTNMDAVQMVitEAQKVDTRAKNAGVT--IQDTlntldgLLHLMDQ 1174
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARL--REQSGEEFEDSQDVTeyMQQL------LEREREL 643
|
490 500 510
....*....|....*....|....*....|....*.
gi 2462509082 1175 PLSVDEeglvlLEQKLSRAKTQINSQLRPMMSELEE 1210
Cdd:PRK04863 644 TVERDE-----LAARKQALDEEIERLSQPGGSEDPR 674
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
636-667 |
2.12e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.11 E-value: 2.12e-05
10 20 30
....*....|....*....|....*....|...
gi 2462509082 636 CNCNPMGSEPVGC-RSDGTCVCKPGFGGPNCEH 667
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDR 33
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
818-1128 |
2.72e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 48.45 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 818 KSLAQEATRLA---ESHVESASNMEQLTRETEDYSKQA---LSLvRKALHEGVGSGSGSPDGAVVQGLVEklektksLAQ 891
Cdd:pfam13779 406 RALIEQRRRLAldrENRPRVARALDALTLAPEEFGPDAgvyLGL-RSALARLELARSDEALDEVADLLWE-------LAL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 892 QLT-REATQAEIEADRSYQhslRLLDSVSRlqGVSDqsfqvEEakrIKQKADSLSSLVTRHMDEFKRTQKNLGNwkEEAQ 970
Cdd:pfam13779 478 RIEdGDLSDAERRLRAAQE---RLSEALER--GASD-----EE---IAKLMQELREALDDYMQALAEQAQQNPQ--DLQQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 971 QLLQNGKSGREKS-DQLLSR-ANLAKS----RAQEALSmgnatfyEVESILKNLR--EFDLQVDNRKAEAEEAMKRLSYI 1042
Cdd:pfam13779 543 PDDPNAQEMTQQDlQRMLDRiEELARSgrraEAQQMLS-------QLQQMLENLQagQPQQQQQQGQSEMQQAMDELGDL 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1043 SQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGAL-----AMEKGLASLKSEMR 1117
Cdd:pfam13779 616 LREQQQLLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLaerqqALRRRLEELQDELK 695
|
330
....*....|.
gi 2462509082 1118 EVEGELERKEL 1128
Cdd:pfam13779 696 ELGGKEPGQAL 706
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1062-1243 |
2.84e-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: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1062 SAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVI 1141
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1142 TEAQKVDTRAKNAGV-----TIQDTLNTLDGLLHLMDQPLSVDEEgLVLLEQKLSRAKTQINSQLRpmmsELEERARQQR 1216
Cdd:COG3883 93 RALYRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLA----ELEALKAELE 167
|
170 180
....*....|....*....|....*..
gi 2462509082 1217 GHLHLLETSIDGILADVKNLENIRDNL 1243
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAA 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
677-1229 |
3.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMDQFMQQLQRMEALISkAQGGDGVvpdTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQS 756
Cdd:COG4913 312 ERLEARLDALREELDELEAQIR-GNGGDRL---EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 757 RLDDLKMTVERVRAlgsQYQNRVRDTHRLITQMQLSLAESE---ASL--GNTNIPASDHYVgpngfKSLAQEATRLAESH 831
Cdd:COG4913 388 EAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEaeiASLerRKSNIPARLLAL-----RDALAEALGLDEAE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 832 V----------------ESAsnMEQLTR--------ETEDYsKQALSLVRkALH-------EGVGSGSGSPDGAVV--QG 878
Cdd:COG4913 460 LpfvgelievrpeeerwRGA--IERVLGgfaltllvPPEHY-AAALRWVN-RLHlrgrlvyERVRTGLPDPERPRLdpDS 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 879 LVEKLEKTKSLAqqltREATQAEIEADRSYqhslRLLDSVSRLQGVS-------------------DQSFQVEE------ 933
Cdd:COG4913 536 LAGKLDFKPHPF----RAWLEAELGRRFDY----VCVDSPEELRRHPraitragqvkgngtrhekdDRRRIRSRyvlgfd 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 934 -AKRIKQKADSLSSLvTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQ-----EALSMGNAT 1007
Cdd:COG4913 608 nRAKLAALEAELAEL-EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEleaelERLDASSDD 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1008 fyevesiLKNLREfdlQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAknGAGEALEISSEIEQE 1087
Cdd:COG4913 687 -------LAALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1088 IGSLNLEAnVTADGALAMEKGLASLKSEMREVEGELERKELEFdtnmdavqmviteaqkvDTRAKNAGVTIQDTLNTLDG 1167
Cdd:COG4913 755 FAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRAF-----------------NREWPAETADLDADLESLPE 816
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509082 1168 LLHLMDQplsVDEEGLVLLEQKLSRAktqinsqlrpmmseLEERARQQRGHL-HLLETSIDGI 1229
Cdd:COG4913 817 YLALLDR---LEEDGLPEYEERFKEL--------------LNENSIEFVADLlSKLRRAIREI 862
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1026-1236 |
4.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1026 DNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALgsaaadAQ-RAKNGAGEALEISSEIEQEIGSLNLEanvtadgala 1104
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAAL------EEfRQKNGLVDLSEEAKLLLQQLSELESQ---------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1105 mekgLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKnagvtIQDTLNTLDGLLhlmdQPLSVDEEGLV 1184
Cdd:COG3206 228 ----LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQ-----LAELEAELAELS----ARYTPNHPDVI 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462509082 1185 LLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNL 1236
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
636-667 |
4.97e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 4.97e-05
10 20 30
....*....|....*....|....*....|...
gi 2462509082 636 CNCNPMGSEPVGCRSD-GTCVCKPGFGGPNCEH 667
Cdd:smart00180 1 CDCDPGGSASGTCDPDtGQCECKPNVTGRRCDR 33
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
872-1163 |
5.49e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.30 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 872 DGAVVQGLVEKLEKTKSLAQQLTreaTQAEIEADrsyqhslrllDSVSRLQGVSDQSFQ-VEEAKRIKQKADslsslvtr 950
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMT---DLKERESQ----------EDAKRAQQLKEELDKkQIDADKAQQKAD-------- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 951 hmdefkRTQKNLGNWKEEAQQLLQNGKSGREKSDqllsranlaKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKA 1030
Cdd:pfam05262 238 ------FAQDNADKQRDEVRQKQQEAKNLPKPAD---------TSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1031 EAEEAMKRLSYISQKvsDASDKTQQAERALGSAAADAQRAKNgAGEAlEISSEIEQEIGSLN--LEANVTADGALAMEKG 1108
Cdd:pfam05262 303 HKAFDLKQESKASEK--EAEDKELEAQKKREPVAEDLQKTKP-QVEA-QPTSLNEDAIDSSNpvYGLKVVDPITNLSELV 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462509082 1109 LASLKSEMREVEGELE--RKELEFDTNMDAVQMVITEA----QKVDTRAKNAGVTIQDTLN 1163
Cdd:pfam05262 379 LIDLKTEVRLRESAQQtiRRRGLYEREKDLVAIAITSGnaklQLVDIDLKNLEVIKESNFE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1009-1243 |
1.39e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1009 YEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVS-----------------DASDKTQQAERALGSAAADAQRAK 1071
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAeleaeleelrleleeleLELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1072 NGAGEALEissEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRA 1151
Cdd:COG1196 305 ARLEERRR---ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1152 KNAGVTIQDTLNTLDGLLHLMDQpLSVDEEGLVLLEQKLSRAKTQINSQLRpmmsELEERARQQRGHLHLLETSIDGILA 1231
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEE 456
|
250
....*....|..
gi 2462509082 1232 DVKNLENIRDNL 1243
Cdd:COG1196 457 EEEALLELLAEL 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1043-1216 |
1.78e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1043 SQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGE 1122
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1123 LERKElefdtnmDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDE---EGLVLLEQKLSRAKTQINS 1199
Cdd:COG4942 99 LEAQK-------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEA 171
|
170
....*....|....*..
gi 2462509082 1200 QLRPMMSELEERARQQR 1216
Cdd:COG4942 172 ERAELEALLAELEEERA 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
876-1102 |
2.32e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 876 VQGLVEKLEKTKSLAQQLTRE--ATQAEIEAD--------RSYQHSLRLLDSVSRLqgVSDQSFQ--VEEAKRIKQKADS 943
Cdd:COG3883 53 YNELQAELEALQAEIDKLQAEiaEAEAEIEERreelgeraRALYRSGGSVSYLDVL--LGSESFSdfLDRLSALSKIADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 944 LSSLvtrhMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSmgnatfyEVESILKNLREFDL 1023
Cdd:COG3883 131 DADL----LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA-------QLSAEEAAAEAQLA 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509082 1024 QVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGA 1102
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
711-922 |
2.82e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 711 ELEGRMQQAEQALQDILRDAQISEGASRSLGL--QLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRD--THRLI 786
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 787 TQMQLSLAESEAslgntnipasdhyvgpngfkSLAQEATRLAESHVEsasnMEQLTRETEDYSKQALSLVRKALHEGVGS 866
Cdd:COG3206 266 QQLRAQLAELEA--------------------ELAELSARYTPNHPD----VIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509082 867 GSGSpdGAVVQGLVEKLEKTKSLAQQLTR-EATQAEIEadRSYQHSLRLLDS-VSRLQ 922
Cdd:COG3206 322 LEAL--QAREASLQAQLAQLEARLAELPElEAELRRLE--REVEVARELYESlLQRLE 375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
717-1214 |
3.31e-04 |
|
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: 44.96 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 717 QQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERV-------------RALGSQYQNRVRDTH 783
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInrarkaaplaahiKAVTQIEQQAQRIHT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 784 RLITQMQlSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDysKQALslvrKALHEg 863
Cdd:TIGR00618 315 ELQSKMR-SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL--TQHI----HTLQQ- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 864 vgsgsgspdgaVVQGLVEKLEKTKSLAQQLTREatQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADS 943
Cdd:TIGR00618 387 -----------QKTTLTQKLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 944 LsSLVTRHMDEFKRTQKNLgnwKEEAQQLLQNGKSGREKSDQLLSRANLAKSraQEALSMGNATFYEVESILKNLREFD- 1022
Cdd:TIGR00618 454 E-KLEKIHLQESAQSLKER---EQQLQTKEQIHLQETRKKAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1023 ---LQVDNRKAEAEEAMKRLSYISQKVSD--ASDKtQQAERALGSAAADAQRaKNGAGEALEISSEIEQEI---GSLNLE 1094
Cdd:TIGR00618 528 rrmQRGEQTYAQLETSEEDVYHQLTSERKqrASLK-EQMQEIQQSFSILTQC-DNRSKEDIPNLQNITVRLqdlTEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1095 ANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQD------TLNTLDGL 1168
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPkellasRQLALQKM 685
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2462509082 1169 LHLMDQpLSVDEEGLvlleqklsrakTQINSQLRPMMSELEERARQ 1214
Cdd:TIGR00618 686 QSEKEQ-LTYWKEML-----------AQCQTLLRELETHIEEYDRE 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
888-1120 |
3.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 888 SLAQQLTREATQAEIEADRsyQHSLRLLDSVSRLQgvSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKE 967
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQ--QEIAELEKELAALK--KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 968 EAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFdlqVDNRKAEAEEAMKRLSYISQKVS 1047
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL---APARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509082 1048 DASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVE 1120
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
715-1216 |
5.79e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 715 RMQQAEQALQDILRDAQISEGASRSLGL---------QLAKVRSQENSyqsRLDDLKmtveRVRALGSQYQNRVRDTHRL 785
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELSKaeknsltetLKKEVKSLQNE---KADLDR----KLRKLDQEMEQLNHHTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 786 iTQMqLSLAESEAS----LGNTNIPASDHYVGPNGF---------------KSLAQEATRLAESHVESAS---NMEQLTR 843
Cdd:TIGR00606 535 -TQM-EMLTKDKMDkdeqIRKIKSRHSDELTSLLGYfpnkkqledwlhsksKEINQTRDRLAKLNKELASleqNKNHINN 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 844 ETEDYSKQALSLVRKaLHEGVGSGSGSPDgavVQGLVEKLEKT-KSLA-------------QQLTREATQAEIEADRSYQ 909
Cdd:TIGR00606 613 ELESKEEQLSSYEDK-LFDVCGSQDEESD---LERLKEEIEKSsKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQ 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 910 HSLRLLDSVSRLQGV-----SDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQL---LQNGKSGRE 981
Cdd:TIGR00606 689 TEAELQEFISDLQSKlrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVnrdIQRLKNDIE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 982 KSDQLLSRAN----LAK---------SRAQEALSMGNATFYEVESILKNLrEFDLQVDNRKAEAEEAMKRLSYISQKVSD 1048
Cdd:TIGR00606 769 EQETLLGTIMpeeeSAKvcltdvtimERFQMELKDVERKIAQQAAKLQGS-DLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1049 ---ASDKTQQAERALGSA-----------AADAQRAKNGAGEALEISSEIEqeigSLNLEANVTADGALAMEKglaSLKS 1114
Cdd:TIGR00606 848 nrkLIQDQQEQIQHLKSKtnelkseklqiGTNLQRRQQFEEQLVELSTEVQ----SLIREIKDAKEQDSPLET---FLEK 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1115 EMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTldgllHLMDQPLSVDEEGLVLLEQKLSRAK 1194
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD-----YLKQKETELNTVNAQLEECEKHQEK 995
|
570 580
....*....|....*....|..
gi 2462509082 1195 tqINSQLRPMMSELEERARQQR 1216
Cdd:TIGR00606 996 --INEDMRLMRQDIDTQKIQER 1015
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
677-1156 |
6.40e-04 |
|
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: 44.19 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 677 NQVKIQMDQFMQQLQRMEALISKAQggdgvvpDTELEGRMQQAEQALQDILRDAQIS----EGASRSLGLQLAKVRSQEN 752
Cdd:TIGR00618 362 EVATSIREISCQQHTLTQHIHTLQQ-------QKTTLTQKLQSLCKELDILQREQATidtrTSAFRDLQGQLAHAKKQQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 753 SYQSRLDDLKMTVE------------------RVRALGSQYQN------RVRDTHRLITQMQLSLAESEASL-GNTNIPA 807
Cdd:TIGR00618 435 LQQRYAELCAAAITctaqceklekihlqesaqSLKEREQQLQTkeqihlQETRKKAVVLARLLELQEEPCPLcGSCIHPN 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 808 SDHYV----GPN------GFKSLAQEATRLAESHVESASNMEQLTR-----ETEDYSKQALSLVRKALHEGVgSGSGSPD 872
Cdd:TIGR00618 515 PARQDidnpGPLtrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASlkeqmQEIQQSFSILTQCDNRSKEDI-PNLQNIT 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 873 GAVVQGLVEKLEKTKSLAQQLTREATQAEIEAD--------RSYQHSLRL-LDSVSRLQGVSDQSFQVEEAKRIKQKADS 943
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdvrlhlQQCSQELALkLTALHALQLTLTQERVREHALSIRVLPKE 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 944 LSSLVTRHMDEFKRTQKNLGNWKEEAQQ---LLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFyeVESILKNLRE 1020
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQcqtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL--NQSLKELMHQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1021 FDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKngagealEISSEIEQEIGSLNLEANVTAD 1100
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK-------TLEAEIGQEIPSDEDILNLQCE 824
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509082 1101 galAMEKGLASLKSEMRE---VEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGV 1156
Cdd:TIGR00618 825 ---TLVQEEEQFLSRLEEksaTLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
818-1202 |
6.48e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 818 KSLAQEATRlaesHVESASNMEQLT-RE---TEDYskQA----LSLVRKAL--HEGVGSGSgspdgAVVQGLVEKLEK-- 885
Cdd:COG3096 299 RQLAEEQYR----LVEMARELEELSaREsdlEQDY--QAasdhLNLVQTALrqQEKIERYQ-----EDLEELTERLEEqe 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 886 --TKSLAQQLTR---EATQAEIEADR------SYQhslRLLDSVSRLQGVSDQSFQ-VEEAKRIKQKADslsslvtrhmd 953
Cdd:COG3096 368 evVEEAAEQLAEaeaRLEAAEEEVDSlksqlaDYQ---QALDVQQTRAIQYQQAVQaLEKARALCGLPD----------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 954 efkRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVE---------SILKNLREFDLQ 1024
Cdd:COG3096 434 ---LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVErsqawqtarELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1025 VDnrkaeaeeamkRLSYISQKVSDASDKTQQAERALGSAAADAQRAK---NGAGEALEISSEIEQEIGSLNLEANVTADG 1101
Cdd:COG3096 511 AQ-----------RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGqqlDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1102 ALAMEKGLASLKSEMRevegELERKELEFDTNMDAVQMVITEaqkvdtraknagvtIQDTLNTLDGLLHLMDQPLSvDEE 1181
Cdd:COG3096 580 RSELRQQLEQLRARIK----ELAARAPAWLAAQDALERLREQ--------------SGEALADSQEVTAAMQQLLE-RER 640
|
410 420
....*....|....*....|.
gi 2462509082 1182 GLVLLEQKLSRAKTQINSQLR 1202
Cdd:COG3096 641 EATVERDELAARKQALESQIE 661
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
884-1154 |
1.28e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 884 EKTKSLAQQLTREATQAEIEADR---------------------SYQ-HSLRLLDSVSRLQGVSDQ--SFQVEEAKRIKQ 939
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADRlrgeaadqaeqlkgaakddtkEYRaKTVELQEEARRLRGEAEQlrAEAVAEGERIRG 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 940 KAdslSSLVTRHMDEFKRTQKN-LGNWKEEAQQLLQNGKSGREK-SDQLLSRAN---------LAKSRAQ------EALS 1002
Cdd:NF041483 466 EA---RREAVQQIEEAARTAEElLTKAKADADELRSTATAESERvRTEAIERATtlrrqaeetLERTRAEaerlraEAEE 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1003 MGNATFYEVESILKNLR-EFDLQVDNRKAEAEEAMKRLSyisqkvSDASDKTQQAERALGSAAADAQRAKNGAGEALE-- 1079
Cdd:NF041483 543 QAEEVRAAAERAARELReETERAIAARQAEAAEELTRLH------TEAEERLTAAEEALADARAEAERIRREAAEETErl 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1080 ----------ISSEIEQEIGSLNLEANVTADGALAMEKGLA-SLKSemrEVEGELERKELEFDTNMDAVQM-VITEAQKV 1147
Cdd:NF041483 617 rteaaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAvRLRS---EAAAEAERLKSEAQESADRVRAeAAAAAERV 693
|
....*..
gi 2462509082 1148 DTRAKNA 1154
Cdd:NF041483 694 GTEAAEA 700
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
967-1125 |
1.41e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 967 EEAQQLLQNGKSG------REKS-----DQLLSRANLAKSRAQEALSMGNatfyevESI----LKNLREFDLQVDNRKAE 1031
Cdd:COG1842 33 RDMEEDLVEARQAlaqviaNQKRlerqlEELEAEAEKWEEKARLALEKGR------EDLareaLERKAELEAQAEALEAQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1032 AEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAK--------------NGAGEALEissEIEQEIgsLNLEANV 1097
Cdd:COG1842 107 LAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKaqekvnealsgidsDDATSALE---RMEEKI--EEMEARA 181
|
170 180 190
....*....|....*....|....*....|..
gi 2462509082 1098 TADGALAMEKGL----ASLKSEMrEVEGELER 1125
Cdd:COG1842 182 EAAAELAAGDSLddelAELEADS-EVEDELAA 212
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
783-1063 |
1.49e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 783 HRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALhe 862
Cdd:pfam06008 15 YKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIK-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 863 gvgsgsgspdgAVVQGLVEKLEKTKSLAQQL------TREATQAEIeadrsyQHSLRLLDSvsrlqgvSDQSFQVEEAKR 936
Cdd:pfam06008 93 -----------NLIDNIKEINEKVATLGENDfalpssDLSRMLAEA------QRMLGEIRS-------RDFGTQLQNAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 937 IKQKADSLsslvtrhmdeFKRTQKNLGNWKEEAQQLLQNGKSG-REKSDQL-----LSRANLAKSRAQEALSMGNAtfye 1010
Cdd:pfam06008 149 ELKAAQDL----------LSRIQTWFQSPQEENKALANALRDSlAEYEAKLsdlreLLREAAAKTRDANRLNLANQ---- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462509082 1011 vesilKNLREFdlqvdNRKAEAEEAMKRLsyISQKVSDASDKTQQAERALGSA 1063
Cdd:pfam06008 215 -----ANLREF-----QRKKEEVSEQKNQ--LEETLKTARDSLDAANLLLQEI 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
879-1091 |
1.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 879 LVEKLEKTKSLAQ--QLTREATQAEIEADRsyqhsLRLLDSVSRLQgvsdqsFQVEEAKRIKQKADSLSSLVTRHMDEFK 956
Cdd:COG4913 244 LEDAREQIELLEPirELAERYAAARERLAE-----LEYLRAALRLW------FAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 957 RTQKNLGNWKEEA----QQLLQNGksGREKSD--QLLSRANLAKSRAQEALsmgnatfyevESILKNLREFDLQVDNRKA 1030
Cdd:COG4913 313 RLEARLDALREELdeleAQIRGNG--GDRLEQleREIERLERELEERERRR----------ARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462509082 1031 EAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNgagealeissEIEQEIGSL 1091
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------ELEAEIASL 431
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
881-1129 |
1.92e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 881 EKLEKTKSLAQQLtreatqAEIEADRSyqhslRLLDSVSRLQGVSDQSFqvEEAKRIKQKADSLSSLvtrhMDEFKRTQK 960
Cdd:COG1340 47 ELNAQVKELREEA------QELREKRD-----ELNEKVKELKEERDELN--EKLNELREELDELRKE----LAELNKAGG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 961 NLGNWKEEAQQL---LQNGKSGREKSDQLLSRANLAKSRAQEAlsmgnatfyevesilKNLREFDLQVDNRKAEAEEAMK 1037
Cdd:COG1340 110 SIDKLRKEIERLewrQQTEVLSPEEEKELVEKIKELEKELEKA---------------KKALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1038 RLSYISQKVSDASDKTQQAERALGSA--AADAQRAkngagEALEISSEIE---QEIGSLNLEANVTADGALAMEKGLASL 1112
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELykEADELRK-----EADELHKEIVeaqEKADELHEEIIELQKELRELRKELKKL 249
|
250
....*....|....*..
gi 2462509082 1113 KSEMREVEGELERKELE 1129
Cdd:COG1340 250 RKKQRALKREKEKEELE 266
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
547-572 |
2.30e-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: 2.30e-03
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
879-1116 |
3.26e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 879 LVEKLEKTKSLAQQLTREATQAEIEADRsyqhslrlldSVSRLQGvsdqsfqveEAKRIKQKADSLsslvtrhmdefkrt 958
Cdd:COG1842 17 LLDKAEDPEKMLDQAIRDMEEDLVEARQ----------ALAQVIA---------NQKRLERQLEEL-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 959 QKNLGNWKEEAQQLLQngkSGREKsdqlLSRANLAKSRAQEALSMGNATFYE-----VESILKNLREFDLQVDNRKAEAE 1033
Cdd:COG1842 64 EAEAEKWEEKARLALE---KGRED----LAREALERKAELEAQAEALEAQLAqleeqVEKLKEALRQLESKLEELKAKKD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1034 EAMKRlsyisQKVSDASDKTQQAERALGSAAA-----------DAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADga 1102
Cdd:COG1842 137 TLKAR-----AKAAKAQEKVNEALSGIDSDDAtsalermeekiEEMEARAEAAAELAAGDSLDDELAELEADSEVEDE-- 209
|
250
....*....|....
gi 2462509082 1103 lamekgLASLKSEM 1116
Cdd:COG1842 210 ------LAALKAKM 217
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
91-149 |
3.47e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 36.56 E-value: 3.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462509082 91 CDCNG---KSRQCifdrelHRQTGngfRCLnCNDNTDGIHCEKCKNGFYRHRerdRCLPCNC 149
Cdd:pfam00053 1 CDCNPhgsLSDTC------DPETG---QCL-CKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
709-1166 |
3.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 709 DTELEGRMQQAEQALQDIlrDAQIS------EGASRSLGlQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQnRVRDT 782
Cdd:PRK02224 201 EKDLHERLNGLESELAEL--DEEIEryeeqrEQARETRD-EADEVLEEHEERREELETLEAEIEDLRETIAETE-REREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 783 HRLITQMQLSLAESEASlgntnipASDHYVGPNGFKSLAQEA------------TRLAESHVESASNMEQLTRETEDYSK 850
Cdd:PRK02224 277 LAEEVRDLRERLEELEE-------ERDDLLAEAGLDDADAEAvearreeledrdEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 851 QALSLVRKA--LHEGVGSgsgspDGAVVQGLVEKLEKTKSlaqqlTREATQAEIEADRSyqhslRLLDSVSRLQGVSDQS 928
Cdd:PRK02224 350 DADDLEERAeeLREEAAE-----LESELEEAREAVEDRRE-----EIEELEEEIEELRE-----RFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 929 FQVEEAK-RIKQKADSLSSlvtrhmdefkrTQKNLGNWKEEAQQLLQNGK------------------SGREKSDQLlsR 989
Cdd:PRK02224 415 EELREERdELREREAELEA-----------TLRTARERVEEAEALLEAGKcpecgqpvegsphvetieEDRERVEEL--E 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 990 ANLAKSRAQ--------EALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALG 1061
Cdd:PRK02224 482 AELEDLEEEveeveerlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1062 SAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAME---------KGLASLKSEMREVEGEL-ERK-ELEF 1130
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDeierlrekrEALAELNDERRERLAEKrERKrELEA 641
|
490 500 510
....*....|....*....|....*....|....*.
gi 2462509082 1131 DTNMDAVQmvitEAQKVDTRAKNAGVTIQDTLNTLD 1166
Cdd:PRK02224 642 EFDEARIE----EAREDKERAEEYLEQVEEKLDELR 673
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
91-141 |
3.89e-03 |
|
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: 36.56 E-value: 3.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462509082 91 CDCNG---KSRQCifdrelHRQTGngfRCLnCNDNTDGIHCEKCKNGFYRHRER 141
Cdd:cd00055 2 CDCNGhgsLSGQC------DPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
682-1127 |
4.04e-03 |
|
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: 41.57 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 682 QMDQFMQQLQRMEAlISKAQGGDGVVPDTELEGRMQQAEQALQdiLRDAQISEGAsrslglQLAKVRSQENSYQSRLDDL 761
Cdd:TIGR00606 180 SATRYIKALETLRQ-VRQTQGQKVQEHQMELKYLKQYKEKACE--IRDQITSKEA------QLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 762 KmtvERVRALgsqyQNRVRDTHRLITQMQlSLAESEASLGNTNIPASDHYVGPngFKSLAQEATRLAESHVESASNMEQ- 840
Cdd:TIGR00606 251 K---NRLKEI----EHNLSKIMKLDNEIK-ALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNDLYHNHQRTVREKERe 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 841 ---LTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQglvEKLEKTKSLAQQLtreATQAEIEADRSYQHSLRLLDS 917
Cdd:TIGR00606 321 lvdCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQ---EHIRARDSLIQSL---ATRLELDGFERGPFSERQIKN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 918 VSRLQgvsdQSFQVEEAKRIKQKADSLSS---LVTRHMDEFKRTQKNLGNW-----------KEEAQQLLQNGKSGREKS 983
Cdd:TIGR00606 395 FHTLV----IERQEDEAKTAAQLCADLQSkerLKQEQADEIRDEKKGLGRTielkkeilekkQEELKFVIKELQQLEGSS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 984 DQLLSRAN-LAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMkrlsyiSQKVSDASDKTQQAERALGS 1062
Cdd:TIGR00606 471 DRILELDQeLRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEM------EQLNHHTTTRTQMEMLTKDK 544
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462509082 1063 AAADAQRAKNGAGEALEISS---------EIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKE 1127
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKE 618
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
726-1096 |
4.21e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 41.16 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 726 ILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNI 805
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 806 PASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEK 885
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 886 TKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSS------LVTRHMDEFKRTQ 959
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgdltvrIDVDSKDEIGQLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 960 KNLGNWKEEAQQLLQNGKSG----REKSDQLLSRANLAKSRAQEALSmgnatfyEVESILknlrefdlqvdnrkAEAEEA 1035
Cdd:COG0840 242 DAFNRMIENLRELVGQVRESaeqvASASEELAASAEELAAGAEEQAA-------SLEETA--------------AAMEEL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462509082 1036 MKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEAN 1096
Cdd:COG0840 301 SATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQ 361
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
820-1131 |
4.87e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 820 LAQEATRL--AESHVESASNMEQLTRETEDYSKQALSLVRKALHEgvgsgsgspdgAVV---QGLVEKLEktkSLAQQLT 894
Cdd:COG3096 838 LAALRQRRseLERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQ-----------ANLladETLADRLE---ELREELD 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 895 rEATQAEIEADRSYQHSLRLLDSVSRLQgvSD-QSF-----QVEEAK----RIKQKADSLSSLVTR--HMdefkrtqknl 962
Cdd:COG3096 904 -AAQEAQAFIQQHGKALAQLEPLVAVLQ--SDpEQFeqlqaDYLQAKeqqrRLKQQIFALSEVVQRrpHF---------- 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 963 gNWKEEAQQLLQNgksgREKSDQL---LSRANLAKSRAQEALSMGNATFYEVESILKNLREfdlQVDNRKAEAEEAMKRL 1039
Cdd:COG3096 971 -SYEDAVGLLGEN----SDLNEKLrarLEQAEEARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTLQELEQEL 1042
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1040 SYISQKVSDASDKTQQAERalgsaaadaqrakngagealeisSEIEQEIGSLNLEANvtadgalAMEKGLASLKSEMREV 1119
Cdd:COG3096 1043 EELGVQADAEAEERARIRR-----------------------DELHEELSQNRSRRS-------QLEKQLTRCEAEMDSL 1092
|
330
....*....|..
gi 2462509082 1120 EGELerKELEFD 1131
Cdd:COG3096 1093 QKRL--RKAERD 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1024-1245 |
4.91e-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: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1024 QVDNRKAEAEEAMKRLSY--ISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEAnvtadg 1101
Cdd:COG4913 266 AARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1102 alamekgLASLKSEMREVEGELERKElefdtnmdavqmviTEAQKVDTRAKNAGVTIQDtlntldgllhlmdqplsvDEE 1181
Cdd:COG4913 340 -------LEQLEREIERLERELEERE--------------RRRARLEALLAALGLPLPA------------------SAE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462509082 1182 GLVLLEQKLSRAKTQINSQLRpmmsELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPP 1245
Cdd:COG4913 381 EFAALRAEAAALLEALEEELE----ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
880-1243 |
7.02e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 880 VEKLEKTKSLAQQlTREATQAEIEADRsyQHSLRLLDSVSRLqgVSDQSFQVEEAKRIKQKADSLSslvtrhmDEFKRTQ 959
Cdd:PRK02224 260 IEDLRETIAETER-EREELAEEVRDLR--ERLEELEEERDDL--LAEAGLDDADAEAVEARREELE-------DRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 960 KNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSmgnatfyEVESILKNLREFDLQVDNRKAEAEEAMKRL 1039
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES-------ELEEAREAVEDRREEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1040 SYISQKVSDASDKTQ--QAERA-----LGSAAADAQRAKNGAGEALEISS-----EIEQEI-GSLNLEANVTADGALA-M 1105
Cdd:PRK02224 401 GDAPVDLGNAEDFLEelREERDelrerEAELEATLRTARERVEEAEALLEagkcpECGQPVeGSPHVETIEEDRERVEeL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1106 EKGLASLKSEMREVEGELERKElefdtnmDAVQmVITEAQKVDTRAKNAGVTIQDTLNTLDG----LLHLMDQPLSVDEE 1181
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAE-------DLVE-AEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAE 552
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462509082 1182 GlvllEQKLSRAktqinsqlrpmmSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNL 1243
Cdd:PRK02224 553 A----EEKREAA------------AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLL 598
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
954-1174 |
7.30e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.35 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 954 EFKRTQKNLGNWKEEAQQLLQNGKSGREKSdqllsranlaksraqealsmgnatfyEVESILKNLREFDLQVDNRK---- 1029
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLE--------------------------SVEALLKKHEALEAELAAHEerve 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509082 1030 ---AEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLN-LEANVTADGALAM 1105
Cdd:cd00176 58 alnELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEeKEAALASEDLGKD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509082 1106 EKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAgvTIQDTLNTLDGLLHLMDQ 1174
Cdd:cd00176 138 LESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEE--KLEELNERWEELLELAEE 204
|
|
| |
