|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
42-276 |
1.01e-108 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 345.72 E-value: 1.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 42 CYPATGNLLIGRAVnlSATSTCGLNGPQPYCIVSHLQESDKCFECNSQHrfdpyrHRNSHRIENVIYLMDGNgDNTWWQS 121
Cdd:pfam00055 1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRD------PHNSHPPSNLTDSNNGT-NETWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 122 VNGE---ESVSIRLNLEAEFHFTHLIIKFKTFRPAAMFIERSADFGRTWRPYRYFASNCTKTFpGIPANGLHHIND--II 196
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIKDdeVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 197 CEERYSDIEPSTNGEVIYKVL--DPAIHVKDpYSLDIQELLRITNLRINFTKLNTLGDDLLDRRfDVLQKYYYAIYELVV 274
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDP-SVLRKYYYAISDISV 228
|
..
gi 1848696099 275 RG 276
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
36-276 |
3.49e-83 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 273.08 E-value: 3.49e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 36 GCTDGSCYPATGNLLIGRAVnlSATSTCGLNGPQPYCI-VSHLQESDKCFECNSQHrfdpyrHRNSHRIENVIylmDGNG 114
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREV--TATSTCGEPGPERYCKlVGHTEQGKKCDYCDARN------PRRSHPAENLT---DGNN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 115 DN--TWWQS---VNGEESVSIRLNLEAEFHFTHLIIKFKTFRPAAMFIERSaDFGRTWRPYRYFASNCTKTFPGIP--AN 187
Cdd:smart00136 70 PNnpTWWQSeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPrgPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 188 GLHHINDIICEERYSDIEPSTNGEVIYKVLDPAIHVKD-PYSLDIQELLRITNLRINFTKLNTLGDDLLDRRFDVLQKYY 266
Cdd:smart00136 149 TKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYY 228
|
250
....*....|
gi 1848696099 267 YAIYELVVRG 276
Cdd:smart00136 229 YAISDIAVGG 238
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1780-1849 |
1.14e-24 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 98.89 E-value: 1.14e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1780 NQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1510-1846 |
1.30e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 95.86 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1510 TDSLNAAKEELQSVAKKLQDIASLTQDVKNQamntLKKAQKKkdhFENNNKKLKDFIKKIRDFLTEegadPESIEKVAQQ 1589
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQ----LSEKQKE---LEQNNKKIKELEKQLNQLKSE----ISDLNNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1590 VLSITLpvnKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHIS-IAKELLDKAKDAKSRAEGVKDSANNTKQaldmsekaI 1668
Cdd:TIGR04523 307 DWNKEL---KSELKNQEKKLEEIQNQISQNNKIISQLNEQISqLKKELTNSESENSEKQRELEEKQNEIEK--------L 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1669 EKARAALKEANNNLNSTRNA---TVEVDERLTQLEDKQMDVM-MRLNNLSREVEALRNKTEQNRQMAKDAIAQ------- 1737
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDlesKIQNQEKLNQQKDEQIKKLqQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeli 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1738 ANNATQVASSLEQSLNDTENRY----QELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKS 1813
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350
....*....|....*....|....*....|...
gi 1848696099 1814 NEQRMQKQRMELDELKENatLVRDVIREQVQKY 1846
Cdd:TIGR04523 536 KESKISDLEDELNKDDFE--LKKENLEKEIDEK 566
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
876-924 |
9.11e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 9.11e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 876 CDCHSEGSLSHQCDPVTGQCQCRHGATGRQCSDCQPGQWGFPSCSPCQC 924
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
828-873 |
2.16e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.88 E-value: 2.16e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 828 CQCDPQGSLSGECHKVGGDCHCKPNVMGRRCDQCTPGTYGYGANGC 873
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1273-1845 |
3.09e-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: 78.62 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1273 DTRIKELERKLKGVQD---LISMEDSNRIHQLIGQSIDDLRAEIALTDGRLMGVTRELNTTADEEEALRHILSVLEKELT 1349
Cdd:pfam15921 230 DTEISYLKGRIFPVEDqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1350 HINATVAHKQRLLDNYLtSGFADQFEKVKKFYQESAKAEEKCNASVSGPLSPVEQSKETRAVTEDLLDASKVKFLRALAA 1429
Cdd:pfam15921 310 NQNSMYMRQLSDLESTV-SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1430 QNKSLS-ELQQKAHDLDK------KVHHLSHKVcgGHSNASVNG-----SCPDSQCGGAgcHDDQGNHVCGGHGCNGTVS 1497
Cdd:pfam15921 389 REKELSlEKEQNKRLWDRdtgnsiTIDHLRREL--DDRNMEVQRleallKAMKSECQGQ--MERQMAAIQGKNESLEKVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1498 TSVAALNHA----RNATDSLNAAKEELQSVAKKLQDIASLTQDVKN--QAMNT-LKKAQKKKD-------HFENNNKKLK 1563
Cdd:pfam15921 465 SLTAQLESTkemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERaiEATNAeITKLRSRVDlklqelqHLKNEGDHLR 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1564 DFIKKIRDFLTEEGADPESIEKVAQQVLSITLPVNKTALDQMVMQIKDSlsnltNVEGIVNQTSQHISIAKELLDKaKDA 1643
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA-----QLEKEINDRRLELQEFKILKDK-KDA 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1644 KSRA----------EGVK--DSANNTKQALdmseKAIEKARAAL----KEANNNLNSTrNATVEVDERltQLEDKQMDVM 1707
Cdd:pfam15921 619 KIRElearvsdlelEKVKlvNAGSERLRAV----KDIKQERDQLlnevKTSRNELNSL-SEDYEVLKR--NFRNKSEEME 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1708 MRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLggESGGLNSiNQKAQDIK 1787
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL--EEAMTNA-NKEKHFLK 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 1788 NE----AEDLLSKATKGIDQLKKLEKkFKSNEQRMQKQRMELDELKENATL----VRDVIREQVQK 1845
Cdd:pfam15921 769 EEknklSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLqfaeCQDIIQRQEQE 833
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
828-876 |
2.30e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.84 E-value: 2.30e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 828 CQCDPQGSLSGECHKVGGDCHCKPNVMGRRCDQCTPGTYGYGANGCTVC 876
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
876-918 |
3.96e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.45 E-value: 3.96e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1848696099 876 CDCHSEGSLSHQCDPVTGQCQCRHGATGRQCSDCQPGQWGFPS 918
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1842 |
6.68e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 72.63 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1603 DQMVMQIKD---SLSNLTNVEGIV-----NQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAA 1674
Cdd:COG4372 2 DRLGEKVGKarlSLFGLRPKTGILiaalsEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1675 LKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLND 1754
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1755 TENRYQELQMKVDSLggesgGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATL 1834
Cdd:COG4372 162 LQEELAALEQELQAL-----SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
....*...
gi 1848696099 1835 VRDVIREQ 1842
Cdd:COG4372 237 ALLDALEL 244
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
827-872 |
1.75e-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: 63.53 E-value: 1.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 827 SCQCDPQGSLSGECHKVGGDCHCKPNVMGRRCDQCTPGTYGYGANG 872
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
876-919 |
3.97e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 3.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 876 CDCHSEGSLSHQCDPVTGQCQCRHGATGRQCSDCQPGQWG--FPSC 919
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1276-1848 |
9.05e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1276 IKELERKLKGVQDLISMEDSnrIHQLIG----------QSIDDLRAEIALTDGRLMGVTR---ELNTTADEEEALRHILS 1342
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTEN--IEELIKekekeleevlREINEISSELPELREELEKLEKevkELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1343 VLEKEL-----------THINATVAHKQRLLDNY--LTS--GFADQFEKVKKFYQESAKAEEKcnasVSGPLSPVEQskE 1407
Cdd:PRK03918 249 SLEGSKrkleekireleERIEELKKEIEELEEKVkeLKElkEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEE--E 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1408 TRAVTEDLLDASKVKflRALAAQNKSLSELQQKAHDLDKKvHHLSHKVCGGHSNASvngscpdsqcggagchddqgnhvc 1487
Cdd:PRK03918 323 INGIEERIKELEEKE--ERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELE------------------------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1488 gghgcngTVSTSVAALN--HARNATDSLNAAKEELQSVAKKLQD-IASLTQDVK--NQAMNTLKKAQKK---------KD 1553
Cdd:PRK03918 376 -------RLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITArIGELKKEIKelKKAIEELKKAKGKcpvcgreltEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1554 HFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVLSI-----TLPVNKTALDQmVMQIKDSLSNLtNVEGIVNQTSQ 1628
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkesELIKLKELAEQ-LKELEEKLKKY-NLEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1629 hisiAKELLDKAKDAKSRAEGVKDSA---NNTKQALDMSEKAIEKARAALKEANNNLNSTRNATV-EVDERLTQLEdKQM 1704
Cdd:PRK03918 527 ----YEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELE-PFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1705 DVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQElqmkvdslggesgglnsinQKAQ 1784
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-------------------EEYE 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1785 DIKNEAEDLLSkatkgidQLKKLEKKFKSNEQRMQKQRMELDELKENATLVR----------------DVIREQVQKYSN 1848
Cdd:PRK03918 663 ELREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEELEEREkakkeleklekalervEELREKVKKYKA 735
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1187-1227 |
9.20e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 9.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1848696099 1187 CNCHLLGSEMAQCDRSTGACECKEGAAGKHCDECARGFTGD 1227
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1139-1187 |
1.70e-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: 57.75 E-value: 1.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 1139 CGCDPQHALGTHCNMFTGQCQCRPGFGGKQCTECEQFHWGDPRLQCQEC 1187
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
405-462 |
2.42e-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: 57.36 E-value: 2.42e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1848696099 405 CDCDPVGSmEGGVCDSHTdldvgmisGQCRCKANVKGTRCDDCKESYYGLSQNDPLGC 462
Cdd:pfam00053 1 CDCNPHGS-LSDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1187-1235 |
3.71e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 3.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 1187 CNCHLLGSEMAQCDRSTGACECKEGAAGKHCDECARGFTGDFPKCVQCH 1235
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1187-1231 |
1.62e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 1187 CNCHLLGSEMAQCDRSTGACECKEGAAGKHCDECARGFTGD-FPKC 1231
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-515 |
1.76e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 1.76e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 464 PCNCDPRGIImmGAPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSNDLAGCR 515
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
465-519 |
3.27e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 3.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1848696099 465 CNCDPRGIImmGAPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSNDLagcrPCDC 519
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1139-1180 |
5.05e-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: 53.51 E-value: 5.05e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1848696099 1139 CGCDPQHALGTHCNMFTGQCQCRPGFGGKQCTECEQFHWGDP 1180
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1139-1184 |
7.33e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 7.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 1139 CGCDPQHALGTHCNMFTGQCQCRPGFGGKQCTECEQFHWGDPRLQC 1184
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1030-1081 |
6.45e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 6.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1848696099 1030 PCECNGNIDTkdPGSCDPRTGQCLnCLYHTDGPSCGHCQHGYYGNAL-AHDCR 1081
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
516-555 |
7.62e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 7.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1848696099 516 PCDCDFGGAYNNRCMMESGQCDCRRHLIGRQCSEVQPGYF 555
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
404-463 |
8.57e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 8.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 404 ACDCDPVGSmEGGVCDSHTdldvgmisGQCRCKANVKGTRCDDCKESYYGLSQNdPLGCQ 463
Cdd:cd00055 1 PCDCNGHGS-LSGQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
517-555 |
9.35e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.35e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1848696099 517 CDCDFGGAYNNRCMMESGQCDCRRHLIGRQCSEVQPGYF 555
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1031-1075 |
1.25e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.25e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1848696099 1031 CECNGNIDTkdPGSCDPRTGQCLnCLYHTDGPSCGHCQHGYYGNA 1075
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1101-1136 |
1.26e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.26e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1848696099 1101 HCDRQTGACPCRQNVAGHNCDQCAPNHWNYGQDQGC 1136
Cdd:pfam00053 12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
921-966 |
2.70e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 2.70e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 921 PCQCNSHADI---CDPRNGECRdCRDYTTGHLCDSCADGFFGNPVLGSG 966
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
465-508 |
3.12e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1848696099 465 CNCDPRGIImmGAPCDQISGDCSCKRYVTGRYCNQCLPEYWGLS 508
Cdd:smart00180 1 CDCDPGGSA--SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
971-1026 |
5.00e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 5.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 971 PCPCPGNpGSDHfnaHSCHADHtsnqIICNCREGYTGLRCDQCAPGYYGNPEQYGG 1026
Cdd:cd00055 1 PCDCNGH-GSLS---GQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
405-458 |
7.05e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 405 CDCDPVGSmEGGVCDSHTdldvgmisGQCRCKANVKGTRCDDCKESYYGLSQND 458
Cdd:smart00180 1 CDCDPGGS-ASGTCDPDT--------GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
922-969 |
8.37e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 47.35 E-value: 8.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1848696099 922 CQCNSHA---DICDPRNGECrDCRDYTTGHLCDSCADGFFGNPVlGSGDHC 969
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1137 |
1.46e-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: 1.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 1083 CTCVTAGTIHSacsdgqcHCDRQTGACPCRQNVAGHNCDQCAPNHWNY-GQDQGCE 1137
Cdd:cd00055 2 CDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-330 |
1.69e-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: 46.58 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1848696099 277 SCFCYGHAS---ECAPVpgvdarengmiHGRCVCKHNTEGLNCERCRHFHNDLPWRP 330
Cdd:cd00055 1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1083-1136 |
2.31e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 2.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 1083 CTCVTAGTIHSacsdgqcHCDRQTGACPCRQNVAGHNCDQCAPNHWNYgQDQGC 1136
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
342-398 |
2.54e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 2.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 342 CNCNGHSS---HCHFdmavylatgniSGGVCDdCQHNTMGRNCEMCKPFYYQDPNRDVRD 398
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
972-1028 |
3.40e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 3.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1848696099 972 CPCPGNpGSDHfnaHSCHadhtSNQIICNCREGYTGLRCDQCAPGYYGNPEQYGGQC 1028
Cdd:pfam00053 1 CDCNPH-GSLS---DTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
342-392 |
6.41e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 6.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 342 CNCNGHSS---HCHFDmavylatgnisGGVCDdCQHNTMGRNCEMCKPFYYQDP 392
Cdd:cd00055 2 CDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
517-555 |
7.25e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 44.65 E-value: 7.25e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1848696099 517 CDCDFGGAYNNRCMMESGQCDCRRHLIGRQCSEVQPGYF 555
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
987-1023 |
5.56e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 5.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1848696099 987 SCHADHTSNQI------ICNCREGYTGLRCDQCAPGYYGNPEQ 1023
Cdd:smart00180 2 DCDPGGSASGTcdpdtgQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1031-1074 |
7.04e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 7.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 1031 CECN--GNIDtkdpGSCDPRTGQCLnCLYHTDGPSCGHCQHGYYGN 1074
Cdd:smart00180 1 CDCDpgGSAS----GTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1581-1812 |
1.18e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 45.74 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1581 ESIEKVAQQVLSITLPVNKTA--LDQMVMQIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKD-AKSRAEGVKDSANNT 1657
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAerMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITaMDQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1658 KQALDMSEK----------------------AIEKARA---------------ALkeANNnlnsTRNATVEVDERLTQLE 1700
Cdd:smart00283 84 EELEESSDEigeivsviddiadqtnllalnaAIEAARAgeagrgfavvadevrKL--AER----SAESAKEIESLIKEIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1701 DKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSlggesgglnsIN 1780
Cdd:smart00283 158 EETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDE----------IA 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1848696099 1781 QKAQDIKNEAEDlLSKATKGI----DQLKKLEKKFK 1812
Cdd:smart00283 228 QVTQETAAMSEE-ISAAAEELsglaEELDELVERFK 262
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
1511-1726 |
1.73e-04 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 45.72 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1511 DSLNAAKEELQSVakkLQDIASLTQDVKNQAMNTLKKAQKKKDHFENNN---KKLKDFIKKIRDFLTEEG----ADPESI 1583
Cdd:cd22654 104 SQLQTIQNSMEQT---SSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSNgeiAQLRTQIKTINDEIQEELtkilNRPIEV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1584 EKVAQQVLSITLP-VNKTALDQMVmqikdslsNLTNVEGIVNQT-----SQHISIAKELLDKAK----------DAKSRA 1647
Cdd:cd22654 181 GDGSINIGKQVFTiTITTATTKTV--------DVTSIGGLINGIgnasdDEVKEAANKIQQKQKelvdlikklsDAEIQA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1648 EG---VKDSANNTKQALDMSEKAIEKARAALKEANNNLNstrnatvEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKT 1724
Cdd:cd22654 253 TQltlVEDQVNGFTELIKRQIATLENLVEDWEMLNQNMN-------QLQTNVNSGKIDSKLLQKQLKQIKKISDELNKQT 325
|
..
gi 1848696099 1725 EQ 1726
Cdd:cd22654 326 KQ 327
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1734-1828 |
2.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1734 AIAQANNATQVASSlEQSLNDTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKS 1813
Cdd:COG3883 1 ALALALAAPTPAFA-DPQIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE 76
|
90
....*....|....*
gi 1848696099 1814 NEQRMQKQRMELDEL 1828
Cdd:COG3883 77 AEAEIEERREELGER 91
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1745-1821 |
2.91e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 42.19 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1745 ASSLE---QSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNE------AEDLLSKATKGIDQLKKLEKKFKSNE 1815
Cdd:pfam18595 1 SSTLAeekEELAELERKARELQAKIDALQVVEKDLRSCIKLLEEIEAElakleeAKKKLKELRDALEEKEIELRELERRE 80
|
....*.
gi 1848696099 1816 QRMQKQ 1821
Cdd:pfam18595 81 ERLQRQ 86
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
342-392 |
6.50e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 6.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 342 CNCNG---HSSHCHFDmavylatgnisGGVCDdCQHNTMGRNCEMCKPFYYQDP 392
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
301-332 |
1.68e-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: 38.10 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|..
gi 1848696099 301 IHGRCVCKHNTEGLNCERCRHFHNDLPWRPAE 332
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-328 |
3.20e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 3.20e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1274-1451 |
9.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1274 TRIKELERKLKGVQDLISM---EDSNRIHQLIGQSIDDLRAEIALTDGRLMGVTRELNTTADEEEALRHI--------LS 1342
Cdd:COG4913 262 ERYAAARERLAELEYLRAAlrlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1343 VLEKELTHINATVAHKQRLLDNYLT-------------SGFADQFEKVKKFYQESAKAEEKCNAsvsgplspveqsketr 1409
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEAllaalglplpasaEEFAALRAEAAALLEALEEELEALEE---------------- 405
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1848696099 1410 AVTEdlLDASKVKFLRALAAQNKSLSELQQKAHDLDKKVHHL 1451
Cdd:COG4913 406 ALAE--AEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
42-276 |
1.01e-108 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 345.72 E-value: 1.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 42 CYPATGNLLIGRAVnlSATSTCGLNGPQPYCIVSHLQESDKCFECNSQHrfdpyrHRNSHRIENVIYLMDGNgDNTWWQS 121
Cdd:pfam00055 1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRD------PHNSHPPSNLTDSNNGT-NETWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 122 VNGE---ESVSIRLNLEAEFHFTHLIIKFKTFRPAAMFIERSADFGRTWRPYRYFASNCTKTFpGIPANGLHHIND--II 196
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIKDdeVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 197 CEERYSDIEPSTNGEVIYKVL--DPAIHVKDpYSLDIQELLRITNLRINFTKLNTLGDDLLDRRfDVLQKYYYAIYELVV 274
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDP-SVLRKYYYAISDISV 228
|
..
gi 1848696099 275 RG 276
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
36-276 |
3.49e-83 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 273.08 E-value: 3.49e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 36 GCTDGSCYPATGNLLIGRAVnlSATSTCGLNGPQPYCI-VSHLQESDKCFECNSQHrfdpyrHRNSHRIENVIylmDGNG 114
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREV--TATSTCGEPGPERYCKlVGHTEQGKKCDYCDARN------PRRSHPAENLT---DGNN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 115 DN--TWWQS---VNGEESVSIRLNLEAEFHFTHLIIKFKTFRPAAMFIERSaDFGRTWRPYRYFASNCTKTFPGIP--AN 187
Cdd:smart00136 70 PNnpTWWQSeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPrgPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 188 GLHHINDIICEERYSDIEPSTNGEVIYKVLDPAIHVKD-PYSLDIQELLRITNLRINFTKLNTLGDDLLDRRFDVLQKYY 266
Cdd:smart00136 149 TKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYY 228
|
250
....*....|
gi 1848696099 267 YAIYELVVRG 276
Cdd:smart00136 229 YAISDIAVGG 238
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1780-1849 |
1.14e-24 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 98.89 E-value: 1.14e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1780 NQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1510-1846 |
1.30e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 95.86 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1510 TDSLNAAKEELQSVAKKLQDIASLTQDVKNQamntLKKAQKKkdhFENNNKKLKDFIKKIRDFLTEegadPESIEKVAQQ 1589
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQ----LSEKQKE---LEQNNKKIKELEKQLNQLKSE----ISDLNNQKEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1590 VLSITLpvnKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHIS-IAKELLDKAKDAKSRAEGVKDSANNTKQaldmsekaI 1668
Cdd:TIGR04523 307 DWNKEL---KSELKNQEKKLEEIQNQISQNNKIISQLNEQISqLKKELTNSESENSEKQRELEEKQNEIEK--------L 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1669 EKARAALKEANNNLNSTRNA---TVEVDERLTQLEDKQMDVM-MRLNNLSREVEALRNKTEQNRQMAKDAIAQ------- 1737
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDlesKIQNQEKLNQQKDEQIKKLqQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeli 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1738 ANNATQVASSLEQSLNDTENRY----QELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKS 1813
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350
....*....|....*....|....*....|...
gi 1848696099 1814 NEQRMQKQRMELDELKENatLVRDVIREQVQKY 1846
Cdd:TIGR04523 536 KESKISDLEDELNKDDFE--LKKENLEKEIDEK 566
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
876-924 |
9.11e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 9.11e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 876 CDCHSEGSLSHQCDPVTGQCQCRHGATGRQCSDCQPGQWGFPSCSPCQC 924
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1242-1849 |
1.69e-14 |
|
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: 79.72 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1242 DDVVCQIKRDLEHIQYTAQKIlesgvmpgvgdTRIKELERKLKGVQDLISMedsNRIHQLIGQsIDDLRAEIALTDGRLM 1321
Cdd:TIGR02168 192 EDILNELERQLKSLERQAEKA-----------ERYKELKAELRELELALLV---LRLEELREE-LEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1322 GVTRELNTTADEEEALRHILSVLEKELTHINATVahkqrlldnYLTSGFADQFEKVKKFYQESAKAEEKCNASVSGPLSP 1401
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKEL---------YALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1402 VEQSKETravTEDLLDASKVKF----------------LRALAAQNKSLSELQQKAHD---------------------- 1443
Cdd:TIGR02168 328 LESKLDE---LAEELAELEEKLeelkeelesleaeleeLEAELEELESRLEELEEQLEtlrskvaqlelqiaslnneier 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1444 LDKKVHHLSHKVCGGHSNASVNGSCPDSqcggAGCHDDQGNHVCGGHGCNGTVSTSVAALNHARNATDSLNAAKEELQSV 1523
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEE----AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1524 AKKLQDIASLtQDVKNQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRDFLTeegADPE---SIEKV----AQQVLSITLP 1596
Cdd:TIGR02168 481 ERELAQLQAR-LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS---VDEGyeaAIEAAlggrLQAVVVENLN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1597 VNKTALDQM------------VMQIKDSLSNLTNVEGIVNQTSqHISIAKELLDKAKDAKSRAEGVKDS---ANNTKQAL 1661
Cdd:TIGR02168 557 AAKKAIAFLkqnelgrvtflpLDSIKGTEIQGNDREILKNIEG-FLGVAKDLVKFDPKLRKALSYLLGGvlvVDDLDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1662 DMSEK-------------------AIEKARAalkEANNNLNSTRNATVEVDERLTQLEDKqmdvmmrLNNLSREVEALRN 1722
Cdd:TIGR02168 636 ELAKKlrpgyrivtldgdlvrpggVITGGSA---KTNSSILERRREIEELEEKIEELEEK-------IAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1723 KTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKAtkgID 1802
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EA 782
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1848696099 1803 QLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
828-873 |
2.16e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.88 E-value: 2.16e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 828 CQCDPQGSLSGECHKVGGDCHCKPNVMGRRCDQCTPGTYGYGANGC 873
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1273-1845 |
3.09e-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: 78.62 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1273 DTRIKELERKLKGVQD---LISMEDSNRIHQLIGQSIDDLRAEIALTDGRLMGVTRELNTTADEEEALRHILSVLEKELT 1349
Cdd:pfam15921 230 DTEISYLKGRIFPVEDqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1350 HINATVAHKQRLLDNYLtSGFADQFEKVKKFYQESAKAEEKCNASVSGPLSPVEQSKETRAVTEDLLDASKVKFLRALAA 1429
Cdd:pfam15921 310 NQNSMYMRQLSDLESTV-SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1430 QNKSLS-ELQQKAHDLDK------KVHHLSHKVcgGHSNASVNG-----SCPDSQCGGAgcHDDQGNHVCGGHGCNGTVS 1497
Cdd:pfam15921 389 REKELSlEKEQNKRLWDRdtgnsiTIDHLRREL--DDRNMEVQRleallKAMKSECQGQ--MERQMAAIQGKNESLEKVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1498 TSVAALNHA----RNATDSLNAAKEELQSVAKKLQDIASLTQDVKN--QAMNT-LKKAQKKKD-------HFENNNKKLK 1563
Cdd:pfam15921 465 SLTAQLESTkemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERaiEATNAeITKLRSRVDlklqelqHLKNEGDHLR 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1564 DFIKKIRDFLTEEGADPESIEKVAQQVLSITLPVNKTALDQMVMQIKDSlsnltNVEGIVNQTSQHISIAKELLDKaKDA 1643
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA-----QLEKEINDRRLELQEFKILKDK-KDA 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1644 KSRA----------EGVK--DSANNTKQALdmseKAIEKARAAL----KEANNNLNSTrNATVEVDERltQLEDKQMDVM 1707
Cdd:pfam15921 619 KIRElearvsdlelEKVKlvNAGSERLRAV----KDIKQERDQLlnevKTSRNELNSL-SEDYEVLKR--NFRNKSEEME 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1708 MRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLggESGGLNSiNQKAQDIK 1787
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL--EEAMTNA-NKEKHFLK 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 1788 NE----AEDLLSKATKGIDQLKKLEKkFKSNEQRMQKQRMELDELKENATL----VRDVIREQVQK 1845
Cdd:pfam15921 769 EEknklSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLqfaeCQDIIQRQEQE 833
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1273-1848 |
1.51e-13 |
|
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: 76.63 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1273 DTRIKELERKLKGVQDLISMEDSNRIH---QLIGQSIDDLRAEIALTDGRLMGVTRELNTTADEEEALRHILSVLEKELT 1349
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1350 HINATVAHKQRLLDNYLTsgfadqfekvkkfYQESAKAEEKCNASVSGPLSPVEQSKETRAVTEDLLDASKVKFLRALAA 1429
Cdd:TIGR02168 486 QLQARLDSLERLQENLEG-------------FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1430 QNKslsELQQKAHDLDKKvhHLSHKVcgghsnasvnGSCPDSQCGGAGCHDDQGNHVCGGHGCNGTVSTSVAALNHARNA 1509
Cdd:TIGR02168 553 ENL---NAAKKAIAFLKQ--NELGRV----------TFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1510 ----------TDSLNAAkeelQSVAKKLQ----------DIA----SLTQDVKNQAMNTLKKAQKkkdhFENNNKKLKDF 1565
Cdd:TIGR02168 618 lsyllggvlvVDDLDNA----LELAKKLRpgyrivtldgDLVrpggVITGGSAKTNSSILERRRE----IEELEEKIEEL 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1566 IKKIRDFLTEEGADPESIEKVAQQVLSItlpvnKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHISIAKELLdkaKDAKS 1645
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL---TELEA 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1646 RAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRnkte 1725
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE---- 837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1726 qnrQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESG----GLNSINQKAQDIKNEAEDLLSKATKGI 1801
Cdd:TIGR02168 838 ---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEELSEELRELESKRSELR 914
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1848696099 1802 DQLKKLEKKFKSNEQRMQKQRMELDELKENAT-LVRDVIREQVQKYSN 1848
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENK 962
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
828-876 |
2.30e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.84 E-value: 2.30e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 828 CQCDPQGSLSGECHKVGGDCHCKPNVMGRRCDQCTPGTYGYGANGCTVC 876
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1515-1847 |
3.90e-13 |
|
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: 75.10 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1515 AAKEELQSVAKKLqDIASLTQDVKNQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRdfLTEEGADPESIEKVAQQVLSIT 1594
Cdd:TIGR02169 174 KALEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEL--LKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1595 lpvnkTALDQMVMQIKDSLSNLTNVEGIVNQTSQHISiaKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAA 1674
Cdd:TIGR02169 251 -----EELEKLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1675 LKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQnrqmakdaIAQANNATQVA-SSLEQSLN 1753
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE--------VDKEFAETRDElKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1754 DTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSKATK-------GIDQLKKLEKKFKSNEQRMQKQRMELD 1826
Cdd:TIGR02169 396 KLKREINELKRELDRLQEE---LQRLSEELADLNAAIAGIEAKINEleeekedKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340
....*....|....*....|.
gi 1848696099 1827 ELKENATLVRDVIREQVQKYS 1847
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELA 493
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
876-918 |
3.96e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 65.45 E-value: 3.96e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1848696099 876 CDCHSEGSLSHQCDPVTGQCQCRHGATGRQCSDCQPGQWGFPS 918
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1842 |
6.68e-13 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 72.63 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1603 DQMVMQIKD---SLSNLTNVEGIV-----NQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAA 1674
Cdd:COG4372 2 DRLGEKVGKarlSLFGLRPKTGILiaalsEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1675 LKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLND 1754
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1755 TENRYQELQMKVDSLggesgGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATL 1834
Cdd:COG4372 162 LQEELAALEQELQAL-----SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
....*...
gi 1848696099 1835 VRDVIREQ 1842
Cdd:COG4372 237 ALLDALEL 244
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
827-872 |
1.75e-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: 63.53 E-value: 1.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 827 SCQCDPQGSLSGECHKVGGDCHCKPNVMGRRCDQCTPGTYGYGANG 872
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
876-919 |
3.97e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 3.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 876 CDCHSEGSLSHQCDPVTGQCQCRHGATGRQCSDCQPGQWG--FPSC 919
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1326-1848 |
5.99e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.82 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1326 ELNTTADEEEALRHILSVLEKELTHINATVA--HKQRLLDNYLTSGFADQFEKVKKFYQESAKAEEKcNASVSGPLSpvE 1403
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDkiKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ-NNQLKDNIE--K 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1404 QSKETRAVTEDLLDASKvKFLRALAAQNKSLSELQQKAHDLDKKVHHLSHKvcgghsnasvngscpdsqcggagchDDQG 1483
Cdd:TIGR04523 237 KQQEINEKTTEISNTQT-QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-------------------------EKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1484 NhvcgghgcngTVSTSVAALNHARNAtDSLNAAKEELQSVAKKLQDIAS-LTQDVK--NQAMNTLKKAQKKKDHFENNNK 1560
Cdd:TIGR04523 291 N----------QLKSEISDLNNQKEQ-DWNKELKSELKNQEKKLEEIQNqISQNNKiiSQLNEQISQLKKELTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1561 KLKDFIK----KIRDFLTEEGADPESIEKVAQQVLSI-------------------TLPVNKTALDQ-------MVMQIK 1610
Cdd:TIGR04523 360 EKQRELEekqnEIEKLKKENQSYKQEIKNLESQINDLeskiqnqeklnqqkdeqikKLQQEKELLEKeierlkeTIIKNN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1611 DSLSNLTNVEgivnqTSQHISIaKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAiekaraaLKEANNNLNSTRNATV 1690
Cdd:TIGR04523 440 SEIKDLTNQD-----SVKELII-KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE-------LKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1691 EVDERLTQLEDKQMDVMMRLNNLSREV------------EALRNKTEQNRQMAKDAIAQANnatQVASSLEQSLNDTENR 1758
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKkekeskisdledELNKDDFELKKENLEKEIDEKN---KEIEELKQTQKSLKKK 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1759 YQELQMKVDSLggesgglnsiNQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDV 1838
Cdd:TIGR04523 584 QEEKQELIDQK----------EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
570
....*....|
gi 1848696099 1839 IREQVQKYSN 1848
Cdd:TIGR04523 654 IKEIRNKWPE 663
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1619-1845 |
7.09e-12 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 68.40 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1619 VEGIVNQTSQHISIAKELLDKAKDAKSRaegvKDSANNTKQALdmsekaIEKARAaLKEANNNLNSTRNATVEVDERLTQ 1698
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEE----RDELNEKLNEL------REELDE-LRKELAELNKAGGSIDKLRKEIER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1699 LEDKQ----------MDVMMRLNNLSREVEALRNKTEQNRQMaKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDS 1768
Cdd:COG1340 121 LEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKL-KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848696099 1769 LggesgglnsiNQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKE-NATLVRDVIREQVQK 1845
Cdd:COG1340 200 L----------YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKkQRALKREKEKEELEE 267
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1276-1848 |
9.05e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1276 IKELERKLKGVQDLISMEDSnrIHQLIG----------QSIDDLRAEIALTDGRLMGVTR---ELNTTADEEEALRHILS 1342
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTEN--IEELIKekekeleevlREINEISSELPELREELEKLEKevkELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1343 VLEKEL-----------THINATVAHKQRLLDNY--LTS--GFADQFEKVKKFYQESAKAEEKcnasVSGPLSPVEQskE 1407
Cdd:PRK03918 249 SLEGSKrkleekireleERIEELKKEIEELEEKVkeLKElkEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEE--E 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1408 TRAVTEDLLDASKVKflRALAAQNKSLSELQQKAHDLDKKvHHLSHKVCGGHSNASvngscpdsqcggagchddqgnhvc 1487
Cdd:PRK03918 323 INGIEERIKELEEKE--ERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELE------------------------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1488 gghgcngTVSTSVAALN--HARNATDSLNAAKEELQSVAKKLQD-IASLTQDVK--NQAMNTLKKAQKK---------KD 1553
Cdd:PRK03918 376 -------RLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITArIGELKKEIKelKKAIEELKKAKGKcpvcgreltEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1554 HFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVLSI-----TLPVNKTALDQmVMQIKDSLSNLtNVEGIVNQTSQ 1628
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkesELIKLKELAEQ-LKELEEKLKKY-NLEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1629 hisiAKELLDKAKDAKSRAEGVKDSA---NNTKQALDMSEKAIEKARAALKEANNNLNSTRNATV-EVDERLTQLEdKQM 1704
Cdd:PRK03918 527 ----YEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELE-PFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1705 DVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQElqmkvdslggesgglnsinQKAQ 1784
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-------------------EEYE 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1785 DIKNEAEDLLSkatkgidQLKKLEKKFKSNEQRMQKQRMELDELKENATLVR----------------DVIREQVQKYSN 1848
Cdd:PRK03918 663 ELREEYLELSR-------ELAGLRAELEELEKRREEIKKTLEKLKEELEEREkakkeleklekalervEELREKVKKYKA 735
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1187-1227 |
9.20e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 9.20e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1848696099 1187 CNCHLLGSEMAQCDRSTGACECKEGAAGKHCDECARGFTGD 1227
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1139-1187 |
1.70e-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: 57.75 E-value: 1.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 1139 CGCDPQHALGTHCNMFTGQCQCRPGFGGKQCTECEQFHWGDPRLQCQEC 1187
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1507-1837 |
2.04e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1507 RNATDSLNAAKEELQSVAKKLQDIASLTQDVKNQAMnTLKKAQKKKDHFENNNKKLKDFIKKIRDFLTEEGADPE----S 1582
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERREELETLEAEIEDLRE-TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddaD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1583 IEKVAQQvlsitlpvnKTALDQMVMQIKDSLsnltnvEGIVNQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTKQALD 1662
Cdd:PRK02224 309 AEAVEAR---------REELEDRDEELRDRL------EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1663 MSEKAIEKARAALKEANNNLNSTR----NATV---EVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMakdai 1735
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRerfgDAPVdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL----- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1736 AQANNATQVASSLEQS-----LNDTENRYQELQMKVDSLGGEsggLNSINQKAqdikNEAEDLLSKAtkgiDQLKKLEKK 1810
Cdd:PRK02224 449 LEAGKCPECGQPVEGSphvetIEEDRERVEELEAELEDLEEE---VEEVEERL----ERAEDLVEAE----DRIERLEER 517
|
330 340
....*....|....*....|....*..
gi 1848696099 1811 FKSNEQRMQKQRMELDELKENATLVRD 1837
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRE 544
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
405-462 |
2.42e-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: 57.36 E-value: 2.42e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1848696099 405 CDCDPVGSmEGGVCDSHTdldvgmisGQCRCKANVKGTRCDDCKESYYGLSQNDPLGC 462
Cdd:pfam00053 1 CDCNPHGS-LSDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1531-1845 |
2.63e-10 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 64.06 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1531 ASLTQDVKNQAMNTLKKAQKKKDhfeNNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVLSITLPVNkTAldqmvmqIK 1610
Cdd:pfam15905 47 ASTPATARKVKSLELKKKSQKNL---KESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLN-AA-------VR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1611 DSLSNLTNVEgivnqtsqhiSIAKELLD--KAKD---AKSRAEGVKDSAN-------NTKQALDMSEKAI----EKARAA 1674
Cdd:pfam15905 116 EKTSLSASVA----------SLEKQLLEltRVNEllkAKFSEDGTQKKMSslsmelmKLRNKLEAKMKEVmakqEGMEGK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1675 LKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDaIAQannatqvassLEQSLND 1754
Cdd:pfam15905 186 LQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD-IAQ----------LEELLKE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1755 TENRYQELQmkvdslggesgglNSINQKAQDIKNEAEDLLSKatkgIDQLKKlEKKFKSNEQRMQKQRM--ELDELKENA 1832
Cdd:pfam15905 255 KNDEIESLK-------------QSLEEKEQELSKQIKDLNEK----CKLLES-EKEELLREYEEKEQTLnaELEELKEKL 316
|
330
....*....|...
gi 1848696099 1833 TLVRDVIREQVQK 1845
Cdd:pfam15905 317 TLEEQEHQKLQQK 329
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1780-1849 |
3.60e-10 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 57.75 E-value: 3.60e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1780 NQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:cd22301 1 NERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1187-1235 |
3.71e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 3.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 1187 CNCHLLGSEMAQCDRSTGACECKEGAAGKHCDECARGFTGDFPKCVQCH 1235
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1638-1845 |
4.65e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1638 DKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDkqmdvmmRLNNLSREV 1717
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1718 EALRNKTEQNRQMAKDAIAQA---NNATQVASSLEQ-SLNDTENRY-------QELQMKVDSLGGESGGLNSINQKAQDI 1786
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyrlGRQPPLALLLSPeDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848696099 1787 KNEAEDLLSKATKGIDQLKKL----EKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQK 1845
Cdd:COG4942 173 RAELEALLAELEEERAALEALkaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1331-1845 |
5.10e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1331 ADEEEALRHILSVLEKELTHINATVAHKQRllDNYLTSGFADQFEKVKKFYQESAKAEEKCNASVSGPLSPVEQSKETRA 1410
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEER--NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1411 VTEdlldASKVKFLRALAAQNKSLSELQQKAHDLDKKVHHLSHKVCGGHSNASVngscpdsqcggagchddqgnhvcggh 1490
Cdd:PTZ00121 1298 AEE----KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA-------------------------- 1347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1491 gcngtvstsvaALNHARNATDSLNAAKEELQSVAKKLQDIASLTQDVKNQAmNTLKKAQKKKDHFENNNKKLKDFIKKir 1570
Cdd:PTZ00121 1348 -----------AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA-EEKKKADEAKKKAEEDKKKADELKKA-- 1413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1571 dflTEEGADPESIEKVAQQVLSITLPVNKTALDQMVMQIKDSLSNLTNVEGIvNQTSQHISIAKELLDKAKDA------K 1644
Cdd:PTZ00121 1414 ---AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA-KKKAEEAKKADEAKKKAEEAkkadeaK 1489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1645 SRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATvEVDERLTQLEDKQMDVMMRLNNLsREVEALRnKT 1724
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK-KADEAKKAEEKKKADELKKAEEL-KKAEEKK-KA 1566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1725 EQNRQMAKDAIAQANNATQVASSLEQSLNDTENRY-QELQMKVDSLGGESGGLNSINQ--KAQDIKNEAEDLLSKATKGI 1801
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYeEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1848696099 1802 DQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQK 1845
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1503-1743 |
1.16e-09 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 61.27 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1503 LNHARNATDSLNAAKEELQsvaKKLQDIASLTQDVKNQAMNTLkkaqkkkdhfeNNNKKLKDFIKKIRDFLTEegadpeS 1582
Cdd:pfam06008 42 IEILEKELSSLAQETEELQ---KKATQTLAKAQQVNAESERTL-----------GHAKELAEAIKNLIDNIKE------I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1583 IEKVAQQVLSITLPVNKTaLDQMVMQIKDSLSNLTNvegivNQTSQHISIAKELLDKAKDAKSRA--------EGVKDSA 1654
Cdd:pfam06008 102 NEKVATLGENDFALPSSD-LSRMLAEAQRMLGEIRS-----RDFGTQLQNAEAELKAAQDLLSRIqtwfqspqEENKALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1655 NNTKQALDMSEKAIEKARAALKEAnnnLNSTRNAT---VEVDERLTQLEDKQmdvmmrlnnlsREVEALRNKTEQNRQMA 1731
Cdd:pfam06008 176 NALRDSLAEYEAKLSDLRELLREA---AAKTRDANrlnLANQANLREFQRKK-----------EEVSEQKNQLEETLKTA 241
|
250
....*....|..
gi 1848696099 1732 KDAIAQANNATQ 1743
Cdd:pfam06008 242 RDSLDAANLLLQ 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1501-1829 |
1.24e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.47 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1501 AALNHARNATDSLNaakEELQSVAKKLQDIASLTQDVKNQAmNTLK--------KAQKKKDHFENNNKKLKDFIKKIRDF 1572
Cdd:COG1340 22 EEIEELKEKRDELN---EELKELAEKRDELNAQVKELREEA-QELRekrdelneKVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1573 ---LTEEGADPESIEKVAQQvlsitlpvnktaLDQMVMQIkdslsnltnvegivnQTSQhISIAKE--LLDKAKDAKSRA 1647
Cdd:COG1340 98 rkeLAELNKAGGSIDKLRKE------------IERLEWRQ---------------QTEV-LSPEEEkeLVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1648 EGVKDSANNTKQALDMSEKaIEKARAALKEANNNLNSTRNatvEVDERLTQledkqmdvmmrLNNLSREVEALRNKteqn 1727
Cdd:COG1340 150 EKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELAE---EAQELHEE-----------MIELYKEADELRKE---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1728 rqmAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLggesgglnsinqkaqdiKNEAEDLLSKATKGIDQLKK- 1806
Cdd:COG1340 211 ---ADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL-----------------RKKQRALKREKEKEELEEKAe 270
|
330 340
....*....|....*....|....
gi 1848696099 1807 -LEKKFKSNEqrmqkqRMELDELK 1829
Cdd:COG1340 271 eIFEKLKKGE------KLTTEELK 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1634-1845 |
1.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1634 KELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNL 1713
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1714 SREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDL 1793
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEA 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1794 LSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQK 1845
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1622-1846 |
1.57e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.11 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1622 IVNQtsqhisIAKELLDKAKDAKSRAegvkdsannTKQALDMSEKAIEKARAALKEANNNLNS--TRNATVEVDERLTQL 1699
Cdd:COG3206 153 VANA------LAEAYLEQNLELRREE---------ARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1700 EDKQMDVMMRLNNLS---REVEALRNKTEQNRQMAKDAIAQANNATQVA------SSLEQSLNDTENRY-------QELQ 1763
Cdd:COG3206 218 LQQLSELESQLAEARaelAEAEARLAALRAQLGSGPDALPELLQSPVIQqlraqlAELEAELAELSARYtpnhpdvIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1764 MKVDSLggesggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQV 1843
Cdd:COG3206 298 AQIAAL------RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
...
gi 1848696099 1844 QKY 1846
Cdd:COG3206 372 QRL 374
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1187-1231 |
1.62e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 1187 CNCHLLGSEMAQCDRSTGACECKEGAAGKHCDECARGFTGD-FPKC 1231
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-515 |
1.76e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.05 E-value: 1.76e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 464 PCNCDPRGIImmGAPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSNDLAGCR 515
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1513-1832 |
1.97e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 63.31 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1513 LNAAKEELQSVAKKLQDIasLTQDVKNQAMNTLKKAQKKKDHFENNNK-KLKDFIKkirdflteegadpESIEKVAQQVL 1591
Cdd:PTZ00440 935 LNNLNKEKEKIEKQLSDT--KINNLKMQIEKTLEYYDKSKENINGNDGtHLEKLDK-------------EKDEWEHFKSE 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1592 SITLPVNKTALDQmvmqikdslsnltNVEGIVNQtsQHISIAkELLDKAKDAKSraegvKDSANNTKQALDMSEKAieKA 1671
Cdd:PTZ00440 1000 IDKLNVNYNILNK-------------KIDDLIKK--QHDDII-ELIDKLIKEKG-----KEIEEKVDQYISLLEKM--KT 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1672 RAALKEANNNLNSTRNATVEvdERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMA-KDAIAQANNATQVASSLEQ 1750
Cdd:PTZ00440 1057 KLSSFHFNIDIKKYKNPKIK--EEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdKEKNKQTEHYNKKKKSLEK 1134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1751 SLNDTENRYQELqmkvDSLGGESGGLNSINQ------------KAQDIKNEAEdllsKATKGIDQLKKLEKKFKSNEQRM 1818
Cdd:PTZ00440 1135 IYKQMEKTLKEL----ENMNLEDITLNEVNEieieyerilidhIVEQINNEAK----KSKTIMEEIESYKKDIDQVKKNM 1206
|
330
....*....|....*
gi 1848696099 1819 QKQRME-LDELKENA 1832
Cdd:PTZ00440 1207 SKERNDhLTTFEYNA 1221
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1781-1849 |
2.38e-09 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 55.56 E-value: 2.38e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1781 QKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENatlVRDVIREQVQK---YSNC 1849
Cdd:cd22300 4 KKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEE---VRSLLQEISQKvavYSTC 72
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
465-519 |
3.27e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 54.28 E-value: 3.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1848696099 465 CNCDPRGIImmGAPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSNDLagcrPCDC 519
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1139-1180 |
5.05e-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: 53.51 E-value: 5.05e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1848696099 1139 CGCDPQHALGTHCNMFTGQCQCRPGFGGKQCTECEQFHWGDP 1180
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1139-1184 |
7.33e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 7.33e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 1139 CGCDPQHALGTHCNMFTGQCQCRPGFGGKQCTECEQFHWGDPRLQC 1184
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1657-1848 |
1.14e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1657 TKQALDMSEKAIEKARAALKEANNNLNSTRNatvEVDERLTQLEdkqmdvmmrlnNLSREVEALRNKTEQNRQMAKDAIA 1736
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLRE---ELEQAREELE-----------QLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1737 QANNATQVASSLEQSLNDTENRYQELQmkvdslggesgglnsinQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQ 1816
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQ-----------------EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150
|
170 180 190
....*....|....*....|....*....|..
gi 1848696099 1817 RMQKQRMELDELKENATLVRDVIREQVQKYSN 1848
Cdd:COG4372 151 ELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1275-1848 |
1.36e-08 |
|
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: 60.13 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1275 RIKELERKLKgvqdlismeDSNRIHQ----LIGQSIDDLRAeialtdgRLMGVTRELNTTAD----EEEALRHILSVLEK 1346
Cdd:pfam15921 86 QVKDLQRRLN---------ESNELHEkqkfYLRQSVIDLQT-------KLQEMQMERDAMADirrrESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1347 ELTHINATVAHKQRLLDNYLTsgfadQFEKVKKFYQesakAEEKCNASVSGPLSPVEQSKETRAVTEDLLdaSKVKFLRA 1426
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNT-----QIEQLRKMML----SHEGVLQEIRSILVDFEEASGKKIYEHDSM--STMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1427 LAAQNKSLSELQQKAHDLDKKVHHLSHKVCGGHSNASVNGSCPDSQcggagcHDDQGNHVCGGHGCNGTVSTSVAAlnHA 1506
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ------HQDRIEQLISEHEVEITGLTEKAS--SA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1507 RNATDSLNAAKEELQSVAK--------KLQDIASLTQDVKNQ---------------------AMNTLKKAQKKKDHFEN 1557
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARnqnsmymrQLSDLESTVSQLRSElreakrmyedkieelekqlvlANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1558 NNKKLKDFIKKIRDFLTEEGADpESIEKVAQQVL-------SITLPVNKTALDQMVMQIKdSLSNL-----TNVEGIVNQ 1625
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKE-LSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQ-RLEALlkamkSECQGQMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1626 TSQHISIAKELLDKAKDAKSRAEGVKDSANNT-------KQALDMSEKAIEKARAALKEANNNLNSTrnatvevDERLTQ 1698
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVveeltakKMTLESSERTVSDLTASLQEKERAIEAT-------NAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1699 LEDKQMDVMMRLNNLSREVEALRN-KTEQNR---QMA-KDAI-----AQANNATQVA--------------SSLEQSLND 1754
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNvQTECEAlklQMAeKDKVieilrQQIENMTQLVgqhgrtagamqvekAQLEKEIND 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1755 TENRYQELQMKVDSlggESGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATL 1834
Cdd:pfam15921 602 RRLELQEFKILKDK---KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
650
....*....|....*..
gi 1848696099 1835 VRDVIR---EQVQKYSN 1848
Cdd:pfam15921 679 LKRNFRnksEEMETTTN 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1494-1786 |
1.86e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1494 GTVSTSVAALNHARNATDSLNAAKEELQSVAKKL----QDIASLTQDVkNQAMNTLKKAQKKKDHFENNNKKLKDFIKKI 1569
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELdalqAELEELNEEY-NELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1570 RDFLTEEGAdpesiekvAQQVLSITLpvnkTALDQMVMQ--IKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRA 1647
Cdd:COG3883 85 REELGERAR--------ALYRSGGSV----SYLDVLLGSesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1648 EGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQN 1727
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1728 RQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDI 1786
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGG 291
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1538-1808 |
2.80e-08 |
|
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: 58.82 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1538 KNQAMNTLKKAqkkkdhFENNNKKLKDFIKKIRDFL-TEEG----ADPESIEKVAQQVLSITlpvnkTALDQMVMQIKDS 1612
Cdd:COG5185 280 LNENANNLIKQ------FENTKEKIAEYTKSIDIKKaTESLeeqlAAAEAEQELEESKRETE-----TGIQNLTAEIEQG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1613 LSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSraegVKDSANNTKQALDMsekaiekARAALKEANNNLNSTRNATVEV 1692
Cdd:COG5185 349 QESLTENLEAIKEEIENIVGEVELSKSSEELDS----FKDTIESTKESLDE-------IPQNQRGYAQEILATLEDTLKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1693 DERltqledkqmdvmmRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSlnDTENRYQELQMKVDSLGGE 1772
Cdd:COG5185 418 ADR-------------QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS--RLEEAYDEINRSVRSKKED 482
|
250 260 270
....*....|....*....|....*....|....*..
gi 1848696099 1773 SGG-LNSINQKAQDIKNEAEDLLSKATKGIDQLKKLE 1808
Cdd:COG5185 483 LNEeLTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1599-1843 |
4.47e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1599 KTALDQMVMQI-----KDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARA 1673
Cdd:PRK02224 186 RGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1674 ALKEANNNLNSTRNATVEVDERLTQLEDKQMD--------------VMMRLNNLSREVEALRNKTEQNRQMAKDAIAQAN 1739
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDllaeaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1740 NATQVASSLEQslndtenRYQELQmkvdslggesgglnsinQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQ 1819
Cdd:PRK02224 346 SLREDADDLEE-------RAEELR-----------------EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
250 260
....*....|....*....|....*..
gi 1848696099 1820 K---QRMELDELKENATLVRDVIREQV 1843
Cdd:PRK02224 402 DapvDLGNAEDFLEELREERDELRERE 428
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1030-1081 |
6.45e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 6.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1848696099 1030 PCECNGNIDTkdPGSCDPRTGQCLnCLYHTDGPSCGHCQHGYYGNAL-AHDCR 1081
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
516-555 |
7.62e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.43 E-value: 7.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1848696099 516 PCDCDFGGAYNNRCMMESGQCDCRRHLIGRQCSEVQPGYF 555
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
404-463 |
8.57e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 8.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 404 ACDCDPVGSmEGGVCDSHTdldvgmisGQCRCKANVKGTRCDDCKESYYGLSQNdPLGCQ 463
Cdd:cd00055 1 PCDCNGHGS-LSGQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
517-555 |
9.35e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.35e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1848696099 517 CDCDFGGAYNNRCMMESGQCDCRRHLIGRQCSEVQPGYF 555
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1547-1832 |
1.24e-07 |
|
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: 56.90 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1547 KAQKKKDHFENNNKKLKDFIKKIRDFLteeGADPESIEKVaqqvlsITLPVNKTA--LDQMVMQIKDSLSNLTNVEGIVN 1624
Cdd:TIGR00618 110 YLEQKKGRGRILAAKKSETEEVIHDLL---KLDYKTFTRV------VLLPQGEFAqfLKAKSKEKKELLMNLFPLDQYTQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1625 QTSQHISIAKELLDKAKDAKSRAEGVKDSAN-------NTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLT 1697
Cdd:TIGR00618 181 LALMEFAKKKSLHGKAELLTLRSQLLTLCTPcmpdtyhERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1698 QLEDKQMDVmMRLNNLSREVEALRNKTEQNRQMAK-----DAIAQANnatQVASSLEQSLNDTEN-------RYQELQMK 1765
Cdd:TIGR00618 261 LLKQLRARI-EELRAQEAVLEETQERINRARKAAPlaahiKAVTQIE---QQAQRIHTELQSKMRsrakllmKRAAHVKQ 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848696099 1766 VDSLGGESGGLNSINQKAQDIKNEAE------DLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENA 1832
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEvatsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1031-1075 |
1.25e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.25e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1848696099 1031 CECNGNIDTkdPGSCDPRTGQCLnCLYHTDGPSCGHCQHGYYGNA 1075
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1101-1136 |
1.26e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.26e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1848696099 1101 HCDRQTGACPCRQNVAGHNCDQCAPNHWNYGQDQGC 1136
Cdd:pfam00053 12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1501-1837 |
1.64e-07 |
|
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: 56.52 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1501 AALNHARNATDSLNAAKEELQSVAKKLQDIASLTQDVKnQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRdfLTEEGADP 1580
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK-QLRARIEELRAQEAVLEETQERINRARKAAP--LAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1581 ESIEKVAQQVLSiTLPVNKTALDQMVMQ----IKDSLSNLTNVEGIVNQTSQHISIAKElldkAKDAKSRAEgVKDSANN 1656
Cdd:TIGR00618 303 TQIEQQAQRIHT-ELQSKMRSRAKLLMKraahVKQQSSIEEQRRLLQTLHSQEIHIRDA----HEVATSIRE-ISCQQHT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1657 TKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDvmmrLNNLSREVEALRNKTEQNR-------Q 1729
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRYAELCAaaitctaQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1730 MAKDAIAQANNATQVASSLEQSLNDTEN--------------RYQELQMKVDSLggeSGGLNSINQKAQDIkNEAEDLLS 1795
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrkkavvlaRLLELQEEPCPL---CGSCIHPNPARQDI-DNPGPLTR 528
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1848696099 1796 KATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRD 1837
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1546-1830 |
1.82e-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: 56.60 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1546 KKAQKKKDHFENNNKKLKDFIKKIRDFLteegadpESIEKVAQQV------------LSITLPVN-----KTALDQMVMQ 1608
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQL-------KSLERQAEKAerykelkaelreLELALLVLrleelREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1609 IKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTKQALdmsEKAIEKARAALKEANNNLnstrna 1688
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLANLERQL------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1689 tVEVDERLTQLEDKqmdvmmrLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDS 1768
Cdd:TIGR02168 319 -EELEAQLEELESK-------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1769 LGGEsggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKsnEQRMQKQRMELDELKE 1830
Cdd:TIGR02168 391 LELQ---IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEE 447
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1534-1846 |
1.82e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1534 TQDVKNQAMntLKKAQKKKDHFENNNKKLKD----FIKKIRDF--LTEEgadpesIEKVAQQVLSIT--LPVNKTALDQM 1605
Cdd:TIGR04523 30 KQDTEEKQL--EKKLKTIKNELKNKEKELKNldknLNKDEEKInnSNNK------IKILEQQIKDLNdkLKKNKDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1606 VmqikdslSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRaegvkdsaNNTKQALDMSEkaIEKARAALKEANNNLNST 1685
Cdd:TIGR04523 102 N-------SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKE--------NKKNIDKFLTE--IKKKEKELEKLNNKYNDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1686 RNATVEVDERLTQLEDKQMDVMMRLNNLSREvealRNKTEQNRQMAKDAIaQANNatqvasSLEQSLNDTENRYQELQmk 1765
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNK----LLKLELLLSNLKKKI-QKNK------SLESQISELKKQNNQLK-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1766 vdslggesgglNSINQKAQDIkNEAEDLLSKATKGIDQLKklEKKFKSNEQRMQKQRmeldELKENATLVRDvIREQVQK 1845
Cdd:TIGR04523 232 -----------DNIEKKQQEI-NEKTTEISNTQTQLNQLK--DEQNKIKKQLSEKQK----ELEQNNKKIKE-LEKQLNQ 292
|
.
gi 1848696099 1846 Y 1846
Cdd:TIGR04523 293 L 293
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1513-1830 |
2.42e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1513 LNAAKEELQSVAKKLQDIASLTQDVKNQAMN---TLKKAQKKKDHFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQ 1589
Cdd:PRK01156 334 LQKDYNDYIKKKSRYDDLNNQILELEGYEMDynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1590 VLS---------ITLPVNKTALDQMVMQIKDSLSNLT---------------NVEGIVNQTSQ----------HISI-AK 1634
Cdd:PRK01156 414 INVklqdisskvSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeKSNHIINHYNEkksrleekirEIEIeVK 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1635 ELLDKAKDAKSRAEGVkdsANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATV---EVDER-----LTQLEDKQMDV 1706
Cdd:PRK01156 494 DIDEKIVDLKKRKEYL---ESEEINKSINEYNKIESARADLEDIKIKINELKDKHDkyeEIKNRykslkLEDLDSKRTSW 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1707 MMRLNNLSR-EVEALRNKTEQNRQMAKDAIAQAN----NATQVAS-------SLEQSLNDTENRYQE----------LQM 1764
Cdd:PRK01156 571 LNALAVISLiDIETNRSRSNEIKKQLNDLESRLQeieiGFPDDKSyidksirEIENEANNLNNKYNEiqenkiliekLRG 650
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1848696099 1765 KVDSLGGESGGLNSINQKAQDIK---NEAEDLLSKATKGIDQLK----KLEKKFKSNEQRMQKQRMELDELKE 1830
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPDLKEITsriNDIEDNLKKSRKALDDAKanraRLESTIEILRTRINELSDRINDINE 723
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1517-1841 |
2.45e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.21 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1517 KEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDH-----------FENNNKKLKDFIKKIRDFLTEEGADPESIEK 1585
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgrqsiIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1586 VAQQVLSIT--------LPVNKTALDQMVMQIKDslsnltNVEGIVNQTSQHISIakELLDKAKDAKSRAEGVKDSANNT 1657
Cdd:TIGR00606 770 QETLLGTIMpeeesakvCLTDVTIMERFQMELKD------VERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTV 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1658 KQALDMSEKAIE---KARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDa 1734
Cdd:TIGR00606 842 VSKIELNRKLIQdqqEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK- 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1735 iAQANNATQVaSSLEQSLNDTENRYQELQMKVDSLGGESGGL-NSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFks 1813
Cdd:TIGR00606 921 -DQQEKEELI-SSKETSNKKAQDKVNDIKEKVKNIHGYMKDIeNKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-- 996
|
330 340 350
....*....|....*....|....*....|....*..
gi 1848696099 1814 nEQRMQKQRMELDE-------LKENATL--VRDVIRE 1841
Cdd:TIGR00606 997 -NEDMRLMRQDIDTqkiqerwLQDNLTLrkRENELKE 1032
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
921-966 |
2.70e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 2.70e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1848696099 921 PCQCNSHADI---CDPRNGECRdCRDYTTGHLCDSCADGFFGNPVLGSG 966
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1518-1844 |
2.90e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1518 EELQSVAKKLQD-IASLTQDVKNqaMNTLK-KAQKKKDHFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVLSITL 1595
Cdd:PRK01156 162 NSLERNYDKLKDvIDMLRAEISN--IDYLEeKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1596 PVNK-TALDQMV----MQIKDSLSNLTNVEGIVNQTSqhiSIAKELLDKAKDA--KSRAE-----GVKDSANNTKQALDM 1663
Cdd:PRK01156 240 ALNElSSLEDMKnryeSEIKTAESDLSMELEKNNYYK---ELEERHMKIINDPvyKNRNYindyfKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1664 SEKAIEKARAALKEAnNNLNSTRNATVEVDERLTQLeDKQMDVM----MRLNNLSREVEALRNKTEQNRQMAKDAIAQAN 1739
Cdd:PRK01156 317 IDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDL-NNQILELegyeMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1740 NATQVASSLEQSLNdteNRYQELQMKVDSLGGESGGLN----SINQKAQDIKNEAEDL-------LSKATKGIDQLKKLE 1808
Cdd:PRK01156 395 EILKIQEIDPDAIK---KELNEINVKLQDISSKVSSLNqrirALRENLDELSRNMEMLngqsvcpVCGTTLGEEKSNHII 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 1848696099 1809 KKFKSNEQRMQKqrmELDELKENATLVRDVIREQVQ 1844
Cdd:PRK01156 472 NHYNEKKSRLEE---KIREIEIEVKDIDEKIVDLKK 504
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
465-508 |
3.12e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1848696099 465 CNCDPRGIImmGAPCDQISGDCSCKRYVTGRYCNQCLPEYWGLS 508
Cdd:smart00180 1 CDCDPGGSA--SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1508-1848 |
4.96e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.06 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1508 NATDSLNAAKEELQ---SVAKKLQDIASLTQDVKNQAMNTLKKaQKKKDHFENNNKKLKDFikkirDFlteEGADPESIE 1584
Cdd:TIGR01612 2188 DISDSLNDDIDALQikyNLNQTKKHMISILADATKDHNNLIEK-EKEATKIINNLTELFTI-----DF---NNADADILH 2258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1585 KVAQQVLSITLPVNKT--ALDQMVMQIKD-SLSNLTNVEGivnqtsQHISIAKELLDKAKDAKSRaegVKDSANNTKQal 1661
Cdd:TIGR01612 2259 NNKIQIIYFNSELHKSieSIKKLYKKINAfKLLNISHINE------KYFDISKEFDNIIQLQKHK---LTENLNDLKE-- 2327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1662 dMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEdKQMDVMMRLNNLSRE--------VEALRNKT--------- 1724
Cdd:TIGR01612 2328 -IDQYISDKKNIFLHALNENTNFNFNALKEIYDDIINRE-NKADEIENINNKENEnimqyidtITKLTEKIqdilifvtt 2405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1725 -EQNRQMAKDAIaQANNATQVaSSLEQSLNDTENRYQELQMKVDSLGGESGGLNSIN-------QKAQDIKNeaedLLSK 1796
Cdd:TIGR01612 2406 yENDNNIIKQHI-QDNDENDV-SKIKDNLKKTIQSFQEILNKIDEIKAQFYGGNNINniiitisQNANDVKN----HFSK 2479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1797 ATKGIDQLKKLEKKFKSNEQRMQKQRMEldELKENATLVRDVIREQVQKYSN 1848
Cdd:TIGR01612 2480 DLTIENELIQIQKRLEDIKNAAHEIRSE--QITKYTNAIHNHIEEQFKKIEN 2529
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
971-1026 |
5.00e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 5.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 971 PCPCPGNpGSDHfnaHSCHADHtsnqIICNCREGYTGLRCDQCAPGYYGNPEQYGG 1026
Cdd:cd00055 1 PCDCNGH-GSLS---GQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1666-1848 |
5.83e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1666 KAIEKARAALkeaNNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQnrqmAKDAIAQANNATQva 1745
Cdd:COG4372 6 EKVGKARLSL---FGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1746 sSLEQSLNDTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMEL 1825
Cdd:COG4372 77 -QLEEELEELNEQLQAAQAELAQAQEE---LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180
....*....|....*....|...
gi 1848696099 1826 DELKENATLVRDVIREQVQKYSN 1848
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQA 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1540-1817 |
5.86e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1540 QAMNTLKKAQKKKDhfennnkklkdfIKKIRDFLTEEGADPESIEKVAQQVLSitlpvNKTALDQM---VMQIKDSLSNL 1616
Cdd:COG4913 192 KALRLLHKTQSFKP------------IGDLDDFVREYMLEEPDTFEAADALVE-----HFDDLERAheaLEDAREQIELL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1617 tnvEGIVNQTSQHISiAKELLDKAKDAKSRAEGVKDSanntkQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERL 1696
Cdd:COG4913 255 ---EPIRELAERYAA-ARERLAELEYLRAALRLWFAQ-----RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1697 TQLEDKqmdvmmRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLggesggL 1776
Cdd:COG4913 326 DELEAQ------IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL------L 393
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1848696099 1777 NSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQR 1817
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1246-1845 |
6.95e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1246 CQIKRDLEHIQYTAQKI------LESGVMpgvgdtRIKELERKLKGVQDLIS------MEDSNRIHQLIGQSIDDLRAEI 1313
Cdd:pfam12128 230 IQAIAGIMKIRPEFTKLqqefntLESAEL------RLSHLHFGYKSDETLIAsrqeerQETSAELNQLLRTLDDQWKEKR 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1314 ALTDGRLmgvtrelnTTADEE-EALRHILSVLEKEL---THINATVAH-KQRLLDNYLT---------SGFADQFEKVKK 1379
Cdd:pfam12128 304 DELNGEL--------SAADAAvAKDRSELEALEDQHgafLDADIETAAaDQEQLPSWQSelenleerlKALTGKHQDVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1380 FYQE-SAKAEEKCNASVSGPLSPVEQSKETR----AVTEDLLDASKVKFLRALAAQNKSLSELQqkahdldkkvhhLSHK 1454
Cdd:pfam12128 376 KYNRrRSKIKEQNNRDIAGIKDKLAKIREARdrqlAVAEDDLQALESELREQLEAGKLEFNEEE------------YRLK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1455 VCGGHSNASVNGSCPDSQCggagcHDDQGNhvcgghgcngtvstSVAALNHARNATDSLNAAKEELQS---VAKKLQDIA 1531
Cdd:pfam12128 444 SRLGELKLRLNQATATPEL-----LLQLEN--------------FDERIERAREEQEAANAEVERLQSelrQARKRRDQA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1532 SLTQDVKNQAMNTLKKAQKKKDHfennnkKLKDFIKKIRDFLTEEGAD-PESIEKVAQQVLsitlpVNKTALDQMVmqIK 1610
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELEL------QLFPQAGTLLHFLRKEAPDwEQSIGKVISPEL-----LHRTDLDPEV--WD 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1611 DSLSNLTNVEGI--------VNQTSQHISIAKELLDKAK----DAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEA 1678
Cdd:pfam12128 572 GSVGGELNLYGVkldlkridVPEWAASEEELRERLDKAEealqSAREKQAAAEEQLVQANGELEKASREETFARTALKNA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1679 NNNL----NSTRNATVEVDErltQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVA-SSLEQSLN 1753
Cdd:pfam12128 652 RLDLrrlfDEKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwQVVEGALD 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1754 DTENRY-QELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIdqlKKLEKKFKSNEQRMQKQRMELDELKENA 1832
Cdd:pfam12128 729 AQLALLkAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI---RTLERKIERIAVRRQEVLRYFDWYQETW 805
|
650
....*....|...
gi 1848696099 1833 TLVRDVIREQVQK 1845
Cdd:pfam12128 806 LQRRPRLATQLSN 818
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
405-458 |
7.05e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.05e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 405 CDCDPVGSmEGGVCDSHTdldvgmisGQCRCKANVKGTRCDDCKESYYGLSQND 458
Cdd:smart00180 1 CDCDPGGS-ASGTCDPDT--------GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1781-1849 |
7.19e-07 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 48.21 E-value: 7.19e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1781 QKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTC 70
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
922-969 |
8.37e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 47.35 E-value: 8.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1848696099 922 CQCNSHA---DICDPRNGECrDCRDYTTGHLCDSCADGFFGNPVlGSGDHC 969
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1652-1827 |
9.79e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1652 DSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNK-TEQNRQM 1730
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1731 AK------------------DAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAED 1792
Cdd:COG3883 96 YRsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1848696099 1793 LLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDE 1827
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1516-1842 |
1.05e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1516 AKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFEnnnKKLKDFIKKIRDFLTEEGADPESIEKVAQQVLSITl 1595
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ---LKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1596 pVNKTALDQMVMQ-----IKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTKQAldmSEKAIEK 1670
Cdd:pfam02463 250 -QEEIESSKQEIEkeeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE---SEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1671 ARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQ 1750
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1751 SLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDI--------KNEAEDLLSKATKGIDQLKKLEKKFKsnEQRMQKQR 1822
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELkqgklteeKEELEKQELKLLKDELELKKSEDLLK--ETQLVKLQ 483
|
330 340
....*....|....*....|
gi 1848696099 1823 MELDELKENATLVRDVIREQ 1842
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKES 503
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1503-1848 |
1.07e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 53.70 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1503 LNHARNATDS--LNAAKEELQSVAKKLQDIASLTQDVkNQAMNTLKKAQKK--------KDHFEN-------NN------ 1559
Cdd:pfam06160 69 LFEAEELNDKyrFKKAKKALDEIEELLDDIEEDIKQI-LEELDELLESEEKnreeveelKDKYRElrktllaNRfsygpa 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1560 -----KKLKDFIKKIRDF--LTEEGaDPESIEKVAQQVLSITlpvnkTALDQMVMQIKDSLSNLTNVegIVNQTSQHISI 1632
Cdd:pfam06160 148 ideleKQLAEIEEEFSQFeeLTESG-DYLEAREVLEKLEEET-----DALEELMEDIPPLYEELKTE--LPDQLEELKEG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1633 AKELLDkakdaksraEGVKDSANNTKQALDMSEKAIEKARAALKeaNNNLNSTRNATVEVDERLTQLEDKqmdvmmrlnn 1712
Cdd:pfam06160 220 YREMEE---------EGYALEHLNVDKEIQQLEEQLEENLALLE--NLELDEAEEALEEIEERIDQLYDL---------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1713 LSREVEAlRNKTEQNRqmakdaiaqannatqvaSSLEQSLNDTENRYQELQMKVDSLGgESGGLNsinqkaqdiKNEAED 1792
Cdd:pfam06160 279 LEKEVDA-KKYVEKNL-----------------PEIEDYLEHAEEQNKELKEELERVQ-QSYTLN---------ENELER 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1848696099 1793 llskaTKGID-QLKKLEKKFKSNEQRMQKQRM---EL-DELKENATLVrDVIREQVQKYSN 1848
Cdd:pfam06160 331 -----VRGLEkQLEELEKRYDEIVERLEEKEVaysELqEELEEILEQL-EEIEEEQEEFKE 385
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1493-1753 |
1.45e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1493 NGTVSTSVAALNHARNATDSlnaaKEELQSVAKKLQDIASLTQDVK------NQAMNTLKKAQKKKDHFENNNKKLKDFI 1566
Cdd:PRK11281 18 LLLCLSSAFARAASNGDLPT----EADVQAQLDALNKQKLLEAEDKlvqqdlEQTLALLDKIDRQKEETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1567 KKIRDFLTEEGADPESIEKVAQQVLSiTLPVnkTALDQMVMQIKDSLSNLTNVEGIVNqtSQHISiAKELLDKAKDAKSR 1646
Cdd:PRK11281 94 AKLRQAQAELEALKDDNDEETRETLS-TLSL--RQLESRLAQTLDQLQNAQNDLAEYN--SQLVS-LQTQPERAQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1647 AEGVKDSANNTKQALDMSEKAIEKARAALKEAN----NNLNSTRNATVEVDERLTQLEDKQMD-VMMRLNNLSREVEALR 1721
Cdd:PRK11281 168 NSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEqallNAQNDLQRKSLEGNTQLQDLLQKQRDyLTARIQRLEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1848696099 1722 N-----KTEQNRQMAKDAIAQANNATQVASSL---EQSLN 1753
Cdd:PRK11281 248 EainskRLTLSEKTVQEAQSQDEAARIQANPLvaqELEIN 287
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1137 |
1.46e-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: 1.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 1083 CTCVTAGTIHSacsdgqcHCDRQTGACPCRQNVAGHNCDQCAPNHWNY-GQDQGCE 1137
Cdd:cd00055 2 CDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1518-1815 |
1.65e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1518 EELQSVAKKLQDIASLTQDVKN------QAMNTLKK----------AQKKKDHFENNNKKLKDFIKKIRDFLTEEgadpE 1581
Cdd:TIGR01612 883 DKLNDYEKKFNDSKSLINEINKsieeeyQNINTLKKvdeyikicenTKESIEKFHNKQNILKEILNKNIDTIKES----N 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1582 SIEKVAQQVLSITLPVNKTALDQMVMQIkdslsNLTNVEGIVNQTSQHISIAKELLDKAKDaksraegvkdsaNNTKQAL 1661
Cdd:TIGR01612 959 LIEKSYKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKE------------NMLYHQF 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1662 DMSEKAIEKARAALKEANNNLNSTrnatvevderltqledkQMDVMMRLNNLSREVEAL--RNKTEQNRQMAKDAIAQAN 1739
Cdd:TIGR01612 1022 DEKEKATNDIEQKIEDANKNIPNI-----------------EIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINIT 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1740 NATQVASSLEqsLNDTENRYQELQMK-VDSLGGESGGLNSINQKA-------QDIKNEAEDLLSKATKGIDQLKKLEKKF 1811
Cdd:TIGR01612 1085 NFNEIKEKLK--HYNFDDFGKEENIKyADEINKIKDDIKNLDQKIdhhikalEEIKKKSENYIDEIKAQINDLEDVADKA 1162
|
....
gi 1848696099 1812 KSNE 1815
Cdd:TIGR01612 1163 ISND 1166
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-330 |
1.69e-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: 46.58 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1848696099 277 SCFCYGHAS---ECAPVpgvdarengmiHGRCVCKHNTEGLNCERCRHFHNDLPWRP 330
Cdd:cd00055 1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1635-1809 |
2.09e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1635 ELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVM-MR-LNN 1712
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKeYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1713 LSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQmkvdslggesgglNSINQKAQDIKNEAED 1792
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK-------------AELDEELAELEAELEE 160
|
170 180
....*....|....*....|..
gi 1848696099 1793 LLSK---ATKGIDQ--LKKLEK 1809
Cdd:COG1579 161 LEAEreeLAAKIPPelLALYER 182
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1083-1136 |
2.31e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 2.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 1083 CTCVTAGTIHSacsdgqcHCDRQTGACPCRQNVAGHNCDQCAPNHWNYgQDQGC 1136
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
342-398 |
2.54e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.19 E-value: 2.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 342 CNCNGHSS---HCHFdmavylatgniSGGVCDdCQHNTMGRNCEMCKPFYYQDPNRDVRD 398
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1579-1848 |
2.61e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1579 DPESIEKVAQQVLSI---------------TLPVNKTALDQMVM---QIKDSLSN----LTNVEGIVNQTSQHISIAKEL 1636
Cdd:PRK03918 143 SDESREKVVRQILGLddyenayknlgevikEIKRRIERLEKFIKrteNIEELIKEkekeLEEVLREINEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1637 LDKAKDAKSRAEGVKDSANNtkqaLDMSEKAIEKARAALKEANNNLNSTRNatvEVDERLTQLEDKQmdvmmrlnnlsRE 1716
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIE---ELKKEIEELEEKV-----------KE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1717 VEALRNKTEQNRQMAKdaiaQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDL--- 1793
Cdd:PRK03918 285 LKELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeer 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1848696099 1794 ---LSKATKGIDQLKKLEKKFKSNEqrMQKQRMELDELKENATLVRDVIREQVQKYSN 1848
Cdd:PRK03918 361 helYEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1633-1832 |
2.92e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 50.38 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1633 AKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAA-------------LKEANNNLNSTRNATVEVDERLTQL 1699
Cdd:pfam12795 25 ALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKaeaapkeilaslsLEELEQRLLQTSAQLQELQNQLAQL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1700 EDkqmdvmmRLNNLSREVEALRNKTEQNRQmAKDAIAQANNATQVASSL-----------EQSLNDTENRYQELQmkvds 1768
Cdd:pfam12795 105 NS-------QLIELQTRPERAQQQLSEARQ-RLQQIRNRLNGPAPPGEPlseaqrwalqaELAALKAQIDMLEQE----- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1769 lggesggLNSINQKaQDIKNEAEDLLSKatkgidQLKKLEKKFKS-----NEQRMQ---KQRMELDELKENA 1832
Cdd:pfam12795 172 -------LLSNNNR-QDLLKARRDLLTL------RIQRLEQQLQAlqellNEKRLQeaeQAVAQTEQLAEEA 229
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1275-1791 |
3.17e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1275 RIKELERKLK----GVQDLISMEDSNRIHQLIGQSIDDLRAEIALTDGRLMGVTRELNttadeeeALRHILSVLEKELTH 1350
Cdd:PRK03918 267 RIEELKKEIEeleeKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN-------GIEERIKELEEKEER 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1351 INATVAHKQRLLDNYLT-SGFADQFE--KVKKFYQESAKAEEKCNA--SVSGPLSPVEQSKETraVTEDLldaSKVKflr 1425
Cdd:PRK03918 340 LEELKKKLKELEKRLEElEERHELYEeaKAKKEELERLKKRLTGLTpeKLEKELEELEKAKEE--IEEEI---SKIT--- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1426 alaaqnKSLSELQQKAHDLDKKVHHLShkvcgghsnaSVNGSCPdsqcggagchddqgnhVCGghgcngtvstsvaalnh 1505
Cdd:PRK03918 412 ------ARIGELKKEIKELKKAIEELK----------KAKGKCP----------------VCG----------------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1506 aRNATDS-----LNAAKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFENnnKKLKDFIKKIRDFLTEEG--- 1577
Cdd:PRK03918 443 -RELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL--KELAEQLKELEEKLKKYNlee 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1578 --ADPESIEKVAQQVLSIT---------------LPVNKTALDQMVMQIKDSLSNLTN---------VEGIVNQTSQHIS 1631
Cdd:PRK03918 520 leKKAEEYEKLKEKLIKLKgeikslkkelekleeLKKKLAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEP 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1632 IAKELLdKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEvdERLTQLEDKQMDvmmrln 1711
Cdd:PRK03918 600 FYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLE------ 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1712 nLSREVEALRNKTEQNRQMAKdaiaqannatQVASSLEQSLNDTENRyQELQMKVDSLGGESGGLNSINQKAQDIKNEAE 1791
Cdd:PRK03918 671 -LSRELAGLRAELEELEKRRE----------EIKKTLEKLKEELEER-EKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1508-1828 |
3.39e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1508 NATDSLNAAKEELQSVAKKLQDIASLTQDVKNqamntLKKAQKKKdhFEnnnKKLKDfIKKIRDFLTEEGADPESIEKVA 1587
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEE-----LIKEKEKE--LE---EVLRE-INEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1588 QQVLSItlpvnKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHIsiaKELLDKAKDAKSRAEGVKDSANNTKQALDMSEkA 1667
Cdd:PRK03918 231 KELEEL-----KEEIEELEKELESLEGSKRKLEEKIRELEERI---EELKKEIEELEEKVKELKELKEKAEEYIKLSE-F 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1668 IEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQmdvmMRLNNLSREVEALRNKTE------QNRQMAKDAIAQANN- 1740
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEeleerhELYEEAKAKKEELERl 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1741 ----ATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSIN----------QKAQDI---------KNEAEDLLSKA 1797
Cdd:PRK03918 378 kkrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIkelkkaieelKKAKGKcpvcgreltEEHRKELLEEY 457
|
330 340 350
....*....|....*....|....*....|.
gi 1848696099 1798 TKgidQLKKLEKKFKSNEQRMQKQRMELDEL 1828
Cdd:PRK03918 458 TA---ELKRIEKELKEIEEKERKLRKELREL 485
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
972-1028 |
3.40e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 3.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1848696099 972 CPCPGNpGSDHfnaHSCHadhtSNQIICNCREGYTGLRCDQCAPGYYGNPEQYGGQC 1028
Cdd:pfam00053 1 CDCNPH-GSLS---DTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1639-1836 |
3.41e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1639 KAKDAKsRAEGVKDSANNTKQAldmsekaiEKARAALKEANN----NLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLS 1714
Cdd:PTZ00121 1219 KAEDAK-KAEAVKKAEEAKKDA--------EEAKKAEEERNNeeirKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1715 REVEALRnKTEQNRQmAKDAIAQANNATQVassleqslNDTENRYQELQMKVDSLggesgglnsiNQKAQDIKNEAEDLL 1794
Cdd:PTZ00121 1290 KKADEAK-KAEEKKK-ADEAKKKAEEAKKA--------DEAKKKAEEAKKKADAA----------KKKAEEAKKAAEAAK 1349
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1848696099 1795 SKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVR 1836
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1513-1847 |
3.88e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1513 LNAAKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVls 1592
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1593 itlpvnkTALDQMVMQIKDSLSNLTnvEGIVNQTSQhisiAKELLDKAKDAKSRAEGVKDSANNTKQAldmseKAIEKAR 1672
Cdd:COG4372 125 -------QDLEQQRKQLEAQIAELQ--SEIAEREEE----LKELEEQLESLQEELAALEQELQALSEA-----EAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1673 AALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLN--NLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQ 1750
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDslEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1751 SLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLskaTKGIDQLKKLEKKFKSNEQRMQKQRMELDELKE 1830
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI---GALEDALLAALLELAKKLELALAILLAELADLL 343
|
330
....*....|....*..
gi 1848696099 1831 NATLVRDVIREQVQKYS 1847
Cdd:COG4372 344 QLLLVGLLDNDVLELLS 360
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1507-1842 |
4.61e-06 |
|
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: 51.97 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1507 RNATDSLNAAKEELQSVAKKLQDIASLTQDV--KNQAmntLKKAQKKKDHFENNNkkLKDFIKKIRDFLTEEGAD-PESI 1583
Cdd:TIGR00606 443 ELKKEILEKKQEELKFVIKELQQLEGSSDRIleLDQE---LRKAERELSKAEKNS--LTETLKKEVKSLQNEKADlDRKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1584 EKVAQQVLSitLPVNKTALDQMVMQIKDslsNLTNVEGIVNQTSQHisiAKELLDKAKDAKSRAEgVKDSANNTKQALDM 1663
Cdd:TIGR00606 518 RKLDQEMEQ--LNHHTTTRTQMEMLTKD---KMDKDEQIRKIKSRH---SDELTSLLGYFPNKKQ-LEDWLHSKSKEINQ 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1664 SEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMmRLNNLSREVEALRNKTEQNRqmaKDaIAQANNATQ 1743
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-GSQDEESDLERLKEEIEKSS---KQ-RAMLAGATA 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1744 VASSLEQSLNDtenryqelqmkvdslggESGGLNSINQKaqDIKNEAE------DLLSKATKGIDQLKKLEKKFKSNEQR 1817
Cdd:TIGR00606 664 VYSQFITQLTD-----------------ENQSCCPVCQR--VFQTEAElqefisDLQSKLRLAPDKLKSTESELKKKEKR 724
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1848696099 1818 --------------MQKQRMELDELKE-NATLVRDVIREQ 1842
Cdd:TIGR00606 725 rdemlglapgrqsiIDLKEKEIPELRNkLQKVNRDIQRLK 764
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1631-1846 |
4.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1631 SIAKELLDKAKDAKSRAEGVKDSANNTKQaldmseKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDkqmdvmmRL 1710
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKEL------KELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------EL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1711 NNLSREVEALRnkteqnrqmakdAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEA 1790
Cdd:COG4717 112 EELREELEKLE------------KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1791 EDLLSKATKG--------IDQLKKLEKKFKSNEQRMQKQRMELDELKEN-----ATLVRDVIREQVQKY 1846
Cdd:COG4717 180 EELLEQLSLAteeelqdlAEELEELQQRLAELEEELEEAQEELEELEEEleqleNELEAAALEERLKEA 248
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1782-1849 |
5.34e-06 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 45.90 E-value: 5.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848696099 1782 KAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:cd22299 4 KAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTC 71
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1294-1831 |
6.22e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1294 DSNRIHQLIGQ----SIDDLRAE-IALTDGRlmgvTRELNTTaDEEEALRHILSVLEKELTHINATVAHKQRLLDNYLTS 1368
Cdd:TIGR01612 1284 DDDKDHHIISKkhdeNISDIREKsLKIIEDF----SEESDIN-DIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLN 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1369 GFADQFEKVKKFYQESakaeEKCNASVSGPLSPVEqsKETRAVTEDL-LDASKVKFLRALaaQNKSLSELQQKAHDLdkK 1447
Cdd:TIGR01612 1359 KIKKIIDEVKEYTKEI----EENNKNIKDELDKSE--KLIKKIKDDInLEECKSKIESTL--DDKDIDECIKKIKEL--K 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1448 VHHLSHKVCGG--HSNASVNGSCPDSQCGGAGCHDDQGNHVCGGHGCNGTvSTSVAALNHARNATDSLNAAKEELQSVAK 1525
Cdd:TIGR01612 1429 NHILSEESNIDtyFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNAT-NDHDFNINELKEHIDKSKGCKDEADKNAK 1507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1526 KLQDIASLTQDVKNQAMNTLKK--AQKKKDHFENNNKKLKDFIKKIRD----FLTEEGADPESIEKVAQQVLSITLPV-N 1598
Cdd:TIGR01612 1508 AIEKNKELFEQYKKDVTELLNKysALAIKNKFAKTKKDSEIIIKEIKDahkkFILEAEKSEQKIKEIKKEKFRIEDDAaK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1599 KTALDQMVMQIKDSLSNLTNvegivnqtsQHISIAkELLDKAKDAKSRAEGVKdsanntKQaldMSEKAIEKARAALKEA 1678
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFEN---------KFLKIS-DIKKKINDCLKETESIE------KK---ISSFSIDSQDTELKEN 1648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1679 NNNLNSTRNATVEVDERLTQLEDKQMDvmmrLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVAS-----SLEQSLN 1753
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKKNIEDKKKE----LDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANkeeieSIKELIE 1724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1754 DTENRYQElQMKVDSLGG--ESGGLNSINQKAQDIKNEAEDL----------LSKATKGIDQLKKL----EKKFKSNEQR 1817
Cdd:TIGR01612 1725 PTIENLIS-SFNTNDLEGidPNEKLEEYNTEIGDIYEEFIELyniiagcletVSKEPITYDEIKNTrinaQNEFLKIIEI 1803
|
570
....*....|....
gi 1848696099 1818 MQKQRMELDELKEN 1831
Cdd:TIGR01612 1804 EKKSKSYLDDIEAK 1817
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
342-392 |
6.41e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.04 E-value: 6.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 342 CNCNGHSS---HCHFDmavylatgnisGGVCDdCQHNTMGRNCEMCKPFYYQDP 392
Cdd:cd00055 2 CDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLP 43
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1493-1849 |
6.76e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1493 NGTVSTSVAALNHARNATDSLnaaKEELQSVAKKLQDIASLT------QDVKNQAMNTLKKAQKKKDHFENNNKKLKDfI 1566
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENY---IDEIKAQINDLEDVADKAisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-I 1199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1567 KKIRDflteegaDPESIEKVAQQVLSITLPVNKTALDQ----------MVMQIKDSLSNLTNVE----GIVNQTSQHISI 1632
Cdd:TIGR01612 1200 AEIEK-------DKTSLEEVKGINLSYGKNLGKLFLEKideekkksehMIKAMEAYIEDLDEIKekspEIENEMGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1633 AKEL----LDKAKDAKSRAEgvkdSANNTKQALDMSEKAIEKARAALKEAN---------NNLNSTRNATVEVDERLTQL 1699
Cdd:TIGR01612 1273 KAEMetfnISHDDDKDHHII----SKKHDENISDIREKSLKIIEDFSEESDindikkelqKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1700 EDkqMDVMMRLNNLSR---EVEALRNKTEQNRQMAKDAIAQannatqvASSLEQSLNDTENrYQELQMKVDS-LGGEsgg 1775
Cdd:TIGR01612 1349 AN--IYNILKLNKIKKiidEVKEYTKEIEENNKNIKDELDK-------SEKLIKKIKDDIN-LEECKSKIEStLDDK--- 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1776 lnSINQKAQDIKNEAEDLLSKAT------KGIDQL-KKLEKKFKSNEQRMQKQRMELDELKENATLVRDV----IREQVQ 1844
Cdd:TIGR01612 1416 --DIDECIKKIKELKNHILSEESnidtyfKNADENnENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFnineLKEHID 1493
|
....*
gi 1848696099 1845 KYSNC 1849
Cdd:TIGR01612 1494 KSKGC 1498
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1781-1849 |
7.06e-06 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 45.30 E-value: 7.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1781 QKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKYSNC 1849
Cdd:cd22302 2 ERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
517-555 |
7.25e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 44.65 E-value: 7.25e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1848696099 517 CDCDFGGAYNNRCMMESGQCDCRRHLIGRQCSEVQPGYF 555
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1512-1843 |
9.44e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1512 SLNAAKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVL 1591
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1592 SITlpvnkTALDQMVMQIKDSLSNLTNVEGIVNQtsqhisiAKELLDKAK------------------DAKSRAEGVKDS 1653
Cdd:PRK02224 416 ELR-----EERDELREREAELEATLRTARERVEE-------AEALLEAGKcpecgqpvegsphvetieEDRERVEELEAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1654 ANNTKQALDMSEKAIEKARAaLKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKD 1733
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1734 AIAQANNATQVASSLEQSL--NDTE----NRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIDQlkkL 1807
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLaeLKERieslERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE---L 639
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1848696099 1808 EKKFKSN---EQRMQKQRME---------LDELKENatlvRDVIREQV 1843
Cdd:PRK02224 640 EAEFDEArieEAREDKERAEeyleqveekLDELREE----RDDLQAEI 683
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1511-1797 |
9.59e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.84 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1511 DSLNAAKEELQSVAKKLQDIasltqdvkNQAMNTLKKAQKkkdhfenNNKKLKDFIKKIRDFlteegadPESIEKVAQQv 1590
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDL--------QQALSLLDKIDA-------SKQRAAAYQKALDDA-------PAELRELRQE- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1591 lsitLPVNKTALDQMVMQIKDSLSnLTNVEGIVNQTSQHISIAKELLdkaKDAKSRAEGVKDSANNTKQAldMSEkaiek 1670
Cdd:pfam12795 60 ----LAALQAKAEAAPKEILASLS-LEELEQRLLQTSAQLQELQNQL---AQLNSQLIELQTRPERAQQQ--LSE----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1671 ARAALKEANNNLNSTRnatvEVDERLTQLedkqmdvmmRLNNLSREVEALRNKTEQNRQmakdaiAQANNaTQVASSLEQ 1750
Cdd:pfam12795 125 ARQRLQQIRNRLNGPA----PPGEPLSEA---------QRWALQAELAALKAQIDMLEQ------ELLSN-NNRQDLLKA 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1848696099 1751 SLNDTENRYQELQMKVDSLggesggLNSINQK----AQDIKNEAEDLLSKA 1797
Cdd:pfam12795 185 RRDLLTLRIQRLEQQLQAL------QELLNEKrlqeAEQAVAQTEQLAEEA 229
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1507-1842 |
1.03e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 49.69 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1507 RNATDSLNAAKEELQSVAKKLQDIASLTQDVKNQaMNTLKKaqkkkdHFENNNKKLKDFIKKIRDFLTEEgadpesiekv 1586
Cdd:pfam04108 10 RWANELLTDARSLLEELVVLLAKIAFLRRGLSVQ-LANLEK------VREGLEKVLNELKKDFKQLLKDL---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1587 aqqvlsitlpvnKTALDQMvmqiKDSLSNL--TNVEGIVNQTSQHisiAKELLD-----KAKDAKSRAEGVKDSANNTKQ 1659
Cdd:pfam04108 73 ------------DAALERL----EETLDKLrnTPVEPALPPGEEK---QKTLLDfidedSVEILRDALKELIDELQAAQE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1660 ALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSRE----VEALRNkTEQNRQMAKDAI 1735
Cdd:pfam04108 134 SLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASLLESLTNHydqcVTAVKL-TEGGRAEMLEVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1736 aqANNATQVAS---SLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSkatkgidQLKKLEKKFK 1812
Cdd:pfam04108 213 --ENDARELDDvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLA-------ALKEFEERWE 283
|
330 340 350
....*....|....*....|....*....|....*...
gi 1848696099 1813 SNEQRMQKQRMELDELKENAT--------LVRDVIREQ 1842
Cdd:pfam04108 284 EEKETIEDYLSELEDLREFYEgfpsaygsLLLEVERRR 321
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1511-1839 |
1.27e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.60 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1511 DSLNAAKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFENN----------NKKLKDFIKKIRDFLTEEGADP 1580
Cdd:PTZ00440 484 DSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIeglkneieglIELIKYYLQSIETLIKDEKLKR 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1581 ESIEKVAQQVLSITLPVNKtaldqmvmqIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAEGVKDSANNT--- 1657
Cdd:PTZ00440 564 SMKNDIKNKIKYIEENVDH---------IKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKfyk 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1658 ---KQALDMSEKAIEKARAALKEAN--NNLNSTRNATVEVDERLTQLEDKQMDVMmrLNNLSREVEALRNKTEQNRQMak 1732
Cdd:PTZ00440 635 gdlQELLDELSHFLDDHKYLYHEAKskEDLQTLLNTSKNEYEKLEFMKSDNIDNI--IKNLKKELQNLLSLKENIIKK-- 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1733 daiaQANNATQVASSleqSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFK 1812
Cdd:PTZ00440 711 ----QLNNIEQDISN---SLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFL 783
|
330 340 350
....*....|....*....|....*....|.
gi 1848696099 1813 SNEQRMQ--KQRM--ELDELKENATLVRDVI 1839
Cdd:PTZ00440 784 QYKDTILnkENKIsnDINILKENKKNNQDLL 814
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1691-1843 |
1.65e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1691 EVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENR---------YQE 1761
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1762 LQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKK-LEKKFKSNEQRMQKQRMELDELKENatlvRDVIR 1840
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAeLEEKKAELDEELAELEAELEELEAE----REELA 169
|
...
gi 1848696099 1841 EQV 1843
Cdd:COG1579 170 AKI 172
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1634-1830 |
2.82e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.33 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1634 KELLDKAKDAKSRAEGVKDSanntkqaLDMSEKAIEKAR---AALKEANNNLNSTRNATVE-VDERLTQLED-----KQM 1704
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKK-------LEEAEKRAEKAEaevAALNRRIQLLEEELERTEErLAEALEKLEEaekaaDES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1705 DVMMR-LNNLSREVE----ALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGE-SGGLNS 1778
Cdd:pfam00261 77 ERGRKvLENRALKDEekmeILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEElKVVGNN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1848696099 1779 INQ-KAQDIK-NEAEDLLSKATKGI-DQLKKLEKKFKSNEQRMQKQRMELDELKE 1830
Cdd:pfam00261 157 LKSlEASEEKaSEREDKYEEQIRFLtEKLKEAETRAEFAERSVQKLEKEVDRLED 211
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1504-1822 |
2.85e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.44 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1504 NHARNATDSLNAAKEELQS-----VAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRDFLTEEGA 1578
Cdd:PTZ00440 1275 NKMENALHEIKNMYEFLISidsekILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQI 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1579 DPE--SIEKVAQQVLSITLPVN-------------------------KTALDQMVMQIKDSLS---NLTNVEGIVNQTSQ 1628
Cdd:PTZ00440 1355 DDEikKIEQIKEEISNKRKEINkylsniksnkekcdlhvrnasrgkdKIDFLNKHEAIEPSNSkevNIIKITDNINKCKQ 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1629 HISIAKELLDKAK-DAKSRAEGVKDSANNTKQALDMS-EKAIEKARaalKEANNNLNSTRNATVEVDERLTQLEDKqMDV 1706
Cdd:PTZ00440 1435 YSNEAMETENKADeNNDSIIKYEKEITNILNNSSILGkKTKLEKKK---KEATNIMDDINGEHSIIKTKLTKSSEK-LNQ 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1707 MMRLNNLSREVEALRNKTEqnrQMAKDAIaQANNAtqvasSLEQSLNDTENRYQELQmkvdslggesgglnSINQKAQDI 1786
Cdd:PTZ00440 1511 LNEQPNIKREGDVLNNDKS---TIAYETI-QYNLG-----RVKHNLLNILNIKDEIE--------------TILNKAQDL 1567
|
330 340 350
....*....|....*....|....*....|....*..
gi 1848696099 1787 KNEAEDL-LSKATKGIDQLKKLEKKFKSNEQRMQKQR 1822
Cdd:PTZ00440 1568 MRDISKIsKIVENKNLENLNDKEADYVKYLDNILKEK 1604
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1586-1787 |
2.89e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1586 VAQQVLSITLPVNKTALDQMVMQIKDsLSNLTNVEGIVNQTSQH-ISIAKELLDKAKDAKSRAEGVKDSANNTKQALDMS 1664
Cdd:PRK09039 39 VAQFFLSREISGKDSALDRLNSQIAE-LADLLSLERQGNQDLQDsVANLRASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1665 EKAIEKARAALKEANnnlnstrnatvevDERLTQLEDkqmdvmmrlnnLSREVEALRnkteqnRQMAkdaiaqannatqv 1744
Cdd:PRK09039 118 AGELAQELDSEKQVS-------------ARALAQVEL-----------LNQQIAALR------RQLA------------- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1848696099 1745 asSLEQSLNDTENRYQELQMKVDSLGGEsggLNS-INQKAQDIK 1787
Cdd:PRK09039 155 --ALEAALDASEKRDRESQAKIADLGRR---LNVaLAQRVQELN 193
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1577-1831 |
3.40e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1577 GADPESIEKVAQQVLSITLPVNKTALDQ-MVMQIKDSLSNLTNVEGIVNQTSqhisiaKELLDKAKDAKSRAEGVKDSAN 1655
Cdd:pfam10174 154 GARDESIKKLLEMLQSKGLPKKSGEEDWeRTRRIAEAEMQLGHLEVLLDQKE------KENIHLREELHRRNQLQPDPAK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1656 nTK---QALDMSEKAIEKARAALKEANNNLNSTR-NATVEVDERltQLEDKQMDV------MMR---------LNNLSRE 1716
Cdd:pfam10174 228 -TKalqTVIEMKDTKISSLERNIRDLEDEVQMLKtNGLLHTEDR--EEEIKQMEVykshskFMKnkidqlkqeLSKKESE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1717 VEALRNKTE--QNrqmakdaiaQANNATQVASSLEQSLNDTENRYQELQMKVDSLggesgglnsinqkaQDIKNEAEDLL 1794
Cdd:pfam10174 305 LLALQTKLEtlTN---------QNSDCKQHIEVLKESLTAKEQRAAILQTEVDAL--------------RLRLEEKESFL 361
|
250 260 270
....*....|....*....|....*....|....*....
gi 1848696099 1795 SKATKgidQLKKL--EKKFKSNEQRMQKQRMELDELKEN 1831
Cdd:pfam10174 362 NKKTK---QLQDLteEKSTLAGEIRDLKDMLDVKERKIN 397
|
|
| OspD |
pfam03207 |
Borrelia outer surface protein D (OspD); |
1570-1797 |
3.42e-05 |
|
Borrelia outer surface protein D (OspD);
Pssm-ID: 367392 [Multi-domain] Cd Length: 254 Bit Score: 47.54 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1570 RDFLTEEGADpESIEKVAQQVLSitlpvnktALDQMVMQIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAEG 1649
Cdd:pfam03207 37 KGYLDNEGAN-SNYESKKQSILS--------ELNQLLKQTTNSLKEAKNTTDNLNASNEANKVVEAVINAVNLISSAADQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1650 VKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATvevdeRLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNR- 1728
Cdd:pfam03207 108 VKSATKNMHDLAQMAEIDLEKIKNSSDKAIFASNLAKEAY-----SLTKAAEQNMQKLYKEQQKISESESESDYSDSAEi 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1729 QMAKDAIAQANNATQVAsslEQSLNDTENRYQElqmKVDSLGGESgglnSINQKAQDIKNEAEDLLSKA 1797
Cdd:pfam03207 183 KQAKEAVEIAWKATVEA---KDKLIDVENTVKE---TLDKIKTET----TNNTKLADIKEAAELVLQIA 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1553-1830 |
5.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1553 DHFENNNKKLKDFIKKIRdflteegADPESIEKVAQQVLSITlpvnktaldqmvMQIKDSLSNLTNVEGIVNQTSQHISI 1632
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIK-------RRIERLEKFIKRTENIE------------ELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1633 AKELLDKAKDAKSRAEGVKDSANNtkqaLDMSEKAIEKARAALKEANNNLNSTRNatvEVDERLTQLEDKQmdvmmrlnn 1712
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIE---ELKKEIEELEEKV--------- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1713 lsREVEALRNKTEQNRQMAKdaiaQANNATQVASSLEQSLNDTENRYQELQMKVDSLggesgglNSINQKAQDIKNEAED 1792
Cdd:PRK03918 283 --KELKELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKEL-------EEKEERLEELKKKLKE 349
|
250 260 270
....*....|....*....|....*....|....*...
gi 1848696099 1793 LLSKatkgidqLKKLEKKFKSNEQRMQKQRmELDELKE 1830
Cdd:PRK03918 350 LEKR-------LEELEERHELYEEAKAKKE-ELERLKK 379
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
987-1023 |
5.56e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 5.56e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1848696099 987 SCHADHTSNQI------ICNCREGYTGLRCDQCAPGYYGNPEQ 1023
Cdd:smart00180 2 DCDPGGSASGTcdpdtgQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1635-1745 |
5.67e-05 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 45.63 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1635 ELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKAR-------AALKEANNNLNSTRNATVEVDerlTQLEDKQMDVM 1707
Cdd:pfam05335 63 QLEQELREAEAVVQEESASLQQSQANANAAQRAAQQAQqqlealtAALKAAQANLENAEQVAAGAQ---QELAEKTQLLE 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1848696099 1708 ---MRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVA 1745
Cdd:pfam05335 140 aakKRVERLQRQLAEARADLEKTKKAAYKAACAAVEAKQKA 180
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1593-1800 |
5.68e-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: 47.69 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1593 ITLPVNKTALDQMVMQIK-DSLSNLTNVEGIVNQTSQHISIAKELLD-----------KAKDAKSRAEGVKDSANNTKQA 1660
Cdd:pfam05262 156 IVIPLKKNILSGNVSDVDtDSISDKKVVEALREDNEKGVNFRRDMTDlkeresqedakRAQQLKEELDKKQIDADKAQQK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1661 LDMSEKAIEK----ARAALKEANNNLNSTRNATVEVDERLTQledkqmdvmmrlnNLSREVEALRNKTEQNRQMAKDAIA 1736
Cdd:pfam05262 236 ADFAQDNADKqrdeVRQKQQEAKNLPKPADTSSPKEDKQVAE-------------NQKREIEKAQIEIKKNDEEALKAKD 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 1737 QAnnatqvASSLEQSLNDTENRYQ--ELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKG 1800
Cdd:pfam05262 303 HK------AFDLKQESKASEKEAEdkELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPV 362
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1665-1848 |
6.76e-05 |
|
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: 48.13 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1665 EKAIEKARAAL-------KEANNNLNSTRnATVEVDERL----TQLEDKQMDVM-MRLNNLSREVEALRNKTEQNRQMAK 1732
Cdd:TIGR02168 178 ERKLERTRENLdrledilNELERQLKSLE-RQAEKAERYkelkAELRELELALLvLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1733 DAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNS----INQKAQDIKNEA-------EDLLSKATKGI 1801
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqkqiLRERLANLERQLeeleaqlEELESKLDELA 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1802 DQLKKLEKKFKSNEQRMQKQRMELDELK---ENATLVRDVIREQVQKYSN 1848
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEaelEELESRLEELEEQLETLRS 386
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1511-1787 |
6.93e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1511 DSLNAAK-----EELQSVAKKlqdIASLTQDVKNQamntlkkaqkkKDHFENNNKKLKDFIKKIRDFLTEEGADPESIEk 1585
Cdd:PHA02562 169 DKLNKDKirelnQQIQTLDMK---IDHIQQQIKTY-----------NKNIEEQRKKNGENIARKQNKYDELVEEAKTIK- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1586 vaQQVLSITlpvnkTALDQMVMQIKDSLSNLTNV-EGIVNQTSQHISIAKElldkakdAKSRAEGvkDSANNTKQALDMS 1664
Cdd:PHA02562 234 --AEIEELT-----DELLNLVMDIEDPSAALNKLnTAAAKIKSKIEQFQKV-------IKMYEKG--GVCPTCTQQISEG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1665 EKAIEKARAALKEANNNLNSTRNATVEVDERLTQLedkqmdvmmrlNNLSREVEALRNKTEQNRQM----------AKDA 1734
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF-----------NEQSKKLLELKNKISTNKQSlitlvdkakkVKAA 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1848696099 1735 IAQA-----NNATQVAsSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIK 1787
Cdd:PHA02562 367 IEELqaefvDNAEELA-KLQDELDKIVKTKSELVKEKYHRGIVTDLLKDSGIKASIIK 423
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1031-1074 |
7.04e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 7.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1848696099 1031 CECN--GNIDtkdpGSCDPRTGQCLnCLYHTDGPSCGHCQHGYYGN 1074
Cdd:smart00180 1 CDCDpgGSAS----GTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1628-1810 |
7.16e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1628 QHISIAKELLDKAKD--AKSRAEgVKDSANNTKQALDMSEKAIEKARAALKEANNNLnstrnAT------VEVDERLTQL 1699
Cdd:COG1842 30 QAIRDMEEDLVEARQalAQVIAN-QKRLERQLEELEAEAEKWEEKARLALEKGREDL-----ARealerkAELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1700 EdKQMDVMMR-LNNLSREVEALRNKTEQNRQMAKDAIAQANNA---TQVASSLEQ-SLNDTENRYQELQMKVDSLGGESG 1774
Cdd:COG1842 104 E-AQLAQLEEqVEKLKEALRQLESKLEELKAKKDTLKARAKAAkaqEKVNEALSGiDSDDATSALERMEEKIEEMEARAE 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1848696099 1775 GLNSINQKAqDIKNEAEDlLSKATKGIDQLKKLEKK 1810
Cdd:COG1842 183 AAAELAAGD-SLDDELAE-LEADSEVEDELAALKAK 216
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1703-1848 |
8.54e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1703 QMDVM-MRLNNLSREVEALRNKTEQNRQ-------MAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGEsg 1774
Cdd:COG1340 2 KTDELsSSLEELEEKIEELREEIEELKEkrdelneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1775 gLNSINQKAQDIKNEAEDL------LSKATKGIDQLKK----LEKKF------KSNE--------------QRMQKQRME 1824
Cdd:COG1340 80 -RDELNEKLNELREELDELrkelaeLNKAGGSIDKLRKeierLEWRQqtevlsPEEEkelvekikelekelEKAKKALEK 158
|
170 180 190
....*....|....*....|....*....|
gi 1848696099 1825 LDELKENATLVRDV------IREQVQKYSN 1848
Cdd:COG1340 159 NEKLKELRAELKELrkeaeeIHKKIKELAE 188
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1507-1802 |
8.58e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.46 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1507 RNATDSLNAAKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKD--HFENNNKKLKDFIKKIRdflteegaDPESIE 1584
Cdd:pfam18971 559 RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKStgNYDEVKKAQKDLEKSLR--------KREHLE 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1585 K-VAQQVLSITLPVNKTALDQMVMQIKDSLSNLTNVEGivNQTSQHIS-------IAKELLDK----AKDAKSRAEGVKD 1652
Cdd:pfam18971 631 KeVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEA--NRDARAIAytqnlkgIKRELSDKlekiSKDLKDFSKSFDE 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1653 SANNTKQALDMSEKAIEKARAALKEANNNlnstrnatvevDERLTQLEdkqmdvmmrlnNLSREVEALRNKteQNRQMAK 1732
Cdd:pfam18971 709 FKNGKNKDFSKAEETLKALKGSVKDLGIN-----------PEWISKVE-----------NLNAALNEFKNG--KNKDFSK 764
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848696099 1733 daiaqannATQVASSLEQSLNDTENRyQELQMKVD------SLGGESGGLNSINQKAQDIKN-EAEDLLSKATKGID 1802
Cdd:pfam18971 765 --------VTQAKSDLENSVKDVIIN-QKVTDKVDnlnqavSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKNED 832
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1409-1717 |
8.65e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1409 RAVTEDLLDaskVKFLRALAAQNKSL-SELQQKAHDLDKKVHHLSHKVcgghsnasvngscpdsqcggagchDDQGNHVc 1487
Cdd:PHA02562 153 RKLVEDLLD---ISVLSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQI------------------------KTYNKNI- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1488 gghgcngtvsTSVAALNHARNAtdSLNAAKEELQSVAKKL-QDIASLTQDVKNqamntlkkaqkkkdhFENNNKKLKDFI 1566
Cdd:PHA02562 205 ----------EEQRKKNGENIA--RKQNKYDELVEEAKTIkAEIEELTDELLN---------------LVMDIEDPSAAL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1567 KKIRDFLTEEGADPESIEKVAQQVLS-ITLPVNKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKS 1645
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKVIKMYEKgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1646 RAEGVKDSANNTKQALDMSEKAIEKARAALKEAnnnlnstRNATVEVDERLTQLEDKQMDVMMRLNNLSREV 1717
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEEL-------QAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1624-1836 |
8.67e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1624 NQTSQHIsiaKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLED-- 1701
Cdd:COG4942 30 EQLQQEI---AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEel 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1702 -KQMDVMMRLNNLSREVEALRNKTEQN--------RQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGE 1772
Cdd:COG4942 107 aELLRALYRLGRQPPLALLLSPEDFLDavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 1773 SGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVR 1836
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1633-1846 |
8.88e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1633 AKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEAN-------NNLNSTRNATVEVDERLTQLEDKQMD 1705
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelarleQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1706 VMMRLNNLSREVEALRNK---TEQNRQMAKDAIAQANNA-TQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQ 1781
Cdd:COG1196 328 LEEELEELEEELEELEEEleeAEEELEEAEAELAEAEEAlLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1848696099 1782 KAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKENATLVRDVIREQVQKY 1846
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1388-1791 |
9.25e-05 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 47.36 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1388 EEKCNASVSGPLSPVEQSKETRAVTEDllDASKVKFLRALAAQNKSLSELQQKAHDLDKKVHHLSHKVcgGHSNASvngS 1467
Cdd:pfam05911 420 NKKGEESDSEKDSSESTGKELVPVSSK--DISLGKSLSWLQSRISVILESHVTQKSIGKILEDIRCAL--QDINDS---L 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1468 CPDSQCGGAGCHDDQGNHVCGGHGCNGTVSTSVAALNHA--RNATDSLNAAKEELQSVAKKLQD-IASLTQdvknqamnT 1544
Cdd:pfam05911 493 PEADSCLSSGHPSTDASCDYITCKENSSVVEKEGSVSGDdkSSEETSKQSIQQDLSKAISKIIDfVEGLSK--------E 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1545 LKKAQKKKdhFENN--NKKLKDFIKKIRDFLTEEgADPESIEKVAQQVLSITLPVNKTALDQMVMQ--IK--DSLSNLTN 1618
Cdd:pfam05911 565 ALDDQDTS--SDSSelSEVLQQFSATCNDVLSGK-ADLEDFVLELSHILDWISNHCFSLLDVSSMEdeIKkhDCIDKVTL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1619 VEGIVNQTSQ------HISIAKELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRNATVEV 1692
Cdd:pfam05911 642 SENKVAQVDNgcseidNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQES 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1693 DERLTQLEdKQMDVMMRLNNLSREveALRNKTEQNRQM---AKDAIAQANNATQVASSLEQSLNDTEN-------RYQEL 1762
Cdd:pfam05911 722 EQLIAELR-SELASLKESNSLAET--QLKCMAESYEDLetrLTELEAELNELRQKFEALEVELEEEKNcheeleaKCLEL 798
|
410 420
....*....|....*....|....*....
gi 1848696099 1763 QMKVDSLGGESGGLNSINQKAQDIKNEAE 1791
Cdd:pfam05911 799 QEQLERNEKKESSNCDADQEDKKLQQEKE 827
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1639-1847 |
9.46e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1639 KAKDAKSRAEGVKDSANntKQALDMSEKAIEKARAALKEANNNLNStrnatvEVDERLTQLEDKQMDVMMRLNNLSREVE 1718
Cdd:PRK12704 32 KIKEAEEEAKRILEEAK--KEAEAIKKEALLEAKEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1719 ALRNKTEQnrqmakdaiaqannATQVASSLEQSLNDTENRYQELQMKVDSLggesgglnsiNQKAQDI----KNEAEDLL 1794
Cdd:PRK12704 104 LLEKREEE--------------LEKKEKELEQKQQELEKKEEELEELIEEQ----------LQELERIsgltAEEAKEIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 1795 skatkgidqLKKLEKKFKSNEQRMQKQRMEldELKENAT-LVRDVIREQVQKYS 1847
Cdd:PRK12704 160 ---------LEKVEEEARHEAAVLIKEIEE--EAKEEADkKAKEILAQAIQRCA 202
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1503-1847 |
1.15e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.52 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1503 LNHARNATDSLNAAKEELQSVAKKLQDIASLTQDVKNqamNTLKKAQKKKD-------------------HFENNNKKLK 1563
Cdd:PTZ00440 790 LNKENKISNDINILKENKKNNQDLLNSYNILIQKLEA---HTEKNDEELKQllqkfptedenlnlkelekEFNENNQIVD 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1564 DFIKKIRdfltEEGADPESIekvaqQVLSITLP---VNKTALDQMvmqikdslsnLTNVEGIVNQTSQHISIAKELLDKA 1640
Cdd:PTZ00440 867 NIIKDIE----NMNKNINII-----KTLNIAINrsnSNKQLVEHL----------LNNKIDLKNKLEQHMKIINTDNIIQ 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1641 KDAKsraEGVKDSANNTKQAL--DMSEKAIEKARAALKEANNNLNSTRNATVEVDE-RLTQLEDKQMD---VMMRLNNLS 1714
Cdd:PTZ00440 928 KNEK---LNLLNNLNKEKEKIekQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGtHLEKLDKEKDEwehFKSEIDKLN 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1715 REVEALRNKTEqnrqmakDAIAQannatQVASSLEQSLNDTENRYQELQMKVDSlggESGGLNSINQKAQDIKNEAEDLL 1794
Cdd:PTZ00440 1005 VNYNILNKKID-------DLIKK-----QHDDIIELIDKLIKEKGKEIEEKVDQ---YISLLEKMKTKLSSFHFNIDIKK 1069
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1848696099 1795 SKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELK----ENATLVRDVIREQVQKYS 1847
Cdd:PTZ00440 1070 YKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKnkshEHVVNADKEKNKQTEHYN 1126
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1581-1812 |
1.18e-04 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 45.74 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1581 ESIEKVAQQVLSITLPVNKTA--LDQMVMQIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKD-AKSRAEGVKDSANNT 1657
Cdd:smart00283 4 EAVEEIAAGAEEQAEELEELAerMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITaMDQIREVVEEAVSAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1658 KQALDMSEK----------------------AIEKARA---------------ALkeANNnlnsTRNATVEVDERLTQLE 1700
Cdd:smart00283 84 EELEESSDEigeivsviddiadqtnllalnaAIEAARAgeagrgfavvadevrKL--AER----SAESAKEIESLIKEIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1701 DKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSlggesgglnsIN 1780
Cdd:smart00283 158 EETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDE----------IA 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 1848696099 1781 QKAQDIKNEAEDlLSKATKGI----DQLKKLEKKFK 1812
Cdd:smart00283 228 QVTQETAAMSEE-ISAAAEELsglaEELDELVERFK 262
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1634-1763 |
1.39e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1634 KELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNN--LNStrnATVEVD---ERLTQLEDKQMDVMM 1708
Cdd:COG1579 41 AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA---LQKEIEslkRRISDLEDEILELME 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1848696099 1709 RLNNLSREVEALRNKTEQNRQMAKDAIAQannatqvassLEQSLNDTENRYQELQ 1763
Cdd:COG1579 118 RIEELEEELAELEAELAELEAELEEKKAE----------LDEELAELEAELEELE 162
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1638-1830 |
1.57e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1638 DKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEAN--------NNLNSTRNATVEVDERLTQLEDKQM---DV 1706
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIarkqnkydELVEEAKTIKAEIEELTDELLNLVMdieDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1707 MMRLNNLSREVEALRNKTEQNRQMAK------------DAIAQANN----ATQVASSLEQSLNDTENRYQELQMKVDSLG 1770
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctQQISEGPDritkIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 1771 GESGGL----NSINQKAQDIKNEaedlLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKE 1830
Cdd:PHA02562 334 EQSKKLlelkNKISTNKQSLITL----VDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1605-1803 |
1.65e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 45.48 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1605 MVMQIKDSLSNLTNVEGIVNQTSQHISI-----------AKELLDKAKDAKSRA----EGVKDSANNTKQALDmsekAIE 1669
Cdd:pfam06008 17 INYNLENLTKQLQEYLSPENAHKIQIEIlekelsslaqeTEELQKKATQTLAKAqqvnAESERTLGHAKELAE----AIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1670 KARAALKEANNN---LNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEAlrnkTEQNRQMAKDAIAQANNATQ--- 1743
Cdd:pfam06008 93 NLIDNIKEINEKvatLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQN----AEAELKAAQDLLSRIQTWFQspq 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1744 -----VASSLEQSLNDTENRYQELQMKVD---SLGGESGGLNSINQKAQDI-----------KNEAEDLLSKATKGIDQ 1803
Cdd:pfam06008 169 eenkaLANALRDSLAEYEAKLSDLRELLReaaAKTRDANRLNLANQANLREfqrkkeevseqKNQLEETLKTARDSLDA 247
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
1511-1726 |
1.73e-04 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 45.72 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1511 DSLNAAKEELQSVakkLQDIASLTQDVKNQAMNTLKKAQKKKDHFENNN---KKLKDFIKKIRDFLTEEG----ADPESI 1583
Cdd:cd22654 104 SQLQTIQNSMEQT---SSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSNgeiAQLRTQIKTINDEIQEELtkilNRPIEV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1584 EKVAQQVLSITLP-VNKTALDQMVmqikdslsNLTNVEGIVNQT-----SQHISIAKELLDKAK----------DAKSRA 1647
Cdd:cd22654 181 GDGSINIGKQVFTiTITTATTKTV--------DVTSIGGLINGIgnasdDEVKEAANKIQQKQKelvdlikklsDAEIQA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1648 EG---VKDSANNTKQALDMSEKAIEKARAALKEANNNLNstrnatvEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKT 1724
Cdd:cd22654 253 TQltlVEDQVNGFTELIKRQIATLENLVEDWEMLNQNMN-------QLQTNVNSGKIDSKLLQKQLKQIKKISDELNKQT 325
|
..
gi 1848696099 1725 EQ 1726
Cdd:cd22654 326 KQ 327
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1612-1841 |
1.87e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 45.84 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1612 SLSNLTNVE----GIVNQTSQHISIAKELLDKAKDAKSraeGVKDSANNTKQALDMSEKAIEKAR-------AALKEANN 1680
Cdd:pfam04108 1 SLSSAQDLCrwanELLTDARSLLEELVVLLAKIAFLRR---GLSVQLANLEKVREGLEKVLNELKkdfkqllKDLDAALE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1681 NLNSTRN--ATVEVDERLTQLEDKQ---MD-VMMRlnnlsrEVEALRNKteqnrqmAKDAIAQANNATQvasSLEQSLND 1754
Cdd:pfam04108 78 RLEETLDklRNTPVEPALPPGEEKQktlLDfIDED------SVEILRDA-------LKELIDELQAAQE---SLDSDLKR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1755 TENRYQELQMKVDSLGGESGGLNSINQKAQDIK---NEAEDLLSKATKGIDQLKKLEKKFKSNEQRMqkqrmeLDELKEN 1831
Cdd:pfam04108 142 FDDDLRDLQKELESLSSPSESISLIPTLLKELEsleEEMASLLESLTNHYDQCVTAVKLTEGGRAEM------LEVLEND 215
|
250
....*....|
gi 1848696099 1832 ATLVRDVIRE 1841
Cdd:pfam04108 216 ARELDDVVPE 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1734-1828 |
2.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1734 AIAQANNATQVASSlEQSLNDTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKS 1813
Cdd:COG3883 1 ALALALAAPTPAFA-DPQIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE 76
|
90
....*....|....*
gi 1848696099 1814 NEQRMQKQRMELDEL 1828
Cdd:COG3883 77 AEAEIEERREELGER 91
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1625-1809 |
2.23e-04 |
|
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: 44.67 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1625 QTSQHISIAKELLDKAKDAKSRAEG-VKDSANNTKQALDMSEKAIEKARAALKEANNNLnstrnaTVEVDERLTQLEDKQ 1703
Cdd:pfam04012 26 MLEQAIRDMQSELVKARQALAQTIArQKQLERRLEQQTEQAKKLEEKAQAALTKGNEEL------AREALAEKKSLEKQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1704 MD---VMMRLN----NLSREVEALRNKTEQNRQ-------MAKDAIAQANNATQVASSleqSLNDTENRYQELQMKVDSL 1769
Cdd:pfam04012 100 EAletQLAQQRsaveQLRKQLAALETKIQQLKAkknllkaRLKAAKAQEAVQTSLGSL---STSSATDSFERIEEKIEER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1848696099 1770 GGESGGLNSINQkAQDIKNEAEDLLSKATKGIDQLKKLEK 1809
Cdd:pfam04012 177 EARADAAAELAS-AVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1676-1845 |
2.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1676 KEANNNLNSTRnatvevdERLTQLEDKQMDVMMRLNNLSREVE-ALRNKTEQNRQMAKDAIAQA---NNATQVASSLEQS 1751
Cdd:COG1196 175 EEAERKLEATE-------ENLERLEDILGELERQLEPLERQAEkAERYRELKEELKELEAELLLlklRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1752 LNDTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDELKEN 1831
Cdd:COG1196 248 LEELEAELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170
....*....|....
gi 1848696099 1832 ATLVRDVIREQVQK 1845
Cdd:COG1196 325 LAELEEELEELEEE 338
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1745-1821 |
2.91e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 42.19 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1745 ASSLE---QSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNE------AEDLLSKATKGIDQLKKLEKKFKSNE 1815
Cdd:pfam18595 1 SSTLAeekEELAELERKARELQAKIDALQVVEKDLRSCIKLLEEIEAElakleeAKKKLKELRDALEEKEIELRELERRE 80
|
....*.
gi 1848696099 1816 QRMQKQ 1821
Cdd:pfam18595 81 ERLQRQ 86
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1743-1848 |
3.34e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1743 QVASSLEQSLNDTENRYQELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQR 1822
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEK---RDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK 77
|
90 100
....*....|....*....|....*.
gi 1848696099 1823 MELDELKENATLVRDVIREQVQKYSN 1848
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAE 103
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1683-1842 |
3.40e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1683 NSTRNATVEVDERLTQL---EDKQMDVMM---RLNNLSREVEALRNKTEQNRQMAKDAIAQANNAtqvassLEQSLNDTE 1756
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEekeEERRLDEMMeeeRERALEEEEEKEEERKEERKRYRQELEEQIEER------EQKRQEEYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1757 NRYQELQMkvdslggesggLNSINQKAQDikNEAEDLLSKATKgidQLKKLEKKFKSNEQRMQKQRMELDELKENATLVR 1836
Cdd:pfam13868 95 EKLQEREQ-----------MDEIVERIQE--EDQAEAEEKLEK---QRQLREEIDEFNEEQAEWKELEKEEEREEDERIL 158
|
....*.
gi 1848696099 1837 DVIREQ 1842
Cdd:pfam13868 159 EYLKEK 164
|
|
| GARP |
pfam16731 |
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, ... |
1632-1785 |
3.63e-04 |
|
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, is one of a subset of major surface molecules on Trypanosoma species. They are all surface-orientated, immunodominant, and highly charged. GARP is interesting as ts expression coincides with the loss and gain of variant surface glycoprotein (VSG) molecules in the tsetse vector. It has an extended helical bundle structure that is homologous to the core surface structure of VSG, suggesting that it might replace the bloodstream VSG as the trypanosomes differentiate inside the tsetse vector after a blood-meal.
Pssm-ID: 435545 [Multi-domain] Cd Length: 192 Bit Score: 43.52 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1632 IAKELLDKAKDAKSRAEG----VKDSANNTKQAldmsEKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVM 1707
Cdd:pfam16731 26 TAAAASSKAFKAKVQAEEavelAESAGLNDPKA----KEAVTRAREAAVRATEAAEAAATAASNVEINAANLASVAWAYV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1708 MRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATqvASSLEQSLNDTENRYQ------------ELQMKVDSLGGESGG 1775
Cdd:pfam16731 102 PSLDDGLKKLAECGNADEDVREAAKKCTKTAENVT--AQSLTEALEGLRKLFDvksaerlrketvEAHEELKSLEKAVEE 179
|
170
....*....|
gi 1848696099 1776 LNSINQKAQD 1785
Cdd:pfam16731 180 AVRAQKAAED 189
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1614-1678 |
3.72e-04 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 40.44 E-value: 3.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1614 SNLTNVEGIVNQTSQHI----SIAKELLDKAKDAKSRAEGVKDSANntkQALDMSEKAIEKARAALKEA 1678
Cdd:pfam11839 1 AQVEELQSKADQAEQDAaaaqSAADSAKAKADEAAARANAAEAAAE---EAQQAAEEANEKADRMFEKS 66
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1608-1825 |
4.30e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 43.96 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1608 QIkDSLSNlTNVEgiVNQTSQhisiakELLDKAKDAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNSTRN 1687
Cdd:pfam17078 11 QI-DALTK-TNLQ--LTVQSQ------NLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1688 ATvevdERLTqLEDKQMDvmMRLNNLSREVEALRNKTeQNRQMAKDAIAQANNA-----TQVASSLEQSLND--TENRYQ 1760
Cdd:pfam17078 81 SY----EELT-ESNKQLK--KRLENSSASETTLEAEL-ERLQIQYDALVDSQNEykdhyQQEINTLQESLEDlkLENEKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1761 -------------ELQMKVDSLGGESGGLNSINQKAQdikNEAEDLLSKATKGIDqLKKLEKKFKSNEQRM--QKQRMEL 1825
Cdd:pfam17078 153 lenyqqrissndkDIDTKLDSYNNKFKNLDNIYVNKN---NKLLTKLDSLAQLLD-LPSWLNLYPESRNKIleYAEKMEL 228
|
|
| FIVAR |
pfam07554 |
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
1608-1683 |
4.91e-04 |
|
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.
Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 40.00 E-value: 4.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1848696099 1608 QIKDSLSNLTNVEgivnQTSQHISIAKELLDKAKDAKSRAEGVKDSANNTkqalDMSEKAIEKARAALKEANNNLN 1683
Cdd:pfam07554 2 ALKTSINDKNATK----TSSNYINADNDKKAAYNNAITAAKAILNKTNNP----NATQEEVNQALTKLNTAINALN 69
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1509-1848 |
6.27e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1509 ATDSLNAAKEELQSVAKKLQDIASLTQDVKN---QAMNTLK----KAQKKKDHFENNN--KKLKDfIKKIRDFLTEEGAD 1579
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQTelpDQLQELKagyrELVEEGYHLDHLDieKEIQD-LKEQIDENLALLEE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1580 PEsIEKVAQQVLSItlpvnKTALDQM-------------VMQIKDSLSN-LTNVEGIVNQTSQHIsiakELLDK----AK 1641
Cdd:PRK04778 275 LD-LDEAEEKNEEI-----QERIDQLydilerevkarkyVEKNSDTLPDfLEHAKEQNKELKEEI----DRVKQsytlNE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1642 DAKSRAEGVKDSANNTKQALDMSEKAIEKARAALKEANNNLNstrnatvEVDERLTQLEDKQMDVMMRLNNLsREVEA-L 1720
Cdd:PRK04778 345 SELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGL-RKDELeA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1721 RNKTEQNRQ---MAKDAIAQANnatqvASSLEQSLndtENRYQELQMKVDSLGGEsgglnsINQKAQDIKnEAEDLLSKA 1797
Cdd:PRK04778 417 REKLERYRNklhEIKRYLEKSN-----LPGLPEDY---LEMFFEVSDEIEALAEE------LEEKPINME-AVNRLLEEA 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1848696099 1798 TKGIDQLKKlekkfksneqrmqkqrmELDELKENATLVrdvirEQVQKYSN 1848
Cdd:PRK04778 482 TEDVETLEE-----------------ETEELVENATLT-----EQLIQYAN 510
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1493-1841 |
6.43e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1493 NGTVSTSVAALNHARNATDSLNAAKEELQSVAKK-LQDIASLTQD------VKNQAMNTLKKAQKKKDHFEN---NNKKL 1562
Cdd:PTZ00440 514 NNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYyLQSIETLIKDeklkrsMKNDIKNKIKYIEENVDHIKDiisLNDEI 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1563 KDFIKKIRDFLTEEGADPESIEKVAQQVLSITLPVNKTALDQMVMQIKDSLSN-LTNVEGIVNQTSQHISIaKELLDKAK 1641
Cdd:PTZ00440 594 DNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELLDELSHfLDDHKYLYHEAKSKEDL-QTLLNTSK 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1642 DAKSRAEGVK-DSANNTKQALDM-SEKAIEKARAALKEANNNLNStrnatvEVDERLTQLEDKQMDVMMRLNNLSREVEA 1719
Cdd:PTZ00440 673 NEYEKLEFMKsDNIDNIIKNLKKeLQNLLSLKENIIKKQLNNIEQ------DISNSLNQYTIKYNDLKSSIEEYKEEEEK 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1720 LRNKTEQNRQMAKDAIAQANNAtqvasslEQSLNDTENRYQE-LQMKVDSLGGESGGLNSINQKAQDIKNeAEDLLSK-- 1796
Cdd:PTZ00440 747 LEVYKHQIINRKNEFILHLYEN-------DKDLPDGKNTYEEfLQYKDTILNKENKISNDINILKENKKN-NQDLLNSyn 818
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 1797 ---------ATKGIDQLKKLEKKFKSNEQRMQKQRMElDELKENATLVRDVIRE 1841
Cdd:PTZ00440 819 iliqkleahTEKNDEELKQLLQKFPTEDENLNLKELE-KEFNENNQIVDNIIKD 871
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
342-392 |
6.50e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 6.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1848696099 342 CNCNG---HSSHCHFDmavylatgnisGGVCDdCQHNTMGRNCEMCKPFYYQDP 392
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1514-1683 |
7.21e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1514 NAAKEELQSVAKKLQDIASLTQDVKNQAMNTLKKAQKKKDHFEN------NNKKLKDFIKKIRDFLTEEGADPESIEKvA 1587
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNkyneiqENKILIEKLRGKIDNYKKQIAEIDSIIP-D 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1588 QQVLSITLPVNKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHISiakELLDKAKDAKSRAEgvkdsanntkqaldmSEKA 1667
Cdd:PRK01156 669 LKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN---ELSDRINDINETLE---------------SMKK 730
|
170
....*....|....*.
gi 1848696099 1668 IEKARAALKEANNNLN 1683
Cdd:PRK01156 731 IKKAIGDLKRLREAFD 746
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1569-1830 |
7.58e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1569 IRDFLTEEGADPESIEKVAQQVLSITLPVNKTALdqmvmQIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAE 1648
Cdd:pfam19220 8 LRVRLGEMADRLEDLRSLKADFSQLIEPIEAILR-----ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1649 GVKDsanNTKQALDMSEKAIEKARAALKEANNNLnSTRNATVEVDERLTQLEDKQmdvmmrLNNLSREVEALRNKTEQNR 1728
Cdd:pfam19220 83 GELE---ELVARLAKLEAALREAEAAKEELRIEL-RDKTAQAEALERQLAAETEQ------NRALEEENKALREEAQAAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1729 QMAKDAIAQANNATQVASSLEQslndtENRyqELQMKVDSLGGEsggLNSINQKAQDIKNEAEDLLSkatkgidQLKKLE 1808
Cdd:pfam19220 153 KALQRAEGELATARERLALLEQ-----ENR--RLQALSEEQAAE---LAELTRRLAELETQLDATRA-------RLRALE 215
|
250 260
....*....|....*....|..
gi 1848696099 1809 KKFKSNEQRMQKQRMELDELKE 1830
Cdd:pfam19220 216 GQLAAEQAERERAEAQLEEAVE 237
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1709-1827 |
1.11e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1709 RLNNLSREVEALRNKTEQnrqmakdAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKN 1788
Cdd:pfam10473 25 KVENLERELEMSEENQEL-------AILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVS 97
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1848696099 1789 EAEDLLSKATKGI----DQLKKLEKKFKSNEQRMQKQRMELDE 1827
Cdd:pfam10473 98 ELESLNSSLENLLeekeQEKVQMKEESKTAVEMLQTQLKELNE 140
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1512-1841 |
1.28e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1512 SLNAAKEELQSVAKKLQDIASltqdvkNQAMNTLKKAQKKKDHFENNNKKLKDFIKKIRDFLTEEGADPESIEKVAQQVL 1591
Cdd:PTZ00440 2259 KINNIKDKINDKEKELINVDS------SFTLESIKTFNEIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENITHLLNRIN 2332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1592 SITLPVNKTALDQMVMQIKDSLSNLTNVEgiVNQTSQHISIAKELLDKAKDAKSRAEGVkDSANNTKQALDMSEKAIEka 1671
Cdd:PTZ00440 2333 TLINDLDNYQDENYGKDKNIELNNENNSY--IIKTKEKINNLKEEFSKLLKNIKRNNTL-CNNNNIKDFISNIGKSVE-- 2407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1672 raalkeannNLNSTRNATVEVDERLTQLEDKQMDV--MMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLE 1749
Cdd:PTZ00440 2408 ---------TIKQRFSSNLPEKEKLHQIEENLNEIknIMNETKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDLIE 2478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1750 Q-SLNDTENRYQELQMkvdslggesgglNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQ-RMELDE 1827
Cdd:PTZ00440 2479 NvTSHNEKIKSELLII------------NDALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYIINElESHVSK 2546
|
330
....*....|....
gi 1848696099 1828 LKENATLVRDVIRE 1841
Cdd:PTZ00440 2547 LNELLSYIDNEIKE 2560
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1665-1846 |
1.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1665 EKAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQmDVMMRLNNLSRE---VEALRNKTEQnrqmAKDAIAQANNA 1741
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDeidVASAEREIAE----LEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1742 TQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGID--QLKKLEKKFKS-----N 1814
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARleLRALLEERFAAalgdaV 763
|
170 180 190
....*....|....*....|....*....|...
gi 1848696099 1815 EQRMQKQ-RMELDELKENATLVRDVIREQVQKY 1846
Cdd:COG4913 764 ERELRENlEERIDALRARLNRAEEELERAMRAF 796
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
301-332 |
1.68e-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: 38.10 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|..
gi 1848696099 301 IHGRCVCKHNTEGLNCERCRHFHNDLPWRPAE 332
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1581-1726 |
1.83e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.09 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1581 ESIEKVAQQVLSITLPVN-KTALDQMVMQIKDSLSNLTNVEGIVNQTSQHI-SIAKELLDKAKDAKSRAEGVKDSANNTK 1658
Cdd:COG0840 215 EVLERIAEGDLTVRIDVDsKDEIGQLADAFNRMIENLRELVGQVRESAEQVaSASEELAASAEELAAGAEEQAASLEETA 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1659 QAL-DMSEKAIEKARAAlKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQ 1726
Cdd:COG0840 295 AAMeELSATVQEVAENA-QQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQE 362
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1502-1680 |
2.11e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 41.63 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1502 ALNHARNATDSLNAakeELQSVAKKLQD----IASLTQDVKNQAMNTLKKAQKKKDHF-----------ENNNKKLKDFI 1566
Cdd:cd21116 42 ARAHALEWLNEIKP---KLLSLPNDIIGynntFQSYYPDLIELADNLIKGDQGAKQQLlqglealqsqvTKKQTSVTSFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1567 KKIRDFLTEEGADPESIEKVAQQVLS--ITLPVNKTALDQMVMQIKDSLSNLTNVEGIVNQTSQHIsiaKELLDKAKDAK 1644
Cdd:cd21116 119 NELTTFKNDLDDDSRNLQTDATKAQAqvAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDI---KELITDLEDAE 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 1848696099 1645 sraegvkdSANNTKQALDMSEKAIEKARAALKEANN 1680
Cdd:cd21116 196 --------SSIDAAFLQADLKAAKADWNQLYEQAKS 223
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1604-1809 |
2.72e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1604 QMVMQIKDSLSNLTNVEGIVNQTSQHISIAKELLDKAKDAKSRAEGVKDsanntkqALDMSEKAIEKARAALKEANNNLN 1683
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVD-------KLTDFENQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1684 ST------RNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTEN 1757
Cdd:cd22656 167 DLltdeggAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIP 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1848696099 1758 RYQELQmkvdslggesGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEK 1809
Cdd:cd22656 247 ALEKLQ----------GAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEK 288
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1693-1809 |
3.01e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 42.26 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1693 DERLTQLEDK------QMDVMMRLN-NLSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMK 1765
Cdd:PRK15374 98 DVSLSQLESRlavwqaMIESQKEMGiQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPA 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1848696099 1766 VDSLGGESGGLnsinQKAQDIKNEAEDLLSKAT-----KGIDQLKKLEK 1809
Cdd:PRK15374 178 DPGYAQAEAAV----EQAGKEATEAKEALDKATdatvkAGTDAKAKAEK 222
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-328 |
3.20e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 3.20e-03
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1666-1839 |
3.38e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 42.31 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1666 KAIEKARAALKE-ANNNLnsTRNATVEVDERLTQLEDkQMDVMMrlNNLSREVEALRNKTEQN----RQMAKDAIAQANN 1740
Cdd:COG0840 208 RPLRELLEVLERiAEGDL--TVRIDVDSKDEIGQLAD-AFNRMI--ENLRELVGQVRESAEQVasasEELAASAEELAAG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1741 ATQVASSLEQSLNDTEnryqelQMkvdslggeSGGLNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQK 1820
Cdd:COG0840 283 AEEQAASLEETAAAME------EL--------SATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE 348
|
170
....*....|....*....
gi 1848696099 1821 QRMELDELKENATLVRDVI 1839
Cdd:COG0840 349 TAETIEELGESSQEIGEIV 367
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1666-1845 |
4.19e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1666 KAIEKARAALKEANNNLNSTRNATVEVDERLTQLEDKQMDVMMrLNNLSR--EVEALRNKTEQNRQMAKDAIAQAN---- 1739
Cdd:pfam05667 251 RIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTG-LTKGSRftHTEKLQFTNEAPAATSSPPTKVETeeel 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1740 --NATQVASSLEQSLNDTENRYQEL--QMK--------VDSLGGESGGLNSINQKAQDIKNEAEDLLSKATKGIdqlKKL 1807
Cdd:pfam05667 330 qqQREEELEELQEQLEDLESSIQELekEIKklessikqVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENI---AKL 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1848696099 1808 EKKFKSNEQRMQ-------KQR----MELDELKENATLVRDVIREQVQK 1845
Cdd:pfam05667 407 QALVDASAQRLVelagqweKHRvpliEEYRALKEAKSNKEDESQRKLEE 455
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1504-1792 |
4.71e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1504 NHARNATDSLNAAKEELQSVAKKLQDIASL--TQDVKNQAMNTLKKAQKKKDHFENN---NKKL---KDFIKKIRDFLTE 1575
Cdd:PTZ00440 2360 SYIIKTKEKINNLKEEFSKLLKNIKRNNTLcnNNNIKDFISNIGKSVETIKQRFSSNlpeKEKLhqiEENLNEIKNIMNE 2439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1576 EGADPESIEKVAQQVLSITLPVNKTALDQMVMQIKDSLSNLT-NVEGIVNQtsqhISIAKELLDKAKDAKSRaegvkdsa 1654
Cdd:PTZ00440 2440 TKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDLIENVTsHNEKIKSE----LLIINDALRRVKEKKDE-------- 2507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1655 nntkqaldmsekaIEKARAALKEANNNL-NSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREVEALRNKteqnrqmaKD 1733
Cdd:PTZ00440 2508 -------------MNKLFNSLTENNNNNnNSAKNIVDNSTYIINELESHVSKLNELLSYIDNEIKELENE--------KL 2566
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1734 AIAQANNATQVASSLEQSLNDT-ENRYQELQMKVDslgGESGGLNSINQKAQDIKNEAED 1792
Cdd:PTZ00440 2567 KLLEKAKIEESRKERERIESETqEDNTDEEQINRQ---QQERLQKEEEQKAYSQERLNRE 2623
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1619-1794 |
4.80e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1619 VEGIVNQT--SQHISIAKELLDKAKDAKSRAEgvkdSANNTKQALDMSEKAIE---KARAALKEANNNLNSTRNATVEVD 1693
Cdd:COG3096 481 VCKIAGEVerSQAWQTARELLRRYRSQQALAQ----RLQQLRAQLAELEQRLRqqqNAERLLEEFCQRIGQQLDAAEELE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1694 ERLTQLEDKQMDVMMRLNN-------LSREVEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTENRYQELQMKV 1766
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEaveqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL 636
|
170 180
....*....|....*....|....*...
gi 1848696099 1767 DSLGGESGGLNSINQKAQDIKNEAEDLL 1794
Cdd:COG3096 637 EREREATVERDELAARKQALESQIERLS 664
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1678-1820 |
5.20e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1678 ANNNLNSTRNATVEVDERLTQLEDKQMDVMMRLNNLSREvEALRNKTEQNRQMAKDAIAQANNATQVASSLEQSLNDTEN 1757
Cdd:cd22656 75 AGDIYNYAQNAGGTIDSYYAEILELIDDLADATDDEELE-EAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1848696099 1758 ---RYQELQMKVDS-LGGESGGL--NSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQK 1820
Cdd:cd22656 154 dqtALETLEKALKDlLTDEGGAIarKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALR 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1709-1848 |
6.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1709 RLNNLSREVEALRNKTEQNRQmakdaiaqannATQVASSLEQSLNDTENRYQELQMKVDSLggesgglnSINQKAQDIKN 1788
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAE-----------LQEELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQ 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1789 EAEDLLSKATKGIDQLKKLEKKfksnEQRMQKQRMELDELKENATLVRDVIREQVQKYSN 1848
Cdd:COG4717 133 ELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1274-1451 |
9.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1274 TRIKELERKLKGVQDLISM---EDSNRIHQLIGQSIDDLRAEIALTDGRLMGVTRELNTTADEEEALRHI--------LS 1342
Cdd:COG4913 262 ERYAAARERLAELEYLRAAlrlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1343 VLEKELTHINATVAHKQRLLDNYLT-------------SGFADQFEKVKKFYQESAKAEEKCNAsvsgplspveqsketr 1409
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEAllaalglplpasaEEFAALRAEAAALLEALEEELEALEE---------------- 405
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1848696099 1410 AVTEdlLDASKVKFLRALAAQNKSLSELQQKAHDLDKKVHHL 1451
Cdd:COG4913 406 ALAE--AEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1757-1845 |
9.20e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1757 NRYQELQMKVDSLGGESGglNSINQKAQDIKNEAEDLLSKATKGIDQLKKLEKKFKSNEQRMQKQRMELDEL--KENATL 1834
Cdd:pfam03938 15 PEGKAAQAQLEKKFKKRQ--AELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQElqKKQQEL 92
|
90
....*....|.
gi 1848696099 1835 VRDvIREQVQK 1845
Cdd:pfam03938 93 LQP-IQDKINK 102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1733-1845 |
9.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848696099 1733 DAIAQANNATQVASSLEQSLNDTENRYQELQMKVDSLGGESGGLNSINQKAQDIKN---------EAEDLLSKATKGIDQ 1803
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaELEAELERLDASSDD 686
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1848696099 1804 LKKLEKKFKSNEQRMQKQRMELDELKENATLV---RDVIREQVQK 1845
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELDE 731
|
|
| |
