|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1589-1848 |
8.28e-106 |
|
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: 338.62 E-value: 8.28e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1589 TMNIN-LTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERT 1667
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1668 NSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLL 1747
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1748 KRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENT 1827
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 568965053 1828 LKEGNDILDEANRLLGEINSV 1848
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-281 |
7.45e-91 |
|
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: 295.04 E-value: 7.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 29 AHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPYQRHPITNAIDGKN----T 104
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 105 WWQSPSIKNGVeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGP 184
Cdd:smart00136 75 WWQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 185 PSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreI 262
Cdd:smart00136 148 ITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------D 219
|
250
....*....|....*....
gi 568965053 263 DPIVTRRYYYSVKDISVGG 281
Cdd:smart00136 220 RPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-281 |
4.94e-86 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 281.01 E-value: 4.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 35 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPYQRHPITNAIDGKN----TWWQSPS 110
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 111 IKngVEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 189
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 190 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 267
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 568965053 268 RRYYYSVKDISVGG 281
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
1225-1360 |
3.35e-47 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 165.51 E-value: 3.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1225 HLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDEtGFATYKPQVIIRGGtptHARIITRHMAAPLIGQLTRHEIEMTE 1304
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568965053 1305 KEWKYYGddpriSRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEP 1360
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1230-1374 |
7.35e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.97 E-value: 7.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1230 YWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGtptHARIITRHMA--APLIGQLTRHEIEMTEKEW 1307
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568965053 1308 KYygddpRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGhvlAGSPPAHLIE 1374
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG---GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
579-718 |
2.47e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 143.18 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 579 YWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTekILQLMIIFEGNDLRISTAYKE-VYLEPSEEHIEEVSLKEEAFT 657
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568965053 658 iHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVPYPTDRRiATDVE 718
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-706 |
1.95e-33 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 125.84 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 578 YYWSAPPPYLGNRLPAVGGQLSFTISYdleEEEDDTEKILQLMIIFEGNDLRISTAYkEVYLEPSEEHIEEVSLKEEAFT 657
Cdd:smart00281 5 VYWVAPEQFLGDKVTSYGGKLRYTLSF---DGRRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568965053 658 IHGTNlPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVP 706
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1610-1943 |
2.32e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1610 NTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQD----- 1684
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqls 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1685 ---AEAINEKAVQLNETLGNQD--KTAERNLEELQKEID----------RMLKELRsKDLQTQKEVAEDELVAAEGLLKR 1749
Cdd:TIGR02168 754 kelTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEqlkeelkalrEALDELR-AELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1750 VnklfGEPRAQNEDME---KDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIEN 1826
Cdd:TIGR02168 833 I----AATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1827 TLKEGNDILDEANRLLGEINSVIDyvdDIKTKLPPMSEELSDKIDDLAQEIkdrrlAEKVFQAESHAAQLNDSSAVLDGI 1906
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEA-----EALENKIEDDEEEARRRLKRLENK 980
|
330 340 350
....*....|....*....|....*....|....*..
gi 568965053 1907 LDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKE 1943
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
913-960 |
4.18e-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: 62.37 E-value: 4.18e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 913 PCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQL-GRGC 960
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1608-1943 |
1.00e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQELKHLLSPQRAPerlIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:PRK02224 319 LEDRDEELRDRLEECRVA---AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1688 INEKAVQLNETLGNqdktAERNLEELQKEIDRM---LKELRSkDLQTQKE-VAEDELVAAEGllK------------RVN 1751
Cdd:PRK02224 396 LRERFGDAPVDLGN----AEDFLEELREERDELrerEAELEA-TLRTARErVEEAEALLEAG--KcpecgqpvegspHVE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1752 KLfGEPRAQNEDMEKDLQQ---KLAEYKNKLDDAWDLLREATDKTRDANRLSAANQknmtILETKKEAIEGSKRQIENTL 1828
Cdd:PRK02224 469 TI-EEDRERVEELEAELEDleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEE----LIAERRETIEEKRERAEELR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1829 KEGNDILDEA------------------------NRLLGEINSVIDYVDDIktklppmsEELSDKIDDLAQEIKDRR--- 1881
Cdd:PRK02224 544 ERAAELEAEAeekreaaaeaeeeaeeareevaelNSKLAELKERIESLERI--------RTLLAAIADAEDEIERLRekr 615
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568965053 1882 --LAEKVFQAESHAAQLNDSSAVLDGILDEAknisfNATAAFRAYSNIKDYIDEAEKVAREAKE 1943
Cdd:PRK02224 616 eaLAELNDERRERLAEKRERKRELEAEFDEA-----RIEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1635-1912 |
3.90e-11 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 66.09 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1635 NVNTLVMETNELLTRATKVTadgEQTGQDAERTNSRAESLEEF----------IKGLVQDAEAINEKAVQLNETLgnQDK 1704
Cdd:COG1340 2 KTDELSSSLEELEEKIEELR---EEIEELKEKRDELNEELKELaekrdelnaqVKELREEAQELREKRDELNEKV--KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1705 TAERNleELQKEIDRMLKELRSKDLQTQKEVAEDELVAAegLLKRVNKLfgEPRAQNEDM----EKDLQQKLAEYKNKLD 1780
Cdd:COG1340 77 KEERD--ELNEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERL--EWRQQTEVLspeeEKELVEKIKELEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1781 DAwdllREATDKTRDANRLSAAnqknmtiLETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLP 1860
Cdd:COG1340 151 KA----KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568965053 1861 PMSE---ELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKN 1912
Cdd:COG1340 220 EAQEkadELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
914-960 |
4.26e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 4.26e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQ--LGRGC 960
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
914-960 |
7.77e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 7.77e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQlGRGC 960
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
963-1007 |
2.46e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 2.46e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568965053 963 CNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNFQEGGC 1007
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1632-1949 |
2.68e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.00 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1632 AEGNVNTLVMETNElltRATKVTADGEQTGQDA-ERTNSRAESLEEFIKGLVQDAEainekavqlnetlgnqdKTAERNL 1710
Cdd:NF041483 751 AQAEAQRLVEEADR---RATELVSAAEQTAQQVrDSVAGLQEQAEEEIAGLRSAAE-----------------HAAERTR 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1711 EELQKEIDRML------KELRSKDLQTQKEVAEDELVAAEGLLKR-VNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDA- 1782
Cdd:NF041483 811 TEAQEEADRVRsdayaeRERASEDANRLRREAQEETEAAKALAERtVSEAIAEAERLRSDASEYAQRVRTEASDTLASAe 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1783 WDLLREATDKTRDANRL--SAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVID-YVDDIKTKL 1859
Cdd:NF041483 891 QDAARTRADAREDANRIrsDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqLIAEATGEA 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1860 PPMSEELSDKIDDLAQEI-KDRRLAEKV-FQAESHAAQL-NDSSAVLDGILDEAKNISFN--ATAAFRAYSNIKDYIDEA 1934
Cdd:NF041483 971 ERLRAEAAETVGSAQQHAeRIRTEAERVkAEAAAEAERLrTEAREEADRTLDEARKDANKrrSEAAEQADTLITEAAAEA 1050
|
330
....*....|....*
gi 568965053 1935 EKVAREAKELAQGAT 1949
Cdd:NF041483 1051 DQLTAKAQEEALRTT 1065
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1056-1104 |
7.12e-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: 56.21 E-value: 7.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDC 1104
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
962-1006 |
2.16e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 2.16e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568965053 962 PCNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNFQEGG 1006
Cdd:cd00055 1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-912 |
3.29e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.28 E-value: 3.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 860 PCQCNDNldYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVNAKNCQ 912
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1416-1462 |
3.58e-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: 3.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568965053 1416 CQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIVRGLPNDC 1462
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1102-1159 |
6.25e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.51 E-value: 6.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGC 1159
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1056-1098 |
9.95e-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: 52.74 E-value: 9.95e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568965053 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPL 1098
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
963-1010 |
1.05e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.05e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 963 CNCNSFGSKSFDCEAS-GQCWCQPGVAGKKCDRCAHGYFNFQEGGCIAC 1010
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1415-1463 |
1.30e-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: 52.74 E-value: 1.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568965053 1415 PCQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIvRGLPNDCQ 1463
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1009-1054 |
1.70e-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: 52.36 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568965053 1009 ACDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGH-SIVTGCK 1054
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1010-1048 |
2.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568965053 1010 CDCS---HLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHS 1048
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
465-511 |
4.18e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 4.18e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGC 511
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1010-1053 |
4.89e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 4.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 1010 CDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGC 1053
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
410-467 |
6.06e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 6.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 410 CHCDPTGSLSEVCVKDekyaqrglkPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNC 467
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
752-801 |
6.09e-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: 50.82 E-value: 6.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 752 PCQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRgsPEDCQ 801
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1523-1560 |
8.25e-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: 8.25e-08
10 20 30
....*....|....*....|....*....|....*...
gi 568965053 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWH 1560
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1523-1566 |
9.10e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 568965053 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAE 1566
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1056-1097 |
9.46e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568965053 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYP 1097
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1523-1558 |
1.39e-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: 1.39e-07
10 20 30
....*....|....*....|....*....|....*.
gi 568965053 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEH 1558
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
753-800 |
1.70e-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: 49.27 E-value: 1.70e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 753 CQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTrGSPEDC 800
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1682-1881 |
2.07e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 53.60 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1682 VQDAEA-INEKAVQLNETLGNQDktaERNLEELQKEIDRMLKEL-----RSKDLQTQ-KEVAEDELVAAEGLLKRVNKLf 1754
Cdd:cd00176 9 ADELEAwLSEKEELLSSTDYGDD---LESVEALLKKHEALEAELaaheeRVEALNELgEQLIEEGHPDAEEIQERLEEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1755 gepraqnEDMEKDLQQKLAEYKNKLDDAWDLLRE----------ATDKTRDANRLSAAnqKNMTILETKKEAIEGSKRQI 1824
Cdd:cd00176 85 -------NQRWEELRELAEERRQRLEEALDLQQFfrdaddleqwLEEKEAALASEDLG--KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568965053 1825 ENTLKEGNDILDEANRLLGEINSviDYVDDIKTKLppmsEELSDKIDDLAQEIKDRR 1881
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKL----EELNERWEELLELAEERQ 206
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1102-1159 |
2.07e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 2.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGldaKNPLGC 1159
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1102-1159 |
3.19e-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: 48.50 E-value: 3.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGlDAKNPLGC 1159
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-904 |
3.52e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 568965053 861 CQCNdnLDYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 904
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
409-461 |
9.11e-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: 47.35 E-value: 9.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 409 PCHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHGYPD 461
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
861-907 |
1.57e-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: 46.58 E-value: 1.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 861 CQCNDNLDYSipGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVN 907
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1664-1944 |
3.08e-06 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 51.53 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1664 AERTNSRAESLEEFIKGLvQDAEAINEKAVQLNE----TLGNQDKTAERN----LEELQKEIDRMLKELR--SKDLQT-Q 1732
Cdd:NF033928 79 ARNIVVTGNPIIDLINEM-PIIKRGDLTEEELSElppiPLSSDDKEIVKElkeiLEDLKNDIKDYQQKADdvKKELDDfE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1733 KEVAEDELVAAEGLLKRVNKLFGEP-----RAQNEDMEKDLQQKLAEYKNKLDDAWdllreatdktrdanrlSAANQKN- 1806
Cdd:NF033928 158 NDLREELLPQLKLKKKLYDDNLGSDsieelREKIDQLEKEIEQLNKEYDDYVKLSF----------------TGLAGGPi 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1807 -----MTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKlppMSEELS--DKIDDLAQEIkd 1879
Cdd:NF033928 222 glaitGGIFGSKAEKIRKEKNALIQEIDELQEQLKKKNALLGSLERLQTSLDDILTR---MEDALPalKKLKGVWQSL-- 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568965053 1880 rrlaekvfqaeshAAQLNDSSAVLDGILDEAKNISFNAtaafraysNIKDYIDEAEKVAREAKEL 1944
Cdd:NF033928 297 -------------LTDIDSSINALKEIDDADSLRLFKL--------EFEQVIAPWKEIQDYAKQL 340
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1416-1453 |
3.67e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 3.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568965053 1416 CQCNG---HSSQCDPETSVCQnCQHHTAGDFCERCALGYYG 1453
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
410-460 |
7.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 7.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 410 CHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHGYP 460
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-512 |
8.88e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.65 E-value: 8.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 464 PCNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQkGCE 512
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
753-795 |
1.48e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 1.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568965053 753 CQCF---AHAEACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRG 795
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-330 |
6.46e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.96 E-value: 6.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 283 CICYGHARACPL-DPATnkSRCECEHNTCGESCDRCCPGFHQKPWRAGT 330
Cdd:cd00055 2 CDCNGHGSLSGQcDPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
818-859 |
7.13e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.96 E-value: 7.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568965053 818 CHLDRSLGLICD------ECPIGYTGPRCERCAEGYFGQPSIPGGsCQ 859
Cdd:cd00055 4 CNGHGSLSGQCDpgtgqcECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1764-1947 |
9.76e-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: 46.07 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1764 MEKDLQQ--KLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRL 1841
Cdd:COG1579 2 MPEDLRAllDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1842 LGEINSVIDYvddiktklppmsEELSDKIDDLAQEIKDR--RLAEKVFQAESHAAQLNDSSAVLDGILDEAKnisfNATA 1919
Cdd:COG1579 82 LGNVRNNKEY------------EALQKEIESLKRRISDLedEILELMERIEELEEELAELEAELAELEAELE----EKKA 145
|
170 180
....*....|....*....|....*...
gi 568965053 1920 AFRAysNIKDYIDEAEKVAREAKELAQG 1947
Cdd:COG1579 146 ELDE--ELAELEAELEELEAEREELAAK 171
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
818-858 |
1.48e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.18 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 818 CHLDRSLGLICD------ECPIGYTGPRCERCAEGYFGQPSIPGGSC 858
Cdd:pfam00053 3 CNPHGSLSDTCDpetgqcLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
465-506 |
2.10e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 568965053 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQED 506
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
803-851 |
3.33e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 3.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 803 CACPlniPSNNFSPTCHLDrslGLICdECPIGYTGPRCERCAEGYFGQP 851
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1465-1520 |
5.48e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 5.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568965053 1465 CACPLISPSnnfSPSCVLEGledYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1520
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1375-1403 |
2.56e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 37.72 E-value: 2.56e-03
10 20
....*....|....*....|....*....
gi 568965053 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-326 |
3.31e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 3.31e-03
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1375-1403 |
3.53e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.33 E-value: 3.53e-03
10 20
....*....|....*....|....*....
gi 568965053 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1707-1792 |
5.56e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.08 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1707 ERNLEELQKEIDRMLKELRSKD----------LQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEyk 1776
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDlgkdlesveaLLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE-- 81
|
90
....*....|....*.
gi 568965053 1777 nkLDDAWDLLREATDK 1792
Cdd:smart00150 82 --LNERWEELKELAEE 95
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1464-1521 |
9.13e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 36.18 E-value: 9.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1464 PCACPLISpsnNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1521
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1465-1513 |
9.40e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 35.75 E-value: 9.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 1465 CACPlisPSNNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSP 1513
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG---QCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1589-1848 |
8.28e-106 |
|
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: 338.62 E-value: 8.28e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1589 TMNIN-LTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERT 1667
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1668 NSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLL 1747
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1748 KRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENT 1827
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 568965053 1828 LKEGNDILDEANRLLGEINSV 1848
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-281 |
7.45e-91 |
|
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: 295.04 E-value: 7.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 29 AHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVpgqpVRNPQCRICNQNssNPYQRHPITNAIDGKN----T 104
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHT----EQGKKCDYCDAR--NPRRSHPAENLTDGNNpnnpT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 105 WWQSPSIKNGVeyHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLDDVEYKPWQYHAvtdTECLTLYNIyPRTGP 184
Cdd:smart00136 75 WWQSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGR-PPRGP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 185 PSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDP--SPELLEFTSARYIRLRFQRIRTLNADLMMfahkdpreI 262
Cdd:smart00136 148 ITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELMD--------D 219
|
250
....*....|....*....
gi 568965053 263 DPIVTRRYYYSVKDISVGG 281
Cdd:smart00136 220 RPEVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-281 |
4.94e-86 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 281.01 E-value: 4.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 35 LFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQpvrnpQCRICNqnSSNPYQRHPITNAIDGKN----TWWQSPS 110
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNgtneTWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 111 IKngVEYHYVTITLDLQQVFQIAYVIVKAAnSPRPGNWILERSLD-DVEYKPWQYHAvtdTECLTLYNIypRTGPPSYAK 189
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGR--PSGPSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 190 DDEVICTSFYSKIHPLENGEIHISLINGRPSA--DDPSPELLEFTSARYIRLRFQRIRTLNadlmmfahkDPREIDPIVT 267
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLG---------DELLDDPSVL 216
|
250
....*....|....
gi 568965053 268 RRYYYSVKDISVGG 281
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| LamB |
smart00281 |
Laminin B domain; |
1225-1360 |
3.35e-47 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 165.51 E-value: 3.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1225 HLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDEtGFATYKPQVIIRGGtptHARIITRHMAAPLIGQLTRHEIEMTE 1304
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGN---GLRISHPAEGPPLPDELTTVEVRFRE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568965053 1305 KEWKYYGddpriSRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEP 1360
Cdd:smart00281 77 ENWQYYG-----GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1230-1374 |
7.35e-45 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.97 E-value: 7.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1230 YWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGtptHARIITRHMA--APLIGQLTRHEIEMTEKEW 1307
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGN---GLRLSYSSPDqpPPDPGQEQTYSVRLHEENW 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568965053 1308 KYygddpRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGhvlAGSPPAHLIE 1374
Cdd:pfam00052 78 RD-----SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG---GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
579-718 |
2.47e-39 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 143.18 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 579 YWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTekILQLMIIFEGNDLRISTAYKE-VYLEPSEEHIEEVSLKEEAFT 657
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSL--NSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568965053 658 iHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVPYPTDRRiATDVE 718
Cdd:pfam00052 79 -DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQV-SLSNVSLDSAVPGGSGPP-ASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
578-706 |
1.95e-33 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 125.84 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 578 YYWSAPPPYLGNRLPAVGGQLSFTISYdleEEEDDTEKILQLMIIFEGNDLRISTAYkEVYLEPSEEHIEEVSLKEEAFT 657
Cdd:smart00281 5 VYWVAPEQFLGDKVTSYGGKLRYTLSF---DGRRGGTHVSAPDVILEGNGLRISHPA-EGPPLPDELTTVEVRFREENWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568965053 658 IHGTNlPVTRKDFMIVLTNLERVLMQITYNLGMDAIfRLSSVNLESAVP 706
Cdd:smart00281 81 YYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGS-RLSDVSLEVAVP 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1610-1943 |
2.32e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1610 NTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQD----- 1684
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqls 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1685 ---AEAINEKAVQLNETLGNQD--KTAERNLEELQKEID----------RMLKELRsKDLQTQKEVAEDELVAAEGLLKR 1749
Cdd:TIGR02168 754 kelTELEAEIEELEERLEEAEEelAEAEAEIEELEAQIEqlkeelkalrEALDELR-AELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1750 VnklfGEPRAQNEDME---KDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIEN 1826
Cdd:TIGR02168 833 I----AATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1827 TLKEGNDILDEANRLLGEINSVIDyvdDIKTKLPPMSEELSDKIDDLAQEIkdrrlAEKVFQAESHAAQLNDSSAVLDGI 1906
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEA-----EALENKIEDDEEEARRRLKRLENK 980
|
330 340 350
....*....|....*....|....*....|....*..
gi 568965053 1907 LDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKE 1943
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
913-960 |
4.18e-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: 62.37 E-value: 4.18e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 913 PCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQL-GRGC 960
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1608-1879 |
5.54e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATK-------VTADGEQTGQDAERTNSRAESLEEFIKG 1680
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelaeAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1681 LVQDAEAINEKAVQLNETLG---NQDKTAERNLEELQKEIDRMLKELRS-----KDLQTQKEVAEDELvaaEGLLKRVNK 1752
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIESlaaeiEELEELIEELESEL---EALLNERAS 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1753 LFGEPRAQNEDMEkDLQQKLAEYKNKLDDAWDLLREATDKTRDAN-RLSAANQKNMTILE--------------TKKEAI 1817
Cdd:TIGR02168 885 LEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRIDNLQErlseeysltleeaeALENKI 963
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568965053 1818 EGSKRQIENTLKEGNDILDEanrlLGEIN-SVIDYVDDIKTKLppmsEELSDKIDDLAQEIKD 1879
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKE----LGPVNlAAIEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1608-1943 |
1.00e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQELKHLLSPQRAPerlIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:PRK02224 319 LEDRDEELRDRLEECRVA---AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1688 INEKAVQLNETLGNqdktAERNLEELQKEIDRM---LKELRSkDLQTQKE-VAEDELVAAEGllK------------RVN 1751
Cdd:PRK02224 396 LRERFGDAPVDLGN----AEDFLEELREERDELrerEAELEA-TLRTARErVEEAEALLEAG--KcpecgqpvegspHVE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1752 KLfGEPRAQNEDMEKDLQQ---KLAEYKNKLDDAWDLLREATDKTRDANRLSAANQknmtILETKKEAIEGSKRQIENTL 1828
Cdd:PRK02224 469 TI-EEDRERVEELEAELEDleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEE----LIAERRETIEEKRERAEELR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1829 KEGNDILDEA------------------------NRLLGEINSVIDYVDDIktklppmsEELSDKIDDLAQEIKDRR--- 1881
Cdd:PRK02224 544 ERAAELEAEAeekreaaaeaeeeaeeareevaelNSKLAELKERIESLERI--------RTLLAAIADAEDEIERLRekr 615
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568965053 1882 --LAEKVFQAESHAAQLNDSSAVLDGILDEAknisfNATAAFRAYSNIKDYIDEAEKVAREAKE 1943
Cdd:PRK02224 616 eaLAELNDERRERLAEKRERKRELEAEFDEA-----RIEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1635-1912 |
3.90e-11 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 66.09 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1635 NVNTLVMETNELLTRATKVTadgEQTGQDAERTNSRAESLEEF----------IKGLVQDAEAINEKAVQLNETLgnQDK 1704
Cdd:COG1340 2 KTDELSSSLEELEEKIEELR---EEIEELKEKRDELNEELKELaekrdelnaqVKELREEAQELREKRDELNEKV--KEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1705 TAERNleELQKEIDRMLKELRSKDLQTQKEVAEDELVAAegLLKRVNKLfgEPRAQNEDM----EKDLQQKLAEYKNKLD 1780
Cdd:COG1340 77 KEERD--ELNEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERL--EWRQQTEVLspeeEKELVEKIKELEKELE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1781 DAwdllREATDKTRDANRLSAAnqknmtiLETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLP 1860
Cdd:COG1340 151 KA----KKALEKNEKLKELRAE-------LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568965053 1861 PMSE---ELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKN 1912
Cdd:COG1340 220 EAQEkadELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
914-960 |
4.26e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.67 E-value: 4.26e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQ--LGRGC 960
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
914-960 |
7.77e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 7.77e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 914 CRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQlGRGC 960
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG-PPGC 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1638-1909 |
9.35e-11 |
|
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: 67.40 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1638 TLVMETNE----LLTRATKVTADGE-------QTG----------------QDAERTNSRAESLEEFIKGLVQDAEAINE 1690
Cdd:TIGR02169 623 TLVVEDIEaarrLMGKYRMVTLEGElfeksgaMTGgsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRRIEN 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1691 KAVQLNETLgnqdKTAERNLEELQKEIDRMLKEL-----RSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEP-------R 1758
Cdd:TIGR02169 703 RLDELSQEL----SDASRKIGEIEKEIEQLEQEEeklkeRLEELEEDLSSLEQEIENVKSELKELEARIEELeedlhklE 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1759 AQNEDMEKDL-QQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDE 1837
Cdd:TIGR02169 779 EALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1838 ANRLLGEINSVIdyvDDIKTKLPPMSEELSD---KIDDL-----AQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDE 1909
Cdd:TIGR02169 859 LNGKKEELEEEL---EELEAALRDLESRLGDlkkERDELeaqlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1609-1934 |
1.36e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.58 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1609 ENTTQELKHLLSPQrapERLIQlaegNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRA----------------- 1671
Cdd:TIGR04523 306 QDWNKELKSELKNQ---EKKLE----EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKqreleekqneieklkke 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1672 -ESLEEFIKGLVQDAEAIN---EKAVQLNETLGNQDKTAERNLEELQKEIDRmLKELRSKDLQTQKEVaEDELVAAEGLL 1747
Cdd:TIGR04523 379 nQSYKQEIKNLESQINDLEskiQNQEKLNQQKDEQIKKLQQEKELLEKEIER-LKETIIKNNSEIKDL-TNQDSVKELII 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1748 KRVNKLFGEPRAQNEDMEK-------DLQQKLAEYKNKLDDAWDLLREATD---KTRDANRLSAANQKNMTILETKKEAI 1817
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRsinkikqNLEQKQKELKSKEKELKKLNEEKKEleeKVKDLTKKISSLKEKIEKLESEKKEK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1818 EGSKRQIENTLKEGNDILDEANrLLGEINSVIDYVDDIK---TKLPPMSEELSDKIDDLAQEIKD--RRLAEKVFQAESH 1892
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKEN-LEKEIDEKNKEIEELKqtqKSLKKKQEEKQELIDQKEKEKKDliKEIEEKEKKISSL 615
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568965053 1893 AAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEA 1934
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-1883 |
1.80e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1609 ENTTQELKHLLSPQRAPERLIQlAEGNVNTLVMETNELLTRATKVTADGEQtgqDAERTNSRAESLEEFIKGLVQDAEAI 1688
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIK-RTENIEELIKEKEKELEEVLREINEISS---ELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1689 NEKAVQLNETLGNQdktaeRNLEELQKEIDRMLKELRSKDLQTQKEVAE-DELvaaEGLLKRVNKLfGEPRAQNEDMEKD 1767
Cdd:PRK03918 241 EELEKELESLEGSK-----RKLEEKIRELEERIEELKKEIEELEEKVKElKEL---KEKAEEYIKL-SEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1768 LQQKLAEYKNKLDDAWDLLREATDKTRDANRLSaanqKNMTILETKKEAIEGSKRQIEnTLKEgndILDEANRL------ 1841
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEERHELYE-EAKA---KKEELERLkkrltg 383
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568965053 1842 --LGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLA 1883
Cdd:PRK03918 384 ltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
963-1007 |
2.46e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 2.46e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568965053 963 CNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNFQEGGC 1007
Cdd:smart00180 1 CDCDPGGSASGTCDPdTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1632-1949 |
2.68e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 66.00 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1632 AEGNVNTLVMETNElltRATKVTADGEQTGQDA-ERTNSRAESLEEFIKGLVQDAEainekavqlnetlgnqdKTAERNL 1710
Cdd:NF041483 751 AQAEAQRLVEEADR---RATELVSAAEQTAQQVrDSVAGLQEQAEEEIAGLRSAAE-----------------HAAERTR 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1711 EELQKEIDRML------KELRSKDLQTQKEVAEDELVAAEGLLKR-VNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDA- 1782
Cdd:NF041483 811 TEAQEEADRVRsdayaeRERASEDANRLRREAQEETEAAKALAERtVSEAIAEAERLRSDASEYAQRVRTEASDTLASAe 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1783 WDLLREATDKTRDANRL--SAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVID-YVDDIKTKL 1859
Cdd:NF041483 891 QDAARTRADAREDANRIrsDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqLIAEATGEA 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1860 PPMSEELSDKIDDLAQEI-KDRRLAEKV-FQAESHAAQL-NDSSAVLDGILDEAKNISFN--ATAAFRAYSNIKDYIDEA 1934
Cdd:NF041483 971 ERLRAEAAETVGSAQQHAeRIRTEAERVkAEAAAEAERLrTEAREEADRTLDEARKDANKrrSEAAEQADTLITEAAAEA 1050
|
330
....*....|....*
gi 568965053 1935 EKVAREAKELAQGAT 1949
Cdd:NF041483 1051 DQLTAKAQEEALRTT 1065
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1646-1839 |
3.74e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1646 LLTRATKVTADGEQTGQDAE--RTNSRAESLEEFIKGLVQDAEAINEKAVQLN---ETLGNQDKTAERNLEELQKEIDRM 1720
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQaelEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1721 LKEL--RSKDLQTQKEVAE--DELVAAEG---LLKRVNKLFGEPRAQNEDME--KDLQQKLAEYKNKLDDAWDLLR---- 1787
Cdd:COG3883 85 REELgeRARALYRSGGSVSylDVLLGSESfsdFLDRLSALSKIADADADLLEelKADKAELEAKKAELEAKLAELEalka 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568965053 1788 EATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEAN 1839
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1646-1943 |
4.39e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1646 LLTRATKVTADGEQTGQ----DAERTNSRAESLEEFIKGLVQ-DAEA-INEKAVQLNETlgnqDKTAERNLEELQKEIDR 1719
Cdd:PRK02224 82 HIERRVRLSGDRATTAKcvleTPEGTIDGARDVREEVTELLRmDAEAfVNCAYVRQGEV----NKLINATPSDRQDMIDD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1720 MLKELRskdLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDME-KDLQQKLAEYKNKLDDAWDLL------REATDK 1792
Cdd:PRK02224 158 LLQLGK---LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIeryeeqREQARE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1793 TRDA--NRLSAANQKNMTIlETKKEAIEGSKRQIENTLKEGNDILDE-------ANRLLGEINSVIDYVD----DIKTkL 1859
Cdd:PRK02224 235 TRDEadEVLEEHEERREEL-ETLEAEIEDLRETIAETEREREELAEEvrdlrerLEELEEERDDLLAEAGlddaDAEA-V 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1860 PPMSEELSDKIDDLAQEIKDRRLAEKVF--QAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKV 1937
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAHneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
....*.
gi 568965053 1938 AREAKE 1943
Cdd:PRK02224 393 IEELRE 398
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1657-1954 |
4.62e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.77 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1657 GEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQlnetlgnQDKTAERNLEELQKEIDRMLKELRSkdLQTQKEVA 1736
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALF-------ELDKLQEELEQLREELEQAREELEQ--LEEELEQA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1737 EDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEA 1816
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1817 IEGSKRQIENT------LKEGNDILDEA------NRLLGEINSVIDYVdDIKTKLPPMSEELSDKIDDLAQEIKDRRLAE 1884
Cdd:COG4372 152 LKELEEQLESLqeelaaLEQELQALSEAeaeqalDELLKEANRNAEKE-EELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1885 KVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLVYF 1954
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1699-1946 |
5.84e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1699 LGNQDKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDELVAAEGLLKRVNKlfgEPRAQNEDMEKDLQQKLAEYKNK 1778
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEEL--EKLTEEISELEKRLEEIEQLLEELNK---KIKDLGEEEQLRVKEKIGELEAE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1779 LDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGS-------KRQIENTLKEGNDILDEANRLLGEINS---- 1847
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkrRDKLTEEYAELKEELEDLRAELEEVDKefae 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1848 VIDYVDDIKTKLppmsEELSDKIDDLAQEIkdRRLAEKVFQAESHAAQLNDSSAVLdgildEAKNISFNATAafraysni 1927
Cdd:TIGR02169 383 TRDELKDYREKL----EKLKREINELKREL--DRLQEELQRLSEELADLNAAIAGI-----EAKINELEEEK-------- 443
|
250
....*....|....*....
gi 568965053 1928 KDYIDEAEKVAREAKELAQ 1946
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAA 462
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1056-1104 |
7.12e-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: 56.21 E-value: 7.12e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDC 1104
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1628-1956 |
9.71e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1628 LIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERT-------NSRAESLEEFIKGLVQDAEAINEKAVQLNETLg 1700
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeleqaRSELEQLEEELEELNEQLQAAQAELAQAQEEL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1701 nqdKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDElvaaeglLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKnKLD 1780
Cdd:COG4372 104 ---ESLQEEAEELQEELEELQKER--QDLEQQRKQLEAQ-------IAELQSEIAEREEELKELEEQLESLQEELA-ALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1781 DAWDLLREATDKTRDANRLSAANQKNMTILETKK--EAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTK 1858
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEaeKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1859 LPPMSEELSDKIDDLAQEIKDRRLAEKV---FQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAE 1935
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELeiaALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
330 340
....*....|....*....|.
gi 568965053 1936 KVAREAKELAQGATKLVYFQF 1956
Cdd:COG4372 331 ALAILLAELADLLQLLLVGLL 351
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1701-1901 |
1.04e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1701 NQDKTAERNLEELQKEIDRMLKELRS-----KDLQTQKEVAEDELVAAEGLLKRVNKLFGEPR---AQNEDMEKDLQQKL 1772
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAlkkeeKALLKQLAALERRIAALARRIRALEQELAALEaelAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1773 AE------------YKNKLDDAWDLL---REATDKTRDA---NRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDI 1834
Cdd:COG4942 100 EAqkeelaellralYRLGRQPPLALLlspEDFLDAVRRLqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1835 LDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKD-RRLAEKVFQAESHAAQLNDSSA 1901
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAG 247
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
962-1006 |
2.16e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 2.16e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568965053 962 PCNCNSFGSKSFDCEA-SGQCWCQPGVAGKKCDRCAHGYFNFQEGG 1006
Cdd:cd00055 1 PCDCNGHGSLSGQCDPgTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1684-1830 |
3.22e-09 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 57.31 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1684 DAEAINEKAVQLNEtlgnQDKTAERNLEELQKEIdrmlkelrsKDLQTQKEVAEDELVAAEGLLKRVNKLFGEP---RAQ 1760
Cdd:pfam12718 8 EAENAQERAEELEE----KVKELEQENLEKEQEI---------KSLTHKNQQLEEEVEKLEEQLKEAKEKAEESeklKTN 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1761 NEDMEKDLQQkLAEyknKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKE 1830
Cdd:pfam12718 75 NENLTRKIQL-LEE---ELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
860-912 |
3.29e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.28 E-value: 3.29e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 860 PCQCNDNldYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVNAKNCQ 912
Cdd:cd00055 1 PCDCNGH--GSLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1416-1462 |
3.58e-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: 3.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568965053 1416 CQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIVRGLPNDC 1462
Cdd:pfam00053 1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1658-1884 |
5.21e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1658 EQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLnETLGNQDKTAERNLEELQKEI-----------DRMLKELRS 1726
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAELLKELeelgfesveelEERLKELEP 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1727 ------------KDLQTQKE---VAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKlaEYKNKLDDAWDLLREatd 1791
Cdd:PRK03918 600 fyneylelkdaeKELEREEKelkKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRE--- 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1792 ktrdanrLSAanqknmtiLETKKEAIEGSKRQIENTLKEgndiLDEAnrlLGEINSVIDYVDDIKTKLPPMsEELSDKID 1871
Cdd:PRK03918 675 -------LAG--------LRAELEELEKRREEIKKTLEK----LKEE---LEEREKAKKELEKLEKALERV-EELREKVK 731
|
250
....*....|...
gi 568965053 1872 DLAQEIKDRRLAE 1884
Cdd:PRK03918 732 KYKALLKERALSK 744
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1102-1159 |
6.25e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.51 E-value: 6.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGC 1159
Cdd:pfam00053 1 CDCNPHGSLSDTCDPET---------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1665-1909 |
6.48e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1665 ERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLgnqdktaernlEELQKEIDRM-----------LKELRSK--DLQT 1731
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLL-----------EELNKKIKDLgeeeqlrvkekIGELEAEiaSLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1732 QKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEyKNKLDDAWDLLREATDKTR-DANRLSAANQKNMTIL 1810
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRaELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1811 ETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDL-AQEIKDRRLAEKVFQA 1889
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkKQEWKLEQLAADLSKY 467
|
250 260
....*....|....*....|
gi 568965053 1890 EShaaQLNDSSAVLDGILDE 1909
Cdd:TIGR02169 468 EQ---ELYDLKEEYDRVEKE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-1913 |
9.37e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1626 ERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNqdkt 1705
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1706 AERNLEELQKEIDRMLKELRskDLQTQKEVAEDELVAAEGLLKRVNKLfgepRAQNEDMEKDLQQKLAEYKNKLDDAWDL 1785
Cdd:COG1196 314 LEERLEELEEELAELEEELE--ELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1786 LREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEE 1865
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568965053 1866 LSDKIDDLAQEIKDRR--LAEKVFQAESHAAQLNDSSAVLDGILDEAKNI 1913
Cdd:COG1196 468 LLEEAALLEAALAELLeeLAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1701-1943 |
9.49e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.77 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1701 NQDKTAERNLEELQKEIDRMLKELRS-KDLQTQ-----KEVAE--DELVAaegllkRVNKLFGEPRAQNEDMeKDLQQKL 1772
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEElKEKRDElneelKELAEkrDELNA------QVKELREEAQELREKR-DELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1773 AEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIEN---TLKEGNDILDEANRLLGEINsvi 1849
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKELE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1850 dyvddiKTKlppMSEELSDKIDDLAQEIKDRRLaekvfQAESHAAQLNDSSavldgilDEAKNISFNATAAFRAYSNIKD 1929
Cdd:COG1340 151 ------KAK---KALEKNEKLKELRAELKELRK-----EAEEIHKKIKELA-------EEAQELHEEMIELYKEADELRK 209
|
250
....*....|....
gi 568965053 1930 YIDEAEKVAREAKE 1943
Cdd:COG1340 210 EADELHKEIVEAQE 223
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1708-1884 |
9.60e-09 |
|
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: 58.01 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1708 RNLEELQkEIDRMLKELRS--KDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDME---KDLQQKLAEYKNKLDDA 1782
Cdd:COG1579 7 RALLDLQ-ELDSELDRLEHrlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1783 WD------LLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIdyvddik 1856
Cdd:COG1579 86 RNnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL------- 158
|
170 180
....*....|....*....|....*...
gi 568965053 1857 tklppmsEELSDKIDDLAQEIKDRRLAE 1884
Cdd:COG1579 159 -------EELEAEREELAAKIPPELLAL 179
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1056-1098 |
9.95e-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: 52.74 E-value: 9.95e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568965053 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPL 1098
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
963-1010 |
1.05e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.05e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 963 CNCNSFGSKSFDCEAS-GQCWCQPGVAGKKCDRCAHGYFNFQEGGCIAC 1010
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1415-1463 |
1.30e-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: 52.74 E-value: 1.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568965053 1415 PCQCNGHSS---QCDPETSVCQnCQHHTAGDFCERCALGYYGIvRGLPNDCQ 1463
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1009-1054 |
1.70e-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: 52.36 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568965053 1009 ACDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGH-SIVTGCK 1054
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1010-1048 |
2.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568965053 1010 CDCS---HLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHS 1048
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1660-1841 |
3.53e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1660 TGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNEtlgnqdktAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDE 1739
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1740 LVAAEGLLK----RVNKLFG--EPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREAT-----DKTRDANRLSAANQKNMT 1808
Cdd:COG4717 134 LEALEAELAelpeRLEELEErlEELRELEEELEELEAELAELQEELEELLEQLSLATeeelqDLAEELEELQQRLAELEE 213
|
170 180 190
....*....|....*....|....*....|...
gi 568965053 1809 ILETKKEAIEGSKRQIENtLKEGNDILDEANRL 1841
Cdd:COG4717 214 ELEEAQEELEELEEELEQ-LENELEAAALEERL 245
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
465-511 |
4.18e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.20 E-value: 4.18e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGC 511
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1010-1053 |
4.89e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 4.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 1010 CDCSHLG---NNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGC 1053
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
410-467 |
6.06e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.81 E-value: 6.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 410 CHCDPTGSLSEVCVKDekyaqrglkPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNC 467
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
752-801 |
6.09e-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: 50.82 E-value: 6.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 752 PCQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRgsPEDCQ 801
Cdd:cd00055 1 PCDCNGHGslsGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1607-1929 |
7.17e-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: 57.66 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1607 GLENTTQELKHLLSPQRAPERLIQLAEgNVNTLVMETNELLTratkvtadgEQTGQDAERTNSRAESLEEFIKGLVQDAE 1686
Cdd:COG5185 227 EIINIEEALKGFQDPESELEDLAQTSD-KLEKLVEQNTDLRL---------EKLGENAESSKRLNENANNLIKQFENTKE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1687 AINEK-----AVQLNETLGNQDKTAERN--LEELQKEIDRMLKELRSKDLQTQKEVAEDElvaaEGLLKRVNKLFGEPR- 1758
Cdd:COG5185 297 KIAEYtksidIKKATESLEEQLAAAEAEqeLEESKRETETGIQNLTAEIEQGQESLTENL----EAIKEEIENIVGEVEl 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1759 AQNEDMEKDLQQKLAEYKNKLDDAwdlLREATDKTRDANrlsAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEa 1838
Cdd:COG5185 373 SKSSEELDSFKDTIESTKESLDEI---PQNQRGYAQEIL---ATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNE- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1839 nrLLGEINSVIDYVDDIKT-----KLPPMSEELSDKIDDLAQEIKD--RRLAEKVFQAESHAAQLNDSSAVLDGILDEAK 1911
Cdd:COG5185 446 --LISELNKVMREADEESQsrleeAYDEINRSVRSKKEDLNEELTQieSRVSTLKATLEKLRAKLERQLEGVRSKLDQVA 523
|
330
....*....|....*...
gi 568965053 1912 NiSFNATAAFRAYSNIKD 1929
Cdd:COG5185 524 E-SLKDFMRARGYAHILA 540
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1523-1560 |
8.25e-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: 8.25e-08
10 20 30
....*....|....*....|....*....|....*...
gi 568965053 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWH 1560
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1523-1566 |
9.10e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 568965053 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAE 1566
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1056-1097 |
9.46e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 9.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568965053 1056 CNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYP 1097
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1707-1955 |
1.02e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 56.89 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1707 ERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAA-EGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDL 1785
Cdd:COG5185 218 ESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKlEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1786 LREATDK------TRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILD-------EANRLLGE-------- 1844
Cdd:COG5185 298 IAEYTKSidikkaTESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTEnleaikeEIENIVGEvelsksse 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1845 -INSVIDYVDDIKTKLPPMSEELSDKIDD----LAQEIK--DRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNI--SF 1915
Cdd:COG5185 378 eLDSFKDTIESTKESLDEIPQNQRGYAQEilatLEDTLKaaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVmrEA 457
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568965053 1916 NATAAFRAYSNIKDYIDEAEKVAREA-KELAQGATKLVYFQ 1955
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSKKEDLnEELTQIESRVSTLK 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1608-1945 |
1.32e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1688 INEKAVQLNETLgnqdKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKD 1767
Cdd:COG1196 328 LEEELEELEEEL----EELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1768 LQQKLAEYKNKLDdawDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINS 1847
Cdd:COG1196 402 LEELEEAEEALLE---RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1848 VidyvddiktklppmsEELSDKIDDLAQEIKDRRLAEKVFQAESH---AAQLNDSSAVLDGILDEAKNISFNATAAFRAY 1924
Cdd:COG1196 479 L---------------AELLEELAEAAARLLLLLEAEADYEGFLEgvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340
....*....|....*....|...
gi 568965053 1925 --SNIKDYIDEAEKVAREAKELA 1945
Cdd:COG1196 544 laAALQNIVVEDDEVAAAAIEYL 566
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1523-1558 |
1.39e-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: 1.39e-07
10 20 30
....*....|....*....|....*....|....*.
gi 568965053 1523 CECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEH 1558
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKP 36
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1602-1916 |
1.65e-07 |
|
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: 56.90 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1602 YKILYGLENTTQELKHLLSPQRAPERliqlaegnvntlvmETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGL 1681
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQELLRDEQ--------------EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1682 VQDAEAINEKAvqlNETLGNQDKTAERNLEELQKEIdrmlkELRSKDLQTQKEVAEdelvAAEGLLKRVNKlfgePRAQN 1761
Cdd:pfam02463 291 LAKEEEELKSE---LLKLERRKVDDEEKLKESEKEK-----KKAEKELKKEKEEIE----ELEKELKELEI----KREAE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1762 EDMEKDLQQKLAEYKNKLDDAWDLLREATDktrdaNRLSAANQKNMTILETKKEAIEgSKRQIENTLKEGNDILDEANRL 1841
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESE-----RLSSAAKLKEEELELKSEEEKE-AQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1842 LGEINSVIDYVDDIKTKLPPMSEELSD-------KIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNIS 1914
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEEKEELEKqelkllkDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
|
..
gi 568965053 1915 FN 1916
Cdd:pfam02463 509 LK 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1670-1944 |
1.66e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1670 RAESLEEF---IKGLVQDAEAINEKAVQLNETLGNQDKTAERN-----LEELQKEIDRMLKELRSKDLQTQKEVAEDelv 1741
Cdd:PRK03918 450 RKELLEEYtaeLKRIEKELKEIEEKERKLRKELRELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEE--- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1742 aAEGLLKRVNKLFGEPRAQNEDMEK--DLQQKLAEYKNKLDDAWDLLREATdktrdaNRLSAANQKNMTILETK-KEAIE 1818
Cdd:PRK03918 527 -YEKLKEKLIKLKGEIKSLKKELEKleELKKKLAELEKKLDELEEELAELL------KELEELGFESVEELEERlKELEP 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1819 GSKRQIE--NTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKD---RRLAEKVFQAESHA 1893
Cdd:PRK03918 600 FYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETEKRL----EELRKELEELEKKYSEeeyEELREEYLELSREL 675
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 1894 AQLNDSSAVLDGILDEAKnisfnataafRAYSNIKDYIDEAEKVAREAKEL 1944
Cdd:PRK03918 676 AGLRAELEELEKRREEIK----------KTLEKLKEELEEREKAKKELEKL 716
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
753-800 |
1.70e-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: 49.27 E-value: 1.70e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 753 CQCFAHA---EACDDITGECLnCKDHTGGPYCNECLPGFYGDPTrGSPEDC 800
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1682-1881 |
2.07e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 53.60 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1682 VQDAEA-INEKAVQLNETLGNQDktaERNLEELQKEIDRMLKEL-----RSKDLQTQ-KEVAEDELVAAEGLLKRVNKLf 1754
Cdd:cd00176 9 ADELEAwLSEKEELLSSTDYGDD---LESVEALLKKHEALEAELaaheeRVEALNELgEQLIEEGHPDAEEIQERLEEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1755 gepraqnEDMEKDLQQKLAEYKNKLDDAWDLLRE----------ATDKTRDANRLSAAnqKNMTILETKKEAIEGSKRQI 1824
Cdd:cd00176 85 -------NQRWEELRELAEERRQRLEEALDLQQFfrdaddleqwLEEKEAALASEDLG--KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568965053 1825 ENTLKEGNDILDEANRLLGEINSviDYVDDIKTKLppmsEELSDKIDDLAQEIKDRR 1881
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHP--DADEEIEEKL----EELNERWEELLELAEERQ 206
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1102-1159 |
2.07e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 49.23 E-value: 2.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGldaKNPLGC 1159
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1665-1946 |
2.29e-07 |
|
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: 56.13 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1665 ERTNSRAESLE--EFIKGlvqdaEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELva 1742
Cdd:pfam02463 154 RRLEIEEEAAGsrLKRKK-----KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1743 aegLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKtrdaNRLSAANQKNMTILETKKEAIEGSKR 1822
Cdd:pfam02463 227 ---LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE----NKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1823 QIENTLKEGNDILDEANRLLGEINSVIdyvdDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAV 1902
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568965053 1903 LDGILDEAKNISfnatAAFRAYSNIKDYIDEAEKVAREAKELAQ 1946
Cdd:pfam02463 376 LAKKKLESERLS----SAAKLKEEELELKSEEEKEAQLLLELAR 415
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1608-1951 |
2.79e-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: 55.80 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQELKHLLSPQRAperLIQLAEGNVNTLVMETNELLTRAtkvtadgEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTT---EISNTQTQLNQLKDEQNKIKKQL-------SEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1688 INEKAVQ-LNETLGNQDKTAERNLEELQKEID-----------------RMLKELRSKDLQTQKEVAEDE---------- 1739
Cdd:TIGR04523 300 LNNQKEQdWNKELKSELKNQEKKLEEIQNQISqnnkiisqlneqisqlkKELTNSESENSEKQRELEEKQneieklkken 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1740 ---LVAAEGLLKRVNKLfgEPRAQN-EDMEKDLQQK---LAEYKNKLDDAWDLLREATDKTRD----------ANRLSAA 1802
Cdd:TIGR04523 380 qsyKQEIKNLESQINDL--ESKIQNqEKLNQQKDEQikkLQQEKELLEKEIERLKETIIKNNSeikdltnqdsVKELIIK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1803 NQKNMT-ILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIdyvddiktklppmsEELSDKIDDLAQEIKDrr 1881
Cdd:TIGR04523 458 NLDNTReSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK--------------KELEEKVKDLTKKISS-- 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1882 LAEKVFQAESHAAQLNDSsavLDGILDEAKNISFNATaafraYSNIKDYIDEAEKvarEAKELAQGATKL 1951
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESK---ISDLEDELNKDDFELK-----KENLEKEIDEKNK---EIEELKQTQKSL 580
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1102-1159 |
3.19e-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: 48.50 E-value: 3.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1102 CDCFLPGTDATTCDLETrkcscsdqtGQCSCKVNVEGVHCDRCRPGKFGlDAKNPLGC 1159
Cdd:cd00055 2 CDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
861-904 |
3.52e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 3.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 568965053 861 CQCNdnLDYSIPGSCDSLSGSCLiCKPGTTGRYCELCADGYFGD 904
Cdd:smart00180 1 CDCD--PGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1603-1951 |
4.41e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1603 KILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEF---IK 1679
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELekeLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1680 GLVQDAEAINEKAVQLNETLgNQDKTAERNLEELQKEID---------RMLKELRSKDLQTQKEVaEDELVAAEGLLKRV 1750
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKelkekaeeyIKLSEFYEEYLDELREI-EKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1751 NKLFGEPRAQNEDME------KDLQQKLAEYKNKLDdawdLLREATDKTRDANRLSAaNQKNMTI--LETKKEAIEGSKR 1822
Cdd:PRK03918 327 EERIKELEEKEERLEelkkklKELEKRLEELEERHE----LYEEAKAKKEELERLKK-RLTGLTPekLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1823 QIENTLKEgndILDEANRLLGEINSVIDYVDDIKT---KLPPMSEELSDK-----IDDLAQEIKdrRLAEKVFQAESHAA 1894
Cdd:PRK03918 402 EIEEEISK---ITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEhrkelLEEYTAELK--RIEKELKEIEEKER 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568965053 1895 QLNDSSAVLDGILDEAKNISFNATAA---FRAYSNIKDY-IDEAEKVAREAKELAQGATKL 1951
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAeqlKELEEKLKKYnLEELEKKAEEYEKLKEKLIKL 537
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1681-1898 |
5.56e-07 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 51.50 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1681 LVQDAEAINEKAVQLNETLGNQDKTAERNLEelqKEIDRMLKELRsKDLQTQKEvaedelvaaegllkrvnKLfgEPRAq 1760
Cdd:pfam01442 2 LEDSLDELSTYAEELQEQLGPVAQELVDRLE---KETEALRERLQ-KDLEEVRA-----------------KL--EPYL- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1761 nEDMEKDLQQKLAEYKNKLDDAWDLLREATdkTRDANRLSAAnqknmtiLETKKEAIEGSKRQIENTLKEG-NDILDEAN 1839
Cdd:pfam01442 58 -EELQAKLGQNVEELRQRLEPYTEELRKRL--NADAEELQEK-------LAPYGEELRERLEQNVDALRARlAPYAEELR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568965053 1840 RLLGEInsvidyVDDIKTKLPPMSEELSDKIDDLAQEIKDrrlaekvfQAESHAAQLND 1898
Cdd:pfam01442 128 QKLAER------LEELKESLAPYAEEVQAQLSQRLQELRE--------KLEPQAEDLRE 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1626-1913 |
5.64e-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: 54.64 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1626 ERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNetlgNQDKT 1705
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE----SEKKE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1706 AERNLEELQKEIDRMLKELRSKDLQT-----QKEVaeDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLd 1780
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKENLEKeidekNKEI--EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1781 daWDLLREATdKTRDANRLSAANQKNmtiLETKKEAIEGSKRQIENTLKEgndILDEANRLLGEINSVIDYVDDIkTKLp 1860
Cdd:TIGR04523 613 --SSLEKELE-KAKKENEKLSSIIKN---IKSKKNKLKQEVKQIKETIKE---IRNKWPEIIKKIKESKTKIDDI-IEL- 681
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 1861 pMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNI 1913
Cdd:TIGR04523 682 -MKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENI 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1673-1896 |
8.55e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1673 SLEEFIKGLVqdAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRS--------KDLQTQKEVAEDELVAAE 1744
Cdd:COG4717 38 TLLAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaelqeelEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1745 GLLKRVNKLFGEPRAQNEdmEKDLQQKLAEYKNKLDdawDLLREATDKTRDANRLSAANQKnmtiLETKKEAIEGSKRQI 1824
Cdd:COG4717 116 EELEKLEKLLQLLPLYQE--LEALEAELAELPERLE---ELEERLEELRELEEELEELEAE----LAELQEELEELLEQL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568965053 1825 EN-TLKEGNDILDEANRLLGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQL 1896
Cdd:COG4717 187 SLaTEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
409-461 |
9.11e-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: 47.35 E-value: 9.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 568965053 409 PCHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHGYPD 461
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1663-1888 |
1.10e-06 |
|
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: 52.76 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1663 DAERTNSRaESLEEFIKGLVQDAEAINEKAVQLNETLG---NQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEde 1739
Cdd:cd22656 109 DEELEEAK-KTIKALLDDLLKEAKKYQDKAAKVVDKLTdfeNQTEKDQTALETLEKALKDLLTD--EGGAIARKEIKD-- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1740 lvaaegLLKRVnklfgepraqnedmeKDLQQKLA-EYKNKLDDAWDLLREATDKTRDANRLSAanqknmtiletkkeAIE 1818
Cdd:cd22656 184 ------LQKEL---------------EKLNEEYAaKLKAKIDELKALIADDEAKLAAALRLIA--------------DLT 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1819 GSKRQIENTLkegnDILDEAnrlLGEINSVIDYVDDIKTKLppmsEELSDKIDDLAQEIKDRRLAEKVFQ 1888
Cdd:cd22656 229 AADTDLDNLL----ALIGPA---IPALEKLQGAWQAIATDL----DSLKDLLEDDISKIPAAILAKLELE 287
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
861-907 |
1.57e-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: 46.58 E-value: 1.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 861 CQCNDNLDYSipGSCDSLSGSCLiCKPGTTGRYCELCADGYFGDAVN 907
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1678-1951 |
2.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1678 IKGLVQDAEAiNEKAVQlnETLGNQD-KTAERNLEELQKEIDRMLKEL-----RSKDLQTQKEVAEDELvaaEGLLKRVN 1751
Cdd:PRK03918 137 IDAILESDES-REKVVR--QILGLDDyENAYKNLGEVIKEIKRRIERLekfikRTENIEELIKEKEKEL---EEVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1752 KLfgepraqnEDMEKDLQQKLAEYKNKLddawdllrEATDKTRdaNRLSAanqknmtiLETKKEAIEGSKRQIENTLKEG 1831
Cdd:PRK03918 211 EI--------SSELPELREELEKLEKEV--------KELEELK--EEIEE--------LEKELESLEGSKRKLEEKIREL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1832 NDILDEANRLLGEINSVIDYVDDIKTKLPPMSE--ELSDKIDDLAQEIKDR--RLAEKVFQAESHAAQLNDSSAVLDGIL 1907
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRlsRLEEEINGIEERIKELEEKEERLEELK 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568965053 1908 DEAKNISfnataafRAYSNIKDYIDEAEKVAREAKELAQGATKL 1951
Cdd:PRK03918 345 KKLKELE-------KRLEELEERHELYEEAKAKKEELERLKKRL 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1688-1950 |
2.71e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1688 INEKAVQLNEtLGNQDKTAERNLEELQKEIDRMLKELrsKDLQTQKEVAEDELVAAEGLLKRVNKLFgepRAQNEDMEKD 1767
Cdd:COG3883 18 IQAKQKELSE-LQAELEAAQAELDALQAELEELNEEY--NELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1768 LQqklAEYKNKLD-DAWDLLREATDKTRDANRLSAANQknmtILETkkeaiegskrqientlkeGNDILDEANRLLGEIN 1846
Cdd:COG3883 92 AR---ALYRSGGSvSYLDVLLGSESFSDFLDRLSALSK----IADA------------------DADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1847 SVIDYVDDIKtklppmsEELSDKIDDLAQEIKDrrLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSN 1926
Cdd:COG3883 147 AKKAELEAKL-------AELEALKAELEAAKAE--LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
250 260
....*....|....*....|....
gi 568965053 1927 IKDYIDEAEKVAREAKELAQGATK 1950
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
1664-1944 |
3.08e-06 |
|
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.
Pssm-ID: 468250 [Multi-domain] Cd Length: 340 Bit Score: 51.53 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1664 AERTNSRAESLEEFIKGLvQDAEAINEKAVQLNE----TLGNQDKTAERN----LEELQKEIDRMLKELR--SKDLQT-Q 1732
Cdd:NF033928 79 ARNIVVTGNPIIDLINEM-PIIKRGDLTEEELSElppiPLSSDDKEIVKElkeiLEDLKNDIKDYQQKADdvKKELDDfE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1733 KEVAEDELVAAEGLLKRVNKLFGEP-----RAQNEDMEKDLQQKLAEYKNKLDDAWdllreatdktrdanrlSAANQKN- 1806
Cdd:NF033928 158 NDLREELLPQLKLKKKLYDDNLGSDsieelREKIDQLEKEIEQLNKEYDDYVKLSF----------------TGLAGGPi 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1807 -----MTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKlppMSEELS--DKIDDLAQEIkd 1879
Cdd:NF033928 222 glaitGGIFGSKAEKIRKEKNALIQEIDELQEQLKKKNALLGSLERLQTSLDDILTR---MEDALPalKKLKGVWQSL-- 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568965053 1880 rrlaekvfqaeshAAQLNDSSAVLDGILDEAKNISFNAtaafraysNIKDYIDEAEKVAREAKEL 1944
Cdd:NF033928 297 -------------LTDIDSSINALKEIDDADSLRLFKL--------EFEQVIAPWKEIQDYAKQL 340
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1605-1954 |
3.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1605 LYGLENTTQELKHLLspQRAPERLIQLAEGnvntlVMETNELLTRATKVTADGEQTGQDAERT-NSRAESLEEFIKGLVQ 1683
Cdd:COG4717 127 LLPLYQELEALEAEL--AELPERLEELEER-----LEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1684 DAEAINEKAVQLNETLgnqdKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLL---------------- 1747
Cdd:COG4717 200 ELEELQQRLAELEEEL----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglggsllslilti 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1748 ------------------KRVNKLFGEP--RAQNEDMEKDLQQK-------------------LAEYKNKLDDAWDLLRE 1788
Cdd:COG4717 276 agvlflvlgllallflllAREKASLGKEaeELQALPALEELEEEeleellaalglppdlspeeLLELLDRIEELQELLRE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1789 ATDKTRDANR----------LSAANQKNMTILETK----------KEAIEGSKRQIENTLKEGNDILDEAN--RLLGEIN 1846
Cdd:COG4717 356 AEELEEELQLeeleqeiaalLAEAGVEDEEELRAAleqaeeyqelKEELEELEEQLEELLGELEELLEALDeeELEEELE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1847 SVIDYVDDIKTKLppmsEELSDKIDDLAQEIK----DRRLAEKVFQAESHAAQLND------SSAVLDGILDEAKNI--- 1913
Cdd:COG4717 436 ELEEELEELEEEL----EELREELAELEAELEqleeDGELAELLQELEELKAELRElaeewaALKLALELLEEAREEyre 511
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1914 ----SFNATAA--FR-----AYSNIkdYIDEAEKVA--------REAKELAQGATKLVYF 1954
Cdd:COG4717 512 erlpPVLERASeyFSrltdgRYRLI--RIDEDLSLKvdtedgrtRPVEELSRGTREQLYL 569
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1608-1887 |
3.58e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEA 1687
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1688 INEKAVQLNETLGNQDKT-AERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVA----------AEGLLKRVNKLFGE 1756
Cdd:COG4372 162 LQEELAALEQELQALSEAeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAeelleakdslEAKLGLALSALLDA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1757 PRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKnmtILETKKEAIEGSKRQIENTLKEGNDILD 1836
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE---AALELKLLALLLNLAALSLIGALEDALL 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 1837 EANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVF 1887
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1416-1453 |
3.67e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 3.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568965053 1416 CQCNG---HSSQCDPETSVCQnCQHHTAGDFCERCALGYYG 1453
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYG 40
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1658-1898 |
5.29e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1658 EQtGQDAERTNSRAESLEEFIkglvQDAEAINEKAVQLNETLGNQDKTAErNLEELQ---KEIDRMLKEL--------RS 1726
Cdd:TIGR02168 142 EQ-GKISEIIEAKPEERRAIF----EEAAGISKYKERRKETERKLERTRE-NLDRLEdilNELERQLKSLerqaekaeRY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1727 KDLQTQKEVAE-----DELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYkNKLDDAwdlLREATDKTRDANR--L 1799
Cdd:TIGR02168 216 KELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKL-EELRLE---VSELEEEIEELQKelY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1800 SAANQKNmtILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINsvidyvdDIKTKLPPMSEELSDKIDDLAQEIKd 1879
Cdd:TIGR02168 292 ALANEIS--RLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-------EELAELEEKLEELKEELESLEAELE- 361
|
250
....*....|....*....
gi 568965053 1880 rRLAEKVFQAESHAAQLND 1898
Cdd:TIGR02168 362 -ELEAELEELESRLEELEE 379
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1613-1942 |
5.33e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.71 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1613 QELKHLlspQRAPERLIQLAEGNV-------NTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDA 1685
Cdd:pfam01576 327 QEVTEL---KKALEEETRSHEAQLqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1686 EAINEKA-VQLNETLGNQDKTaERNLEEL-------QKEIDR---MLKELRSKDLQTQKEVA--EDELVAAEGLLK---- 1748
Cdd:pfam01576 404 EHKRKKLeGQLQELQARLSES-ERQRAELaeklsklQSELESvssLLNEAEGKNIKLSKDVSslESQLQDTQELLQeetr 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1749 -------RVNKLFGEPRAQNEDMEKD-------------LQQKLAEYKNKLDD---AWDLLREAtdKTRDANRLSAANQK 1805
Cdd:pfam01576 483 qklnlstRLRQLEDERNSLQEQLEEEeeakrnverqlstLQAQLSDMKKKLEEdagTLEALEEG--KKRLQRELEALTQQ 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1806 nmtiLETKKEAIEgskrQIENTlkegndildeANRLLGEINSVIDYVDDIKTKLPPMsEELSDKIDDLAQEIK--DRRLA 1883
Cdd:pfam01576 561 ----LEEKAAAYD----KLEKT----------KNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMLAEEKaiSARYA 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 568965053 1884 EKVFQAESHAAQlndssavldgilDEAKNISFNataafRAYSNIKDYIDEAEKVAREAK 1942
Cdd:pfam01576 622 EERDRAEAEARE------------KETRALSLA-----RALEEALEAKEELERTNKQLR 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1642-1913 |
5.50e-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: 51.59 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1642 ETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDR-- 1719
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqe 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1720 ------MLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEprAQNEDMEKDLQQklaeYKNKLDDAWDLLREATDKT 1793
Cdd:TIGR00606 772 tllgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK--LQGSDLDRTVQQ----VNQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1794 RDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDL 1873
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568965053 1874 AQEIKDRRLAEKVFQAEshaaqLNDSSAVLDGILDEAKNI 1913
Cdd:TIGR00606 926 EELISSKETSNKKAQDK-----VNDIKEKVKNIHGYMKDI 960
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1674-1944 |
5.92e-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: 51.98 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1674 LEEFIKGLVQDAEAInEKAVQLNETLGNQD-------KTAERNLEELQKEIDRMLKELRSKdlqtQKEVAEDELvaaEGL 1746
Cdd:TIGR01612 605 LKEKIKNISDKNEYI-KKAIDLKKIIENNNayidelaKISPYQVPEHLKNKDKIYSTIKSE----LSKIYEDDI---DAL 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1747 LKRVNKLFGEPRAQN-EDmekdlQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNM---TILETKKEaiegskr 1822
Cdd:TIGR01612 677 YNELSSIVKENAIDNtED-----KAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNElldIIVEIKKH------- 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1823 qientlkegndILDEANRLLGEInsvidyVDDIKTKlppmSEELSDKIDDLAQEiKDR--RLAEKVFQAESHaaqLNDSS 1900
Cdd:TIGR01612 745 -----------IHGEINKDLNKI------LEDFKNK----EKELSNKINDYAKE-KDElnKYKSKISEIKNH---YNDQI 799
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568965053 1901 AVlDGILDEAKNISFNATAAFRAYSNIKDyiDEAEKVAREAKEL 1944
Cdd:TIGR01612 800 NI-DNIKDEDAKQNYDKSKEYIKTISIKE--DEIFKIINEMKFM 840
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
410-460 |
7.66e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 7.66e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 410 CHCDPTGSLSEVCVKDEkyaqrglkpGSCHCKTGFGGVNCDRCVRGYHGYP 460
Cdd:smart00180 1 CDCDPGGSASGTCDPDT---------GQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
464-512 |
8.88e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.65 E-value: 8.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 464 PCNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQkGCE 512
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG-GCQ 50
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1668-1913 |
9.39e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1668 NSRAESLEEFIKGLVQDAEAINEKAVQLNETLgnqDKTAERNLEELQKEiDRMLKELRS---KDLQTQKEVAEDELvAAE 1744
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRK---EYLESEEINKSINE-YNKIESARAdleDIKIKINELKDKHD-KYE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1745 GLLKRVNKL-FGEPRAQNEDMEK-----------DLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNM----T 1808
Cdd:PRK01156 550 EIKNRYKSLkLEDLDSKRTSWLNalavislidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIeneaN 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1809 ILETKKEAIEGSKRQIE------NTLKEGNDILDEANRLLGEINSVIdyvDDIKTKLPPMSEELSDKIDDLAqeikdrRL 1882
Cdd:PRK01156 630 NLNNKYNEIQENKILIEklrgkiDNYKKQIAEIDSIIPDLKEITSRI---NDIEDNLKKSRKALDDAKANRA------RL 700
|
250 260 270
....*....|....*....|....*....|.
gi 568965053 1883 AEKVFQAESHAAQLNDSSAVLDGILDEAKNI 1913
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1607-1846 |
1.17e-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: 50.83 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1607 GLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQ--- 1683
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqle 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1684 ---------------DAEAINEKAVQLNETLGNQDKTAER---------NLEELQKEIDRMLKELRSK--DLQTQKEVAE 1737
Cdd:TIGR02168 320 eleaqleeleskldeLAEELAELEEKLEELKEELESLEAEleeleaeleELESRLEELEEQLETLRSKvaQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1738 DELVAAEGLLK----RVNKLFGEPRAQNEDMEK------------------DLQQKLAEYKNKLDDAWDLLREATDKTRD 1795
Cdd:TIGR02168 400 NEIERLEARLErledRRERLQQEIEELLKKLEEaelkelqaeleeleeeleELQEELERLEEALEELREELEEAEQALDA 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568965053 1796 ANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEIN 1846
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1727-1845 |
1.24e-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: 48.49 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1727 KDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEyknkLDDAWDLLREATDKTRDANRLSAANQKN 1806
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEE----LERTEERLAEALEKLEEAEKAADESERG 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 568965053 1807 MTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEI 1845
Cdd:pfam00261 80 RKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
753-795 |
1.48e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.84 E-value: 1.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568965053 753 CQCF---AHAEACDDITGECLnCKDHTGGPYCNECLPGFYGDPTRG 795
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1662-1828 |
3.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1662 QDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLnETLGNQD------KTAERNLEELQKEIDRMLK---ELRSkdLQTQ 1732
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLDAssdDLAA--LEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1733 KEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILET 1812
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170
....*....|....*.
gi 568965053 1813 KKEAIEGSKRQIENTL 1828
Cdd:COG4913 774 RIDALRARLNRAEEEL 789
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1678-1880 |
4.04e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1678 IKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEDELVAAE-------GLLKRV 1750
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE--AKTIKAEIEELTDELLNLVmdiedpsAALNKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1751 NKLFGEPRAQNEDMEKDL-------------QQ------KLAEYKNKLDDAWDLLREATDKTRDAN-RLSAANQKNMTIL 1810
Cdd:PHA02562 261 NTAAAKIKSKIEQFQKVIkmyekggvcptctQQisegpdRITKIKDKLKELQHSLEKLDTAIDELEeIMDEFNEQSKKLL 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1811 ETKKEaIEGSKRQIENTLKEGNDILDEANRLLGEinsVIDYVDDIKTklppMSEELSDKIDDLAQEIKDR 1880
Cdd:PHA02562 341 ELKNK-ISTNKQSLITLVDKAKKVKAAIEELQAE---FVDNAEELAK----LQDELDKIVKTKSELVKEK 402
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1635-1838 |
5.87e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1635 NVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNetLGNQDKTAERNLEELQ 1714
Cdd:COG3206 206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ--LRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1715 ----------KEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRvnklfgepraqnedmEKDLQQKLAEYKNKLDDAWD 1784
Cdd:COG3206 284 arytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR---------------EASLQAQLAQLEARLAELPE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568965053 1785 LLREATDKTRDANrlsaANQKNMTILETKKEAIegskrQIENTLKEGN-DILDEA 1838
Cdd:COG3206 349 LEAELRRLEREVE----VARELYESLLQRLEEA-----RLAEALTVGNvRVIDPA 394
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
283-330 |
6.46e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.96 E-value: 6.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 283 CICYGHARACPL-DPATnkSRCECEHNTCGESCDRCCPGFHQKPWRAGT 330
Cdd:cd00055 2 CDCNGHGSLSGQcDPGT--GQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1686-1946 |
7.03e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.98 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1686 EAINEKAVQLNETlgNQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEDEL-----------VAAEGLLKRVNKLF 1754
Cdd:cd22656 94 AEILELIDDLADA--TDDEELEEAKKTIKALLDDLLKE--AKKYQDKAAKVVDKLtdfenqtekdqTALETLEKALKDLL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1755 GE--PRAQNEDMeKDLQQKLAEYKNKLddawdllreatdktrdANRLsaanqknmtiletkKEAIEGSKRQIENTlkegN 1832
Cdd:cd22656 170 TDegGAIARKEI-KDLQKELEKLNEEY----------------AAKL--------------KAKIDELKALIADD----E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1833 DILDEANRLLGEINSVIDYVDDIKTKLPPMSEELsdkiddlaQEIKDrrlaekVFQAeshaaqLNDSsavLDGILDEAKN 1912
Cdd:cd22656 215 AKLAAALRLIADLTAADTDLDNLLALIGPAIPAL--------EKLQG------AWQA------IATD---LDSLKDLLED 271
|
250 260 270
....*....|....*....|....*....|....
gi 568965053 1913 ISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQ 1946
Cdd:cd22656 272 DISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1665-1911 |
7.12e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1665 ERTNSRAESLEEFIKGLVQDAEAIN----EKAVQ--------------LNETLGNQDKTAE--RNLEELQKEIDRMLKEL 1724
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLQRELEALTqqleEKAAAydklektknrlqqeLDDLLVDLDHQRQlvSNLEKKQKKFDQMLAEE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1725 R--SKDLQTQKEVAE-----------------DELVAAEGLLKRVNKLFgepRAQNEDM--EKD---------------L 1768
Cdd:pfam01576 614 KaiSARYAEERDRAEaeareketralslaralEEALEAKEELERTNKQL---RAEMEDLvsSKDdvgknvhelerskraL 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1769 QQKLAEYKNKLDDAWDLLREATD-KTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINS 1847
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQATEDaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA 770
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568965053 1848 VidyvddiKTKLPPMSEELSDKIDDlAQEIKDRRLAE-KVFQAE--SHAAQLNDSSAVLDGILDEAK 1911
Cdd:pfam01576 771 A-------KKKLELDLKELEAQIDA-ANKGREEAVKQlKKLQAQmkDLQRELEEARASRDEILAQSK 829
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
818-859 |
7.13e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 41.96 E-value: 7.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568965053 818 CHLDRSLGLICD------ECPIGYTGPRCERCAEGYFGQPSIPGGsCQ 859
Cdd:cd00055 4 CNGHGSLSGQCDpgtgqcECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1609-1815 |
7.25e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1609 ENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAI 1688
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1689 N------EKAVQLNETLGN----QDKTAERNLEELQKEIDRMLKELRSKDLQTQkEVAEDELVAAEGLLKRVNKLFGEPR 1758
Cdd:TIGR00606 912 SpletflEKDQQEKEELISsketSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ-DGKDDYLKQKETELNTVNAQLEECE 990
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568965053 1759 AQNEDMEKDLQQKLAEY-KNKLDDAW---DL-LREATDKTRDANRLSAANQKNMT---ILETKKE 1815
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdTQKIQERWlqdNLtLRKRENELKEVEEELKQHLKEMGqmqVLQMKQE 1055
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1608-1890 |
8.18e-05 |
|
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: 47.66 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1608 LENTTQE--LKHLLSPQRAPERLIQLAEgnvntlvMETNELLTRATKVTADGEQTGQdaerTNSRAESLEEFIKGLVQDA 1685
Cdd:TIGR00618 652 QLTLTQErvREHALSIRVLPKELLASRQ-------LALQKMQSEKEQLTYWKEMLAQ----CQTLLRELETHIEEYDREF 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1686 EAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDlqtqkEVAEDELVAAEGLLKRVNKLFGEPRAQNEDME 1765
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAH-----FNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1766 KD---LQQKLAEYKNKLDDaWDLLREATDKT---RDANRLSAANQKNMTILETKKE--AIEGSKRQIENTLKEGNDILDE 1837
Cdd:TIGR00618 796 EDthlLKTLEAEIGQEIPS-DEDILNLQCETlvqEEEQFLSRLEEKSATLGEITHQllKYEECSKQLAQLTQEQAKIIQL 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568965053 1838 ANRLLGeINSVIdyVDDIKTKLPPMSEELS-DKIDDLAQEIKDRRLAEKVFQAE 1890
Cdd:TIGR00618 875 SDKLNG-INQIK--IQFDGDALIKFLHEITlYANVRLANQSEGRFHGRYADSHV 925
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1764-1947 |
9.76e-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: 46.07 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1764 MEKDLQQ--KLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRL 1841
Cdd:COG1579 2 MPEDLRAllDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1842 LGEINSVIDYvddiktklppmsEELSDKIDDLAQEIKDR--RLAEKVFQAESHAAQLNDSSAVLDGILDEAKnisfNATA 1919
Cdd:COG1579 82 LGNVRNNKEY------------EALQKEIESLKRRISDLedEILELMERIEELEEELAELEAELAELEAELE----EKKA 145
|
170 180
....*....|....*....|....*...
gi 568965053 1920 AFRAysNIKDYIDEAEKVAREAKELAQG 1947
Cdd:COG1579 146 ELDE--ELAELEAELEELEAEREELAAK 171
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1697-1952 |
1.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1697 ETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTQKEVAEDELVAAEGLLKRVNKLFgepRAQNEDMEKdLQQKLAEYK 1776
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELA--ELEAELEELRLELEELELELEEAQAEE---YELLAELAR-LEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1777 NKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINsvidyvddik 1856
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---------- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1857 tklppmsEELSDKIDDLAQEIKDRRLAEKvfQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEK 1936
Cdd:COG1196 379 -------EELEELAEELLEALRAAAELAA--QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250
....*....|....*.
gi 568965053 1937 VAREAKELAQGATKLV 1952
Cdd:COG1196 450 EEAELEEEEEALLELL 465
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1644-1879 |
1.34e-04 |
|
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: 46.94 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1644 NELLTRATKVTADGEQTGQDAERTNSraesLEEFIKGLVQDAEAINEKAV-------QLNETL---GNQDKTAERNLEEL 1713
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINN----SNNKIKILEQQIKDLNDKLKknkdkinKLNSDLskiNSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1714 QKEIDRMLKELRSKDlQTQKEVAeDELVAAEGLLKRVNKLFGEPRAQNEDMEKDL----------QQKLAEYKNKLDDAW 1783
Cdd:TIGR04523 123 EVELNKLEKQKKENK-KNIDKFL-TEIKKKEKELEKLNNKYNDLKKQKEELENELnllekeklniQKNIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1784 DLLREATDKTRDANRLSAA----NQKNMTI----------LETKKEAIEGSKRQIENTLKEGNDI----------LDEAN 1839
Cdd:TIGR04523 201 LLLSNLKKKIQKNKSLESQiselKKQNNQLkdniekkqqeINEKTTEISNTQTQLNQLKDEQNKIkkqlsekqkeLEQNN 280
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568965053 1840 RLLGEINsviDYVDDIKTKLppmsEEL-SDKIDDLAQEIKD 1879
Cdd:TIGR04523 281 KKIKELE---KQLNQLKSEI----SDLnNQKEQDWNKELKS 314
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
818-858 |
1.48e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.18 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 568965053 818 CHLDRSLGLICD------ECPIGYTGPRCERCAEGYFGQPSIPGGSC 858
Cdd:pfam00053 3 CNPHGSLSDTCDpetgqcLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1603-1940 |
1.61e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1603 KILYGLENTTQELKHLLspQRAPERLIQLaegnVNTLVMETNELLTRATKVTADG--------EQTGQDAERTNSRAES- 1673
Cdd:PRK04778 198 EILDQLEEELAALEQIM--EEIPELLKEL----QTELPDQLQELKAGYRELVEEGyhldhldiEKEIQDLKEQIDENLAl 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1674 LEEF-IKGLVQDAEAINEKAVQLNETL-----------GNQDKT------AERNLEELQKEIDRmLKE---LRSKDLQTQ 1732
Cdd:PRK04778 272 LEELdLDEAEEKNEEIQERIDQLYDILerevkarkyveKNSDTLpdflehAKEQNKELKEEIDR-VKQsytLNESELESV 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1733 KEVaEDELVAAEGLLKRVNKLFGEPRA---QNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDAnrlsaanQKNMTI 1809
Cdd:PRK04778 351 RQL-EKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEA-------REKLER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1810 LETKKEAIegsKRQIentlkegndildEANRLLGEINSVIDYVddiktklppmsEELSDKIDDLAQEIKDRRL-AEKVfq 1888
Cdd:PRK04778 423 YRNKLHEI---KRYL------------EKSNLPGLPEDYLEMF-----------FEVSDEIEALAEELEEKPInMEAV-- 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568965053 1889 aeshAAQLNDSSAVLDGILDEAKNISFNATAAFRA--YSN--------IKDYIDEAEKVARE 1940
Cdd:PRK04778 475 ----NRLLEEATEDVETLEEETEELVENATLTEQLiqYANryrsdneeVAEALNEAERLFRE 532
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
465-506 |
2.10e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 2.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 568965053 465 CNCSGLGSTNE--DPCVGPCSCKENVEGEDCSRCKSGFFNLQED 506
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1653-1774 |
2.43e-04 |
|
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: 44.63 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1653 VTADGEQTGQDAERTNSRAESLEEFIKGL---VQDAEAINEKAVQLNETLGNQDKT--------------AERNLEELQK 1715
Cdd:pfam00261 125 VEGDLERAEERAELAESKIVELEEELKVVgnnLKSLEASEEKASEREDKYEEQIRFlteklkeaetraefAERSVQKLEK 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568965053 1716 EIDRMlkelrskdlqtqkevaEDELVAAegllkrvnklfgepRAQNEDMEKDLQQKLAE 1774
Cdd:pfam00261 205 EVDRL----------------EDELEAE--------------KEKYKAISEELDQTLAE 233
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1653-1885 |
3.12e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.45 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1653 VTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLnETLGNQDKTAERNLEELQKEIDRMLKELrskdlqTQ 1732
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQL-ESGDDSGTPGGKKYLLLQKQLEQLQEEN------FR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1733 KEVAEDEL-VAAEGLLKRVnklfGEPRAQNEDMekdlqQKLAEYKNKLDDAWDLLREATDKtrdANRLSAAnqknmtiLE 1811
Cdd:pfam05622 78 LETARDDYrIKCEELEKEV----LELQHRNEEL-----TSLAEEAQALKDEMDILRESSDK---VKKLEAT-------VE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1812 TKKEAIEGS---KRQIEnTLKEGN-----------DILDEANRLLGEINSVIDYVDDIKTKLppmSEElSDKIDDLAQEI 1877
Cdd:pfam05622 139 TYKKKLEDLgdlRRQVK-LLEERNaeymqrtlqleEELKKANALRGQLETYKRQVQELHGKL---SEE-SKKADKLEFEY 213
|
....*...
gi 568965053 1878 KdrRLAEK 1885
Cdd:pfam05622 214 K--KLEEK 219
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1626-1950 |
3.31e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.98 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1626 ERLIQL---AEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEfIKGLVQDAEAIN---EKAV--QLNE 1697
Cdd:PTZ00440 1098 NKLIEIknkSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNL-EDITLNEVNEIEieyERILidHIVE 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1698 TLGNQDKTAERNLEELQ---KEID----RMLKELRSKDLQTQKEVAEDELVAAEgllKRVNKLFGEPRAQNEDMEKDLQ- 1769
Cdd:PTZ00440 1177 QINNEAKKSKTIMEEIEsykKDIDqvkkNMSKERNDHLTTFEYNAYYDKATASY---ENIEELTTEAKGLKGEANRSTNv 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1770 QKLAEYKNKLDDAwdlLREATDKTRDANRlSAANQKNM------TILETKKEAIEGSKRQIENTLKEGNDILDEANRLlg 1843
Cdd:PTZ00440 1254 DELKEIKLQVFSY---LQQVIKENNKMEN-ALHEIKNMyeflisIDSEKILKEILNSTKKAEEFSNDAKKELEKTDNL-- 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1844 eINSVIDYVDDIKTKLPPMSEELSDK-IDD-------LAQEIKDRRLAEKVF---------QAESHAAQLNDSSAVLDgI 1906
Cdd:PTZ00440 1328 -IKQVEAKIEQAKEHKNKIYGSLEDKqIDDeikkieqIKEEISNKRKEINKYlsniksnkeKCDLHVRNASRGKDKID-F 1405
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568965053 1907 LDEAKNISFNATAAFRAySNIKDYIDEAEKVAREAKELAQGATK 1950
Cdd:PTZ00440 1406 LNKHEAIEPSNSKEVNI-IKITDNINKCKQYSNEAMETENKADE 1448
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
803-851 |
3.33e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 3.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 803 CACPlniPSNNFSPTCHLDrslGLICdECPIGYTGPRCERCAEGYFGQP 851
Cdd:smart00180 1 CDCD---PGGSASGTCDPD---TGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1666-1833 |
4.09e-04 |
|
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: 42.28 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1666 RTNSRAESLEEFIKGLVQDAEAINEKavqlNETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTqkevaedELVAAeg 1745
Cdd:pfam10473 14 ESERKADSLKDKVENLERELEMSEEN----QELAILEAENSKAEVETLKAEIEEMAQNLR--DLEL-------DLVTL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1746 llkrvnklfgepRAQNEDMEKDLQQKlaeyKNKLDDAwDLLREATdktrdANRLSAANQKNMTILETKKEAIEgskrQIE 1825
Cdd:pfam10473 79 ------------RSEKENLTKELQKK----QERVSEL-ESLNSSL-----ENLLEEKEQEKVQMKEESKTAVE----MLQ 132
|
....*...
gi 568965053 1826 NTLKEGND 1833
Cdd:pfam10473 133 TQLKELNE 140
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1465-1520 |
5.48e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 5.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568965053 1465 CACPLISPSnnfSPSCVLEGledYRCTaCPRGYEGQYCERCAPGYTGSPSSPGGSC 1520
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1672-1849 |
8.09e-04 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 42.62 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1672 ESLEEFIKGLVQDAEAinekavQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKR-- 1749
Cdd:COG1390 2 MSLEKIIEEILEEAEA------EAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1750 -------VNKLFGEPRAQNEDMEKDlqqklAEYKNKLDdawDLLREA---------------TDKTRDANRLSAANQKNM 1807
Cdd:COG1390 76 leakeelIEEVFEEALEKLKNLPKD-----PEYKELLK---KLLKEAaeelgsgdlvvyvneKDKELLEELLKELKKKGL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568965053 1808 TILETKKEAIEG-------SKRQIENTLKEgndILDEA-NRLLGEINSVI 1849
Cdd:COG1390 148 EVSEEDIDILGGvivesedGRIRVDNTFES---LLERLkEELLKEIAEIL 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1607-1846 |
8.41e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1607 GLENTTQELKHL---LSPQRAPERLIQLAEGN---------VNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESL 1674
Cdd:TIGR02169 752 EIENVKSELKELearIEELEEDLHKLEEALNDlearlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1675 EEFIKGLVQDAEAI--NEKAVQLNETLGNQDK-----------TAERNLEE----LQKEIDRMLKELRS----------- 1726
Cdd:TIGR02169 832 EKEIQELQEQRIDLkeQIKSIEKEIENLNGKKeeleeeleeleAALRDLESrlgdLKKERDELEAQLRElerkieeleaq 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1727 --------KDLQTQKEVAEDELVAAEGLLKRvnklfGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDL-LREATDKTRDAN 1797
Cdd:TIGR02169 912 iekkrkrlSELKAKLEALEEELSEIEDPKGE-----DEEIPEEELSLEDVQAELQRVEEEIRALEPVnMLAIQEYEEVLK 986
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568965053 1798 RLSAANQKNMTiLETKKEAIEGSKRQIENTLKEG-----NDILDEANRLLGEIN 1846
Cdd:TIGR02169 987 RLDELKEKRAK-LEEERKAILERIEEYEKKKREVfmeafEAINENFNEIFAELS 1039
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1658-1898 |
1.08e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1658 EQTGQDAERTNSRaESLEEFIKgLVQDAEAINEKAVQLNETLgnqdKTAERNLEELQKEIDRM----------------L 1721
Cdd:pfam12795 7 KAKLDEAAKKKLL-QDLQQALS-LLDKIDASKQRAAAYQKAL----DDAPAELRELRQELAALqakaeaapkeilaslsL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1722 KELRSKDLQTQkevaeDELVAAEGLLKRVNKLFGEPRAQNEdmekDLQQKLAEYKNKLDDawdlLREATDKTRDANRLSA 1801
Cdd:pfam12795 81 EELEQRLLQTS-----AQLQELQNQLAQLNSQLIELQTRPE----RAQQQLSEARQRLQQ----IRNRLNGPAPPGEPLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1802 ANQKNMtiLETKKEAIEGSKRQIENTLkEGNDILDEANRLlgeinsVIDYVddiKTKLppmsEELSDKIDDLAQEIKDRR 1881
Cdd:pfam12795 148 EAQRWA--LQAELAALKAQIDMLEQEL-LSNNNRQDLLKA------RRDLL---TLRI----QRLEQQLQALQELLNEKR 211
|
250
....*....|....*..
gi 568965053 1882 LAEkvfqAESHAAQLND 1898
Cdd:pfam12795 212 LQE----AEQAVAQTEQ 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1655-1789 |
1.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1655 ADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGnqdkTAERNLEELQKEIDRmlkelrskdLQTQKE 1734
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG----RLEKELEQAEEELDE---------LQDRLE 737
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568965053 1735 VAEDElvAAEGLLKRVNKLFGEPRAQN--EDMEKDLQQKLAEYKNKLDDAWDLLREA 1789
Cdd:COG4913 738 AAEDL--ARLELRALLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERA 792
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1662-1922 |
1.25e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 43.31 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1662 QDAERTNSRAESLEEFIKGLVQDAEAINEKAvQL--NETLGNQDKTAERNLEELQKEIDRMLKElrSKDLQTQKEVAEDE 1739
Cdd:pfam03148 10 REAEAQRNDAERLRQESRRLRNETDAKTKWD-QYdsNRRLGERIQDITFWKSELEKELEELDEE--IELLLEEKRRLEKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1740 L--------VAAEGLLKRvnklfgEPRaQNEDM-----EKDLQQKL-------AEYKNKLDDAWDLLREatdktrdaNRl 1799
Cdd:pfam03148 87 LealeeplhIAQECLTLR------EKR-QGIDLvhdevEKELLKEVeliegiqELLQRTLEQAWEQLRL--------LR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1800 saANQKNMTI-LETKKEAIEgskrqientlkegndiLDEANRLLGEINSVIDYVDDIkTKLPPMSEELSDkIDDLAQEIK 1878
Cdd:pfam03148 151 --AARHKLEKdLSDKKEALE----------------IDEKCLSLNNTSPNISYKPGP-TRIPPNSSTPEE-WEKFTQDNI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568965053 1879 DRrlAEKVFQAeshAAQLNdssAVLDGILDEAKNI---SFNAT-AAFR 1922
Cdd:pfam03148 211 ER--AEKERAA---SAQLR---ELIDSILEQTANDlraQADAVnFALR 250
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1745-1949 |
1.31e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1745 GLLKRVNKLFgepRA-------QNEDMEKDLQQKLAEYKNKLDDAwdllREATDKTrdanrlsAANQKNMTI-LETKKEA 1816
Cdd:COG1842 1 GIFKRLSDII---RAninalldKAEDPEKMLDQAIRDMEEDLVEA----RQALAQV-------IANQKRLERqLEELEAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1817 IEGSKRQIENTLKEGNDilDEANRLLGEINSVIDYVDDIKT---KLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHA 1893
Cdd:COG1842 67 AEKWEEKARLALEKGRE--DLAREALERKAELEAQAEALEAqlaQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1894 A----QLNDSSAvldgildeakniSFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGAT 1949
Cdd:COG1842 145 AkaqeKVNEALS------------GIDSDDATSALERMEEKIEEMEARAEAAAELAAGDS 192
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
86-170 |
1.73e-03 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 40.51 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 86 SSNPYQRHPITNAIDGK-NTWWQSpsiKNGVEYHYvtITLDLQQVFQIAYVIVKAANSPRPGN---WILERSLDDVEYKP 161
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDpNTAWSA---WSGDDPQW--IQVDLGKPKKITGVVTQGRQDGSNGYvtsYKIEYSLDGENWTT 79
|
....*....
gi 568965053 162 WQYHAVTDT 170
Cdd:pfam00754 80 VKDEKIPGN 88
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1375-1403 |
2.56e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 37.72 E-value: 2.56e-03
10 20
....*....|....*....|....*....
gi 568965053 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1663-1879 |
3.06e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1663 DAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRskDLQTQKEVAEDELVA 1742
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL--ELEEALLAEEEEERE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1743 AEGLLKRvnklfgepRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANqknmtiLETKKEAIEGSKR 1822
Cdd:COG1196 709 LAEAEEE--------RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD------LEELERELERLER 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1823 QIENtlkegndildeanrlLGEIN-SVIDYVDDIKTKLppmsEELSDKIDDLAQEIKD 1879
Cdd:COG1196 775 EIEA---------------LGPVNlLAIEEYEELEERY----DFLSEQREDLEEARET 813
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
302-326 |
3.31e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 3.31e-03
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1694-1782 |
3.40e-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: 39.87 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1694 QLNETLGNQDKTAERNLEELQKEIDRMLKELRSK--DLQTQKEVAEDELVAAEGLLKRVNklfgepRAQNEDMEKDLQQK 1771
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDgaLLEEEREEKEQELQKKEQELQQLQ------QKAQQELQKKQQEL 92
|
90
....*....|.
gi 568965053 1772 LAEYKNKLDDA 1782
Cdd:pfam03938 93 LQPIQDKINKA 103
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1662-1825 |
3.50e-03 |
|
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: 41.83 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1662 QDAERTNSRAESLEEFikglVQDAEAINEKAVQLNEtlgnQD-KTAERNLEE---LQKEIDRMLKELRS-KDLQTQKEVA 1736
Cdd:pfam13868 81 QIEEREQKRQEEYEEK----LQEREQMDEIVERIQE----EDqAEAEEKLEKqrqLREEIDEFNEEQAEwKELEKEEERE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1737 EDELVAAEGLLK--RVNKLFGEPRAQNEDMEK------DLQQKLAEYKNKLDDAW-DLLREATDKTRDANRLSAANQKnm 1807
Cdd:pfam13868 153 EDERILEYLKEKaeREEEREAEREEIEEEKEReiarlrAQQEKAQDEKAERDELRaKLYQEEQERKERQKEREEAEKK-- 230
|
170
....*....|....*...
gi 568965053 1808 tiLETKKEAIEGSKRQIE 1825
Cdd:pfam13868 231 --ARQRQELQQAREEQIE 246
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1375-1403 |
3.53e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.33 E-value: 3.53e-03
10 20
....*....|....*....|....*....
gi 568965053 1375 RCDCPPGYSGLSCETCAPGFYRLRSEPGG 1403
Cdd:pfam00053 19 QCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1603-1914 |
3.56e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1603 KILYGLENTTQeLKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVtadgeQTGQDAERTNSRAESLEEFI---- 1678
Cdd:PTZ00440 572 KIKYIEENVDH-IKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDL-----QEKVKYILNKFYKGDLQELLdels 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1679 ------KGLVQDAEAINEKAVQLNETLGNQDKtaernLEELQKE-IDRMLKELR--SKDLQTQKEVAEDELVaaegllkr 1749
Cdd:PTZ00440 646 hflddhKYLYHEAKSKEDLQTLLNTSKNEYEK-----LEFMKSDnIDNIIKNLKkeLQNLLSLKENIIKKQL-------- 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1750 vNKLfgepraqNEDMEKDLQQKLAEYKnklddawdllreatDKTRDANRLSAANQKnmtiLETKKEAIEGSKRQIENTLK 1829
Cdd:PTZ00440 713 -NNI-------EQDISNSLNQYTIKYN--------------DLKSSIEEYKEEEEK----LEVYKHQIINRKNEFILHLY 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1830 EGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQA--ESHAAQLNDSsavLDGIL 1907
Cdd:PTZ00440 767 ENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAhtEKNDEELKQL---LQKFP 843
|
....*..
gi 568965053 1908 DEAKNIS 1914
Cdd:PTZ00440 844 TEDENLN 850
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1707-1792 |
5.56e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 38.08 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1707 ERNLEELQKEIDRMLKELRSKD----------LQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEyk 1776
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDlgkdlesveaLLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE-- 81
|
90
....*....|....*.
gi 568965053 1777 nkLDDAWDLLREATDK 1792
Cdd:smart00150 82 --LNERWEELKELAEE 95
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1662-1740 |
7.39e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.57 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1662 QDAERTNSRAESL----EEFIKGLVQDAEAINEKAVQlnetlgNQDKTAERNLEELQKEIDRMLKELRsKDLQTQKEVAE 1737
Cdd:cd06503 40 EEAEKAKEEAEELlaeyEEKLAEARAEAQEIIEEARK------EAEKIKEEILAEAKEEAERILEQAK-AEIEQEKEKAL 112
|
...
gi 568965053 1738 DEL 1740
Cdd:cd06503 113 AEL 115
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1701-1779 |
7.79e-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: 38.71 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568965053 1701 NQDKTAERNLE----ELQKEIDRMLKELRSK--DLQTQKEVAEDELVAAEG-LLKRVNKLfgepRAQNEDMEKDLQQKLA 1773
Cdd:pfam03938 15 PEGKAAQAQLEkkfkKRQAELEAKQKELQKLyeELQKDGALLEEEREEKEQeLQKKEQEL----QQLQQKAQQELQKKQQ 90
|
....*.
gi 568965053 1774 EYKNKL 1779
Cdd:pfam03938 91 ELLQPI 96
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1464-1521 |
9.13e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 36.18 E-value: 9.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568965053 1464 PCACPLISpsnNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSPSSPGGsCQ 1521
Cdd:cd00055 1 PCDCNGHG---SLSGQCDPGTG---QCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1465-1513 |
9.40e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 35.75 E-value: 9.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568965053 1465 CACPlisPSNNFSPSCVLEGLedyRCTaCPRGYEGQYCERCAPGYTGSP 1513
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG---QCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| |
