|
Name |
Accession |
Description |
Interval |
E-value |
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
420-617 |
1.38e-88 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 280.96 E-value: 1.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKCFESNACLSSVTQCCQKETREINGQPIVVVDTPGLFDTKLTDEEIKEELAKCITML 499
Cdd:cd01852 1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 500 APGPHAFLVVVKIDRYTKEEREAIKLIKDFFGSKAVDFIIIIFTRGDELGNQTIESYIQSDREGyLKKTIKDCGNRYQVF 579
Cdd:cd01852 81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEA-LKRLLEKCGGRYVAF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2515696781 580 NNKDRNG---DQVRELLRKIKLMVQENQGKSYTSEIFQEAE 617
Cdd:cd01852 160 NNKAKGReqeQQVKELLAKVEEMVRENGGKPYTNEMYEEAE 200
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
420-632 |
2.81e-64 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 215.16 E-value: 2.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKCFESNACLSSVTQCCQKETREINGQPIVVVDTPGLFDTKLTDEEIKEELAKCITML 499
Cdd:pfam04548 1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 500 APGPHAFLVVVKIDRYTKEEREAIKLIKDFFGSKAVDFIIIIFTRGDELGNQTIESYIQSDREGYLKKTIKDcgnryqvf 579
Cdd:pfam04548 81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDGCPEFLKEVLRT-------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2515696781 580 NNKDRNGDQVRELLRKIKLMVQENQGKSYTSEIFQEaeaaIQKEADRiLKEKQ 632
Cdd:pfam04548 153 ADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEK----IKEEGER-LREQQ 200
|
|
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
205-392 |
9.32e-23 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 96.84 E-value: 9.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 205 LNLVLFGRFQTWKNSATSAILGGRKNDSNDNPL----ECAKFQGEVCGRAVSLVELPVLYGT----PRVKaiKESIHCMS 276
Cdd:cd01852 1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASgvtkTCQKESAVWDGRRVNVIDTPGLFDTsvspEQLS--KEIIRCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 277 LCDPeGVNAFILILPMDSLSDEDERELETLQSIFTSRVKDFIMILITVKCDPSAAAVQSFLKENKHFL-ELCGHCRGRYF 355
Cdd:cd01852 79 LSAP-GPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALkRLLEKCGGRYV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2515696781 356 VLD-----VTDRQQVDQLLHMVEKTSAG-ESKCFIGEIMEKPQ 392
Cdd:cd01852 158 AFNnkakgREQEQQVKELLAKVEEMVREnGGKPYTNEMYEEAE 200
|
|
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
16-191 |
1.00e-14 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 73.72 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 16 LRIVVFGNNQKEKTTLTNNIAKRN-----KPPWEVREQCTVTFGEYKRKRIIVVTTPVMFNL--PEVKLKHEIKRCVAFC 88
Cdd:cd01852 1 LRLVLVGKTGNGKSATGNTILGRKvfeskLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTsvSPEQLSKEIIRCLSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 89 PPGPNVLLWLLNPSDFSEDEHLNVNTILTSFSQEACKFSIVI-------KAQTVD--VEN--DLLNQVIQDCGNKCH--- 154
Cdd:cd01852 81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLftrgddlEGGSLEdyLEDscEALKRLLEKCGGRYVafn 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2515696781 155 --TVSLEKdlpEQDYEALMEKMEIIVNENKGRHlnYTEQ 191
Cdd:cd01852 161 nkAKGREQ---EQQVKELLAKVEEMVRENGGKP--YTNE 194
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
420-548 |
3.44e-12 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 68.64 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTIlgrkcFESNACLSSVTQCCQKETREI-----NGQPIVVVDTPGLFDTKLTDEEIKEelak 494
Cdd:COG3596 40 PVIALVGKTGAGKSSLINAL-----FGAEVAEVGVGRPCTREIQRYrlesdGLPGLVLLDTPGLGEVNERDREYRE---- 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2515696781 495 cITMLAPGPHAFLVVVKI-DRYTKEEREAIKLIKDFFGSKAvdfIIIIFTRGDEL 548
Cdd:COG3596 111 -LRELLPEADLILWVVKAdDRALATDEEFLQALRAQYPDPP---VLVVLTQVDRL 161
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
205-374 |
1.73e-10 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 61.47 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 205 LNLVLFGRFQTWKNSATSAILGGRKNDS----NDNPLECAKFQGEVCGRAVSLVELPVLY--GTPRVKAIKESIHCMSLC 278
Cdd:pfam04548 1 LRIVLVGKTGNGKSATGNSILGRKAFESklraQGVTKTCQLVSRTWDGRIINVIDTPGLFdlSVSNDFISKEIIRCLLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 279 DPeGVNAFILILPMDSLSDEDERELETLQSIFTSRVKDFIMILITVKCDPSAAAVQSFLKE--NKHFLElcghcrgryfV 356
Cdd:pfam04548 81 EP-GPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgcPEFLKE----------V 149
|
170 180
....*....|....*....|..
gi 2515696781 357 LDVTDRQ----QVDQLLHMVEK 374
Cdd:pfam04548 150 LRTADGEekeeQVQQLLALVEA 171
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
16-193 |
4.44e-09 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 57.23 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 16 LRIVVFGNNQKEKTTLTNNIAKRNKPPWEVREQ-----CTVTFGEYKRKRIIVVTTPVMFNL--PEVKLKHEIKRCVAFC 88
Cdd:pfam04548 1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQgvtktCQLVSRTWDGRIINVIDTPGLFDLsvSNDFISKEIIRCLLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 89 PPGPNVLLWLLNPSDFSEDEHLNVNTILTSFSQEACKFSIVIKAQTVDVENDLLNQVIQDCGNKC-HTVSLEKDLPEQDY 167
Cdd:pfam04548 81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDGCPEFlKEVLRTADGEEKEE 160
|
170 180
....*....|....*....|....*...
gi 2515696781 168 EA--LMEKMEIIVNENKGRHlnYTEQND 193
Cdd:pfam04548 161 QVqqLLALVEAIVKENGGKP--YTNDLY 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
593-893 |
5.99e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 593 LRKIKLMVQENQGKSYT----------SEIFQEAEAAIQKEADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRN 662
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTlapyekmerrKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 663 ITAQETELIK-EKEELIRKEQEKIEREQEEKAK--------------EKMRMMLEDEAKRIKWEKTSEDLENSVNATMGT 727
Cdd:pfam17380 293 FEKMEQERLRqEKEEKAREVERRRKLEEAEKARqaemdrqaaiyaeqERMAMERERELERIRQEERKRELERIRQEEIAM 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 728 EEIYMVMMKRETMaEEQEAWEKGRMEYWD----KVLSEEEQNQ-HENKMQLRKLREEYEKdvenynrMKDAQLQKVKNEN 802
Cdd:pfam17380 373 EISRMRELERLQM-ERQQKNERVRQELEAarkvKILEEERQRKiQQQKVEMEQIRAEQEE-------ARQREVRRLEEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 803 VlEELQDTFEEKLEafKKKYQEEARKEAENRNDFLLNYSMNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKD 882
Cdd:pfam17380 445 A-REMERVRLEEQE--RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKE 521
|
330
....*....|.
gi 2515696781 883 FQRLQRKQEEE 893
Cdd:pfam17380 522 MEERQKAIYEE 532
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
551-855 |
1.47e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 55.56 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 551 QTIESYIQSDREGYLKKTIKDCGNRYQVFNNKDRNGDQVR-ELLRKI-----KLMVQENQGKSYTSEIFQEAEAAIQKEA 624
Cdd:PTZ00341 842 EEIISYIVDISLSDIENTAKNAAEQILSDEGLDEKKLKKRaESLKKLanaieKYAGGGKKDKKAKKKDAKDLSGNIAHEI 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 625 DRILKEKQEEIEREKREIEEvftcEIEAKIKEMTEQrNITAQETELIKEKEElirkeqEKIEREQEEKAKEKMRMMLEDE 704
Cdd:PTZ00341 922 NLINKELKNQNENVPEHLKE----HAEANIEEDAEE-NVEEDAEENVEENVE------ENVEENVEENVEENVEENVEEN 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 705 AKRIKWEKTSEDLENSV--NATMGTEEiymvmMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENkmqlrkLREEYEK 782
Cdd:PTZ00341 991 VEENVEENVEENIEENVeeNVEENIEE-----NVEEYDEENVEEVEENVEEYDEENVEEIEENAEEN------VEENIEE 1059
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2515696781 783 DVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEARKEAENrndfllNYSMNVLDQMENDKREN 855
Cdd:PTZ00341 1060 NIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEE------NAEENAEENAEEYDDEN 1126
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-893 |
3.41e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 593 LRKIKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQeeierekreieevftcEIEAKIKEMTEQRNITAQETELIK 672
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA----------------ELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 673 EKEELIRKEQEKIEREQEEKAKEKMRmmLEDEAKRIKWEKTSEDLENSVNATmgteeiymvmmKRETMAEEQEAWEKgRM 752
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRE--LEERLEELEEELAELEEELEELEE-----------ELEELEEELEEAEE-EL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 753 EYWDKVLSEEEQNQHENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEARKEAEN 832
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2515696781 833 RNDFLlnysmNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEE 893
Cdd:COG1196 434 EEEEE-----EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| 3a0901s04IAP86 |
TIGR00993 |
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ... |
294-531 |
2.93e-06 |
|
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273381 [Multi-domain] Cd Length: 763 Bit Score: 51.11 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 294 SLSDEDERELETLQSIftsRVKdFIMILITVKCDPSAAAVQSFLKEnkhFLELCGHCRGRYFVLDVTdrqqvdqllhmve 373
Cdd:TIGR00993 41 TLSEEHKEKLEKLQLI---RVK-FLRLAQRLGQTPENSIAAQVLYR---LGLLAGRQGGGAFSLDAA------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 374 KTSAGESKCfigeimekpqseSGNAEVALStelttvphkpsqneecLRIVLIGKTGSGKSATANTILGrkcfESNACLSS 453
Cdd:TIGR00993 101 KAMAEQLEA------------EGQDPLDFS----------------LNILVLGKSGVGKSATINSIFG----EVKFSTDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 454 VtQCCQKETREI----NGQPIVVVDTPGLFDT---KLTDEEIKEELAKCITMLAPGphaflVVVKIDRYTKEEREA---- 522
Cdd:TIGR00993 149 F-GMGTTSVQEIeglvQGVKIRVIDTPGLKSSasdQSKNEKILSSVKKFIKKNPPD-----IVLYVDRLDMQTRDSndlp 222
|
250
....*....|
gi 2515696781 523 -IKLIKDFFG 531
Cdd:TIGR00993 223 lLRTITDVLG 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
581-868 |
7.61e-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: 46.59 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 581 NKDRNGDQVRELLRK------IKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEIEREKREIEEVFTCEIEAKI 654
Cdd:TIGR02168 705 KELEELEEELEQLRKeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 655 KEMTEQRNITAQETELIKEKEELIRKE--QEKIEREQEEKAKEKMRMMLEDEAKRI-----KWEKTSEDLEnSVNATMGT 727
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLedleeQIEELSEDIE-SLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 728 EEIYMVMMKRET------MAEEQEAWEKGRMEYWDKV--LSEEEQNQHENKMQLRKLREEYEKDVENYNRMKdAQLQKVK 799
Cdd:TIGR02168 864 LEELIEELESELeallneRASLEEALALLRSELEELSeeLRELESKRSELRRELEELREKLAQLELRLEGLE-VRIDNLQ 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515696781 800 nENVLEELQDTFEE--KLEAFKKKYQEEAR---KEAENRNDFLLNYSMNVLDQMENDKRENDVVNqkkQQQKDL 868
Cdd:TIGR02168 943 -ERLSEEYSLTLEEaeALENKIEDDEEEARrrlKRLENKIKELGPVNLAAIEEYEELKERYDFLT---AQKEDL 1012
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
420-617 |
1.38e-88 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 280.96 E-value: 1.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKCFESNACLSSVTQCCQKETREINGQPIVVVDTPGLFDTKLTDEEIKEELAKCITML 499
Cdd:cd01852 1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 500 APGPHAFLVVVKIDRYTKEEREAIKLIKDFFGSKAVDFIIIIFTRGDELGNQTIESYIQSDREGyLKKTIKDCGNRYQVF 579
Cdd:cd01852 81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEA-LKRLLEKCGGRYVAF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2515696781 580 NNKDRNG---DQVRELLRKIKLMVQENQGKSYTSEIFQEAE 617
Cdd:cd01852 160 NNKAKGReqeQQVKELLAKVEEMVRENGGKPYTNEMYEEAE 200
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
420-632 |
2.81e-64 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 215.16 E-value: 2.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKCFESNACLSSVTQCCQKETREINGQPIVVVDTPGLFDTKLTDEEIKEELAKCITML 499
Cdd:pfam04548 1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 500 APGPHAFLVVVKIDRYTKEEREAIKLIKDFFGSKAVDFIIIIFTRGDELGNQTIESYIQSDREGYLKKTIKDcgnryqvf 579
Cdd:pfam04548 81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDGCPEFLKEVLRT-------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2515696781 580 NNKDRNGDQVRELLRKIKLMVQENQGKSYTSEIFQEaeaaIQKEADRiLKEKQ 632
Cdd:pfam04548 153 ADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEK----IKEEGER-LREQQ 200
|
|
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
205-392 |
9.32e-23 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 96.84 E-value: 9.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 205 LNLVLFGRFQTWKNSATSAILGGRKNDSNDNPL----ECAKFQGEVCGRAVSLVELPVLYGT----PRVKaiKESIHCMS 276
Cdd:cd01852 1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASgvtkTCQKESAVWDGRRVNVIDTPGLFDTsvspEQLS--KEIIRCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 277 LCDPeGVNAFILILPMDSLSDEDERELETLQSIFTSRVKDFIMILITVKCDPSAAAVQSFLKENKHFL-ELCGHCRGRYF 355
Cdd:cd01852 79 LSAP-GPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALkRLLEKCGGRYV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2515696781 356 VLD-----VTDRQQVDQLLHMVEKTSAG-ESKCFIGEIMEKPQ 392
Cdd:cd01852 158 AFNnkakgREQEQQVKELLAKVEEMVREnGGKPYTNEMYEEAE 200
|
|
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
16-191 |
1.00e-14 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 73.72 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 16 LRIVVFGNNQKEKTTLTNNIAKRN-----KPPWEVREQCTVTFGEYKRKRIIVVTTPVMFNL--PEVKLKHEIKRCVAFC 88
Cdd:cd01852 1 LRLVLVGKTGNGKSATGNTILGRKvfeskLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTsvSPEQLSKEIIRCLSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 89 PPGPNVLLWLLNPSDFSEDEHLNVNTILTSFSQEACKFSIVI-------KAQTVD--VEN--DLLNQVIQDCGNKCH--- 154
Cdd:cd01852 81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLftrgddlEGGSLEdyLEDscEALKRLLEKCGGRYVafn 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2515696781 155 --TVSLEKdlpEQDYEALMEKMEIIVNENKGRHlnYTEQ 191
Cdd:cd01852 161 nkAKGREQ---EQQVKELLAKVEEMVRENGGKP--YTNE 194
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
420-548 |
3.44e-12 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 68.64 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTIlgrkcFESNACLSSVTQCCQKETREI-----NGQPIVVVDTPGLFDTKLTDEEIKEelak 494
Cdd:COG3596 40 PVIALVGKTGAGKSSLINAL-----FGAEVAEVGVGRPCTREIQRYrlesdGLPGLVLLDTPGLGEVNERDREYRE---- 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2515696781 495 cITMLAPGPHAFLVVVKI-DRYTKEEREAIKLIKDFFGSKAvdfIIIIFTRGDEL 548
Cdd:COG3596 111 -LRELLPEADLILWVVKAdDRALATDEEFLQALRAQYPDPP---VLVVLTQVDRL 161
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
423-596 |
3.99e-11 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 62.47 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 423 VLIGKTGSGKSATANTILGRKCFESNAClSSVTQCCQKETREI--NGQPIVVVDTPGLfdtkltDEEIKEELAKCITMLA 500
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDV-PGTTRDPDVYVKELdkGKVKLVLVDTPGL------DEFGGLGREELARLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 501 PGPHAFLVVVKIDRYTKEEREAIKLIKDFFGSKAVdfIIIIFTRGDELGNQTIESYIQSDREGYLKktikdcGNRYQVFN 580
Cdd:cd00882 74 RGADLILLVVDSTDRESEEDAKLLILRRLRKEGIP--IILVGNKIDLLEEREVEELLRLEELAKIL------GVPVFEVS 145
|
170
....*....|....*.
gi 2515696781 581 NKDRNGdqVRELLRKI 596
Cdd:cd00882 146 AKTGEG--VDELFEKL 159
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
205-374 |
1.73e-10 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 61.47 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 205 LNLVLFGRFQTWKNSATSAILGGRKNDS----NDNPLECAKFQGEVCGRAVSLVELPVLY--GTPRVKAIKESIHCMSLC 278
Cdd:pfam04548 1 LRIVLVGKTGNGKSATGNSILGRKAFESklraQGVTKTCQLVSRTWDGRIINVIDTPGLFdlSVSNDFISKEIIRCLLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 279 DPeGVNAFILILPMDSLSDEDERELETLQSIFTSRVKDFIMILITVKCDPSAAAVQSFLKE--NKHFLElcghcrgryfV 356
Cdd:pfam04548 81 EP-GPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgcPEFLKE----------V 149
|
170 180
....*....|....*....|..
gi 2515696781 357 LDVTDRQ----QVDQLLHMVEK 374
Cdd:pfam04548 150 LRTADGEekeeQVQQLLALVEA 171
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
421-544 |
1.38e-09 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 56.47 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 421 RIVLIGKTGSGKSATANTILGRKCFESNacLSSVTQCCQKETREINGQPIVVVDTPGLFDTKLTDEEIKEELAKCITmla 500
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSD--YPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE--- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2515696781 501 pgPHAFLVVV-KIDRYTKEEREAIKLIKdffgsKAVDFIIIIFTR 544
Cdd:pfam01926 76 --ADLILFVVdSEEGITPLDEELLELLR-----ENKKPIILVLNK 113
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
16-193 |
4.44e-09 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 57.23 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 16 LRIVVFGNNQKEKTTLTNNIAKRNKPPWEVREQ-----CTVTFGEYKRKRIIVVTTPVMFNL--PEVKLKHEIKRCVAFC 88
Cdd:pfam04548 1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQgvtktCQLVSRTWDGRIINVIDTPGLFDLsvSNDFISKEIIRCLLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 89 PPGPNVLLWLLNPSDFSEDEHLNVNTILTSFSQEACKFSIVIKAQTVDVENDLLNQVIQDCGNKC-HTVSLEKDLPEQDY 167
Cdd:pfam04548 81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDGCPEFlKEVLRTADGEEKEE 160
|
170 180
....*....|....*....|....*...
gi 2515696781 168 EA--LMEKMEIIVNENKGRHlnYTEQND 193
Cdd:pfam04548 161 QVqqLLALVEAIVKENGGKP--YTNDLY 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
593-893 |
5.99e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 593 LRKIKLMVQENQGKSYT----------SEIFQEAEAAIQKEADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRN 662
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTlapyekmerrKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 663 ITAQETELIK-EKEELIRKEQEKIEREQEEKAK--------------EKMRMMLEDEAKRIKWEKTSEDLENSVNATMGT 727
Cdd:pfam17380 293 FEKMEQERLRqEKEEKAREVERRRKLEEAEKARqaemdrqaaiyaeqERMAMERERELERIRQEERKRELERIRQEEIAM 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 728 EEIYMVMMKRETMaEEQEAWEKGRMEYWD----KVLSEEEQNQ-HENKMQLRKLREEYEKdvenynrMKDAQLQKVKNEN 802
Cdd:pfam17380 373 EISRMRELERLQM-ERQQKNERVRQELEAarkvKILEEERQRKiQQQKVEMEQIRAEQEE-------ARQREVRRLEEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 803 VlEELQDTFEEKLEafKKKYQEEARKEAENRNDFLLNYSMNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKD 882
Cdd:pfam17380 445 A-REMERVRLEEQE--RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKE 521
|
330
....*....|.
gi 2515696781 883 FQRLQRKQEEE 893
Cdd:pfam17380 522 MEERQKAIYEE 532
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
420-579 |
6.55e-08 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 53.32 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKCFEsnaclSSVTQCCQKETR---EINGQpIVVVDTPGLFDTKLTDEEI-KEELAKC 495
Cdd:cd09912 1 FLLAVVGEFSAGKSTLLNALLGEEVLP-----TGVTPTTAVITVlryGLLKG-VVLVDTPGLNSTIEHHTEItESFLPRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 496 itmlapgpHAFLVVVKIDR-YTKEEREAIKLIKDFFGSKavdfIIIIFTRGDELGNQTIESYIQSDREGYLKKTIKdcGN 574
Cdd:cd09912 75 --------DAVIFVLSADQpLTESEREFLKEILKWSGKK----IFFVLNKIDLLSEEELEEVLEYSREELGVLELG--GG 140
|
....*
gi 2515696781 575 RYQVF 579
Cdd:cd09912 141 EPRIF 145
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
587-891 |
1.05e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 587 DQVRELLRKIKLmvqENQGKSYTSEIfqEAEAAIQKEADRILKEKQEEIERekreieevftCEIEAKIKEMTEQRNI-TA 665
Cdd:pfam17380 307 EKAREVERRRKL---EEAEKARQAEM--DRQAAIYAEQERMAMERERELER----------IRQEERKRELERIRQEeIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 666 QETELIKEKEELIRKEQEKIER-EQEEKAKEKMRMMLEDEAKRIKWEKTsedlensvnatmgteEIYMVMMKRETMAEEQ 744
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERvRQELEAARKVKILEEERQRKIQQQKV---------------EMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 745 -EAWEKGRMEYWDKVLSEEEQNQHenkmQLRKLREEYEKdvenyNRMKDAQLQKVKNENVL--EELQDTFEEKLEAFKKK 821
Cdd:pfam17380 437 vRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEE-----RKRKKLELEKEKRDRKRaeEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2515696781 822 YQEEAR------KEAENRNDfllnysmNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQE 891
Cdd:pfam17380 508 MIEEERkrklleKEMEERQK-------AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
551-855 |
1.47e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 55.56 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 551 QTIESYIQSDREGYLKKTIKDCGNRYQVFNNKDRNGDQVR-ELLRKI-----KLMVQENQGKSYTSEIFQEAEAAIQKEA 624
Cdd:PTZ00341 842 EEIISYIVDISLSDIENTAKNAAEQILSDEGLDEKKLKKRaESLKKLanaieKYAGGGKKDKKAKKKDAKDLSGNIAHEI 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 625 DRILKEKQEEIEREKREIEEvftcEIEAKIKEMTEQrNITAQETELIKEKEElirkeqEKIEREQEEKAKEKMRMMLEDE 704
Cdd:PTZ00341 922 NLINKELKNQNENVPEHLKE----HAEANIEEDAEE-NVEEDAEENVEENVE------ENVEENVEENVEENVEENVEEN 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 705 AKRIKWEKTSEDLENSV--NATMGTEEiymvmMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENkmqlrkLREEYEK 782
Cdd:PTZ00341 991 VEENVEENVEENIEENVeeNVEENIEE-----NVEEYDEENVEEVEENVEEYDEENVEEIEENAEEN------VEENIEE 1059
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2515696781 783 DVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEARKEAENrndfllNYSMNVLDQMENDKREN 855
Cdd:PTZ00341 1060 NIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEE------NAEENAEENAEEYDDEN 1126
|
|
| Toc34_like |
cd01853 |
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ... |
420-532 |
3.12e-07 |
|
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.
Pssm-ID: 206652 Cd Length: 248 Bit Score: 52.71 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKCFESNACLSS---VTQCcqkeTREINGQPIVVVDTPGLFDtkLTDEEIKEELAKCI 496
Cdd:cd01853 32 LTILVLGKTGVGKSSTINSIFGERKVSVSAFQSEtlrPREV----SRTVDGFKLNIIDTPGLLE--SQDQRVNRKILSII 105
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2515696781 497 T--MLAPGPHAFLVVVKIDRYTKE--EREAIKLIKDFFGS 532
Cdd:cd01853 106 KrfLKKKTIDVVLYVDRLDMYRVDnlDVPLLRAITDSFGP 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-893 |
3.41e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 593 LRKIKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQeeierekreieevftcEIEAKIKEMTEQRNITAQETELIK 672
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA----------------ELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 673 EKEELIRKEQEKIEREQEEKAKEKMRmmLEDEAKRIKWEKTSEDLENSVNATmgteeiymvmmKRETMAEEQEAWEKgRM 752
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRE--LEERLEELEEELAELEEELEELEE-----------ELEELEEELEEAEE-EL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 753 EYWDKVLSEEEQNQHENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEARKEAEN 832
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2515696781 833 RNDFLlnysmNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEE 893
Cdd:COG1196 434 EEEEE-----EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-831 |
1.25e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 611 EIFQEAEAAIQKEADRILKEKQEEIEREKreieevftcEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQE 690
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRR---------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 691 EKAK---EKMRMMLEDEAKRIKWEKTSEDLENSVNATMGTEEiymVMMKRETMAEEQEAWEKGRMEywdKVLSEEEQNQH 767
Cdd:COG1196 355 EAEAelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---ELAAQLEELEEAEEALLERLE---RLEEELEELEE 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515696781 768 ENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEARKEAE 831
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
565-894 |
1.53e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 565 LKKTIKDCGNRYQVFNNKDRNGDQVRELLRKIKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEIEREKREIEE 644
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 645 VFTCEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKWEKTSEDLENSVNAT 724
Cdd:pfam02463 778 EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 725 MGTEEIYMVMMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVL 804
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 805 EEL---QDTFEEKLEAFKKKYQ------EEARKEAENRNdfllnySMNVLDQMENDKRENDVVNQKKQQQKdlivqqlNK 875
Cdd:pfam02463 938 EELlleEADEKEKEENNKEEEEernkrlLLAKEELGKVN------LMAIEEFEEKEERYNKDELEKERLEE-------EK 1004
|
330
....*....|....*....
gi 2515696781 876 NKFFRKDFQRLQRKQEEEM 894
Cdd:pfam02463 1005 KKLIRAIIEETCQRLKEFL 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-926 |
1.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 582 KDRNGDQVR-ELLRKIKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEierekreieevftceiEAKIKEMTEQ 660
Cdd:PTZ00121 1574 EDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK----------------AEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 661 RNITAQETeliKEKEELIRKEQE--KIEREQEEKAKEkmrmmlEDEAKRIKWEKTSEDLENSVNATMGTEEiymvMMKRE 738
Cdd:PTZ00121 1638 LKKKEAEE---KKKAEELKKAEEenKIKAAEEAKKAE------EDKKKAEEAKKAEEDEKKAAEALKKEAE----EAKKA 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 739 TMAEEQEAWEKGRMEywdKVLSEEEqnqhENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAF 818
Cdd:PTZ00121 1705 EELKKKEAEEKKKAE---ELKKAEE----ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 819 KKKYQEEARKEAENRNDFLLNYSMNVLDQMEN----DKRENDVVNQKKQQQKDLIVQ-------QLNKNKFFRKDFQRLQ 887
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiiegGKEGNLVINDSKEMEDSAIKEvadsknmQLEEADAFEKHKFNKN 1857
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2515696781 888 RKQEEEMNHLLNTIGE-DNYDNGTEEITQliATHEEEIDK 926
Cdd:PTZ00121 1858 NENGEDGNKEADFNKEkDLKEDDEEEIEE--ADEIEKIDK 1895
|
|
| 3a0901s04IAP86 |
TIGR00993 |
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ... |
294-531 |
2.93e-06 |
|
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273381 [Multi-domain] Cd Length: 763 Bit Score: 51.11 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 294 SLSDEDERELETLQSIftsRVKdFIMILITVKCDPSAAAVQSFLKEnkhFLELCGHCRGRYFVLDVTdrqqvdqllhmve 373
Cdd:TIGR00993 41 TLSEEHKEKLEKLQLI---RVK-FLRLAQRLGQTPENSIAAQVLYR---LGLLAGRQGGGAFSLDAA------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 374 KTSAGESKCfigeimekpqseSGNAEVALStelttvphkpsqneecLRIVLIGKTGSGKSATANTILGrkcfESNACLSS 453
Cdd:TIGR00993 101 KAMAEQLEA------------EGQDPLDFS----------------LNILVLGKSGVGKSATINSIFG----EVKFSTDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 454 VtQCCQKETREI----NGQPIVVVDTPGLFDT---KLTDEEIKEELAKCITMLAPGphaflVVVKIDRYTKEEREA---- 522
Cdd:TIGR00993 149 F-GMGTTSVQEIeglvQGVKIRVIDTPGLKSSasdQSKNEKILSSVKKFIKKNPPD-----IVLYVDRLDMQTRDSndlp 222
|
250
....*....|
gi 2515696781 523 -IKLIKDFFG 531
Cdd:TIGR00993 223 lLRTITDVLG 232
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
649-833 |
3.32e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 649 EIEAKIKEMTEQRnitaqetelikekeeliRKEQEKIEREqeekakEKMRMMLEDEAKRIkwektsedlensvnatmgTE 728
Cdd:pfam15709 349 EVERKRREQEEQR-----------------RLQQEQLERA------EKMREELELEQQRR------------------FE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 729 EIYMVMMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENKMQLRKL-----REEYEKDVENYNRMKDAQLQKVKNENV 803
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELqrkkqQEEAERAEAEKQRQKELEMQLAEEQKR 467
|
170 180 190
....*....|....*....|....*....|..
gi 2515696781 804 LEELQDtfEEKLEAFKKKYQEE--ARKEAENR 833
Cdd:pfam15709 468 LMEMAE--EERLEYQRQKQEAEekARLEAEER 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
588-833 |
5.13e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 588 QVRELLRKIKLmvQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEIEREKREIEEVftcEIEAKIKEMTEQRNITAQE 667
Cdd:COG1196 226 EAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 668 TELIKEKEELIRKEQEKIEREQEEKAKEKMRmMLEDEAKRIKWEKTSEDLENSVNATmgTEEIYMVMMKRETMAEEQEAW 747
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 748 EKGRMEYWDKVLsEEEQNQHENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEAR 827
Cdd:COG1196 378 EEELEELAEELL-EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
....*.
gi 2515696781 828 KEAENR 833
Cdd:COG1196 457 EEEALL 462
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
565-934 |
1.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 565 LKKTIKDCGNRYQVFNNKDRNGDQVRELLRKIKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEIEREKREIEE 644
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 645 VFTCEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKAKEKMRM---MLEDEAKRIKWEKTSEDLENSV 721
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeaKKADEAKKAEEKKKADELKKAE 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 722 NATMGTEEIYMVMMKRET--------MAEEQEAWEKGRMEYWDKVL-------SEEEQNQHENKMQLRKLR--EEYEKDV 784
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEedknmalrKAEEAKKAEEARIEEVMKLYeeekkmkAEEAKKAEEAKIKAEELKkaEEEKKKV 1635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 785 ENYNRMKDAQLQK---VKNENVLEELQDTFEEKLEAFKKKYQEEARKEAENRNDfllnySMNVLDQMENDKRENDVVNQK 861
Cdd:PTZ00121 1636 EQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK-----AAEALKKEAEEAKKAEELKKK 1710
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515696781 862 KQQQKDLiVQQLNKNKFFRK-DFQRLQRKQEEEMNHLLNTIGEDNYDNGTEEITQLIATHEEEIDKWILEHIKK 934
Cdd:PTZ00121 1711 EAEEKKK-AEELKKAEEENKiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
650-893 |
1.41e-05 |
|
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: 48.38 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 650 IEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKW---EKTSEDLENSVNAtmg 726
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWkelEKEEEREEDERIL--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 727 tEEIYMVMMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHE----NKMQLRKLREEYEKDvenyNRMKDAQlQKVKNEN 802
Cdd:pfam13868 159 -EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEkaerDELRAKLYQEEQERK----ERQKERE-EAEKKAR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 803 VLEELQDTFEEKLEAFKKKYQEEARKEAENRNDFLLNY-SMNVLDQMENDKREndvvnQKKQQQKDLIVQQLNKNK---- 877
Cdd:pfam13868 233 QRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQaEDEEIEQEEAEKRR-----MKRLEHRRELEKQIEEREeqra 307
|
250 260
....*....|....*....|
gi 2515696781 878 ----FFRKDFQRLQRKQEEE 893
Cdd:pfam13868 308 aereEELEEGERLREEEAER 327
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-893 |
1.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 606 KSYTSEIFQEAEAAIQKEADrilKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKI 685
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 686 EREQEEKAKEKMRMMLE-----DEAKRIKWE--------KTSEDLENSVNATMGTEEIYMVMMKRETMAEEQEAWEKGRM 752
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEekkkaDEAKKKAEEakkadeakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 753 EYWDKVLSEEEQNQHENKMQLRKLRE-EYEKDVENYNRMKDA----QLQKVKNENVLEELQDTfEEKLEAFKKKYQEEAR 827
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAkkadEAKKAEEKKKADELKKA-EELKKAEEKKKAEEAK 1570
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2515696781 828 KEAENRNDFLlnYSMNVLDQMENDKRENDVVNQ-----------KKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEE 893
Cdd:PTZ00121 1571 KAEEDKNMAL--RKAEEAKKAEEARIEEVMKLYeeekkmkaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-926 |
1.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 582 KDRNGDQVRELLRKIKLMVQENQGKSYTSEIFQEAEAAiQKEADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQR 661
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 662 NiTAQETELIKEKEELiRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKWEKTSEDLENSVNATMGTEEIYMVMMKRETMA 741
Cdd:PTZ00121 1537 D-EAKKAEEKKKADEL-KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 742 EEQEAWEKGRMEYWDKVLSEEEQNQHENKMQLRKlrEEYEKDVENYNRMKDAQLQKVKNEN--VLEELQDTFEEKleafK 819
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK--AEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDE----K 1688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 820 KKYQEEARKEAENRNdfllnySMNVLDQMENDKRENDVVnQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEEMNHLLN 899
Cdd:PTZ00121 1689 KAAEALKKEAEEAKK------AEELKKKEAEEKKKAEEL-KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
330 340
....*....|....*....|....*..
gi 2515696781 900 TIGEDNyDNGTEEITQLIATHEEEIDK 926
Cdd:PTZ00121 1762 LKKEEE-KKAEEIRKEKEAVIEEELDE 1787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
581-868 |
7.61e-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: 46.59 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 581 NKDRNGDQVRELLRK------IKLMVQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEIEREKREIEEVFTCEIEAKI 654
Cdd:TIGR02168 705 KELEELEEELEQLRKeleelsRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 655 KEMTEQRNITAQETELIKEKEELIRKE--QEKIEREQEEKAKEKMRMMLEDEAKRI-----KWEKTSEDLEnSVNATMGT 727
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLedleeQIEELSEDIE-SLAAEIEE 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 728 EEIYMVMMKRET------MAEEQEAWEKGRMEYWDKV--LSEEEQNQHENKMQLRKLREEYEKDVENYNRMKdAQLQKVK 799
Cdd:TIGR02168 864 LEELIEELESELeallneRASLEEALALLRSELEELSeeLRELESKRSELRRELEELREKLAQLELRLEGLE-VRIDNLQ 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515696781 800 nENVLEELQDTFEE--KLEAFKKKYQEEAR---KEAENRNDFLLNYSMNVLDQMENDKRENDVVNqkkQQQKDL 868
Cdd:TIGR02168 943 -ERLSEEYSLTLEEaeALENKIEDDEEEARrrlKRLENKIKELGPVNLAAIEEYEELKERYDFLT---AQKEDL 1012
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
617-838 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 617 EAAIQKEADRILKEKQEEIEREKReieevftcEIEAKIKEMTEQRNITAQETELIKEKEELiRKEQEKIEREQEEKAKE- 695
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK--------ELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREEl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 696 -KMRMMLEDEAKRIKWEKTSEDLENSVNAtmgTEEIYMVMMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENKMQLR 774
Cdd:COG4717 119 eKLEKLLQLLPLYQELEALEAELAELPER---LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515696781 775 KLREEYEkDVENYNRMKDAQLQKVKNEnvLEELqdtfEEKLEAFKKKYQEEARKEAENRNDFLL 838
Cdd:COG4717 196 DLAEELE-ELQQRLAELEEELEEAQEE--LEEL----EEELEQLENELEAAALEERLKEARLLL 252
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
423-524 |
1.13e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 43.39 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 423 VLIGKTGSGKSATANTILGRKCFESnaclSSVTQCCQ----KETREINGQPIVVVDTPGLFD--------TKLT------ 484
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNVGIV----SPIPGTTRdpvrKEWELLPLGPVVLIDTPGLDEegglgrerVEEArqvadr 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2515696781 485 ----------DEEIKEELAKCITMLAPGPHAFLVVVKIDRYTKEEREAIK 524
Cdd:cd00880 77 adlvllvvdsDLTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELL 126
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
650-833 |
1.27e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 650 IEAKIKEMTEqrnitaqETELIKEKEElirKEQEKIEREQEEKAKEKMrmmledEAKRIKWEKTSEDLENSVNATmgtEE 729
Cdd:PRK12704 29 AEAKIKEAEE-------EAKRILEEAK---KEAEAIKKEALLEAKEEI------HKLRNEFEKELRERRNELQKL---EK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 730 IymVMMKRETMAEEQEAWEK--GRMEYWDKVLSEEEQNQHENKMQLRKLREEYEKDVENYnrmkdAQLQK--VKNEnVLE 805
Cdd:PRK12704 90 R--LLQKEENLDRKLELLEKreEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-----SGLTAeeAKEI-LLE 161
|
170 180
....*....|....*....|....*...
gi 2515696781 806 ELQDTFEEKLEAFKKKYQEEARKEAENR 833
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIEEEAKEEADKK 189
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
614-898 |
3.53e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 614 QEAEAAIQKEADRILKEKQEEIEREKREIEevftcEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKA 693
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIQE-----EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 694 KEKMRMMLEDEAKRIKWEKTSEDLENSVNATMGTeeiyMVMMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENKMQL 773
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRA----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 774 RK-LREEYEKDVENYNRMKDAQLQKVKNEnvleelqdtFEEKLEAFKKKYQEEaRKEAENRNDFLLNYSMNVLDQMEndk 852
Cdd:pfam13868 234 RQeLQQAREEQIELKERRLAEEAEREEEE---------FERMLRKQAEDEEIE-QEEAEKRRMKRLEHRRELEKQIE--- 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2515696781 853 rendvvnQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEEMNHLL 898
Cdd:pfam13868 301 -------EREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
756-923 |
3.82e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 756 DKVLSEEEQNQHENKMQLRKLREEYEKDVENYNRmKDAQLQKVKNE-NVLEELQDTFEEKLEAFKKKYQEEARK------ 828
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNE-LQAELEALQAEiDKLQAEIAEAEAEIEERREELGERARAlyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 829 ---------EAENRNDFLLNYSM---------NVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQ 890
Cdd:COG3883 101 svsyldvllGSESFSDFLDRLSAlskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190
....*....|....*....|....*....|...
gi 2515696781 891 EEEMNHLlntigEDNYDNGTEEITQLIATHEEE 923
Cdd:COG3883 181 EALLAQL-----SAEEAAAEAQLAELEAELAAA 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
613-893 |
4.78e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 613 FQEAEAAIQKEADRilKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRNITAQETELIKEKEElIRKEQEKIEREQEEK 692
Cdd:PTZ00121 1265 FARRQAAIKAEEAR--KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE-AKKKADAAKKKAEEA 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 693 AKekmrmmlEDEAKRIKWEKTSEDLENSvnatmgteeiymvmmkretmAEEQEAWEKGRMEywDKVLSEEEQNQHENKMQ 772
Cdd:PTZ00121 1342 KK-------AAEAAKAEAEAAADEAEAA--------------------EEKAEAAEKKKEE--AKKKADAAKKKAEEKKK 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 773 LRKLREEYEKDVENYNRMKDAQLQKVKNENV---LEELQDTFEEKLEAFKKKYQEEARKEAENRNDfllnySMNVLDQME 849
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-----AEEAKKKAE 1467
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2515696781 850 NDKRENDVvnQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEE 893
Cdd:PTZ00121 1468 EAKKADEA--KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
611-892 |
6.31e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 611 EIFQEAEAAIQKEADRILKEKQEEIEREKREIEEvftcEIEAKIKEMTEQRNITAQETELIKEKEEL-----IRKEQEKI 685
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDAR----KAEAARKAEEERKAEEARKAEDAKKAEAVkkaeeAKKDAEEA 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 686 EREQEEKAKEKMRMMLEDEAKRIKWEKTSEDLENSVNAtmgtEEIYMVMMKREtmAEEQEAWEKGRMEYWDKVLSEEEQN 765
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELKKAEEKKK--ADEAKKAEEKKKADEAKKKAEEAKK 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 766 QHENKM---QLRKLREEYEKDVEnyNRMKDAQLQKVKNENVLEELQDTfEEKLEAFKKKYQEEARK-EAENRNDFLLNYS 841
Cdd:PTZ00121 1317 ADEAKKkaeEAKKKADAAKKKAE--EAKKAAEAAKAEAEAAADEAEAA-EEKAEAAEKKKEEAKKKaDAAKKKAEEKKKA 1393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2515696781 842 MNVLDQMENDKRENDVVNQKKQQQKDliVQQLNKNKFFRKDFQRLQRKQEE 892
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKKAEE 1442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
614-831 |
8.62e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 614 QEAEAAIQKEADRILKEKQEEIEREKREIeevftcEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKA 693
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLA------ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 694 KEKMRMMLE----DEAKRIKWEKTSEDLENSVNATMGTEEIYMVMMKR-ETMAEEQEAWEKGRMEywdkvLSEEEQNQHE 768
Cdd:COG4942 104 EELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAE-----LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2515696781 769 NKMQLRKLREEYEKDVENYNR-MKDAQLQKVKNENVLEELQDTfEEKLEAFKKKYQEEARKEAE 831
Cdd:COG4942 179 LLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
587-915 |
9.99e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 587 DQVRELLRKIKL----MVQENQGKSYTSEIFQEAEAAIQKE--ADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQ 660
Cdd:pfam05483 268 DKANQLEEKTKLqdenLKELIEKKDHLTKELEDIKMSLQRSmsTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 661 RNITAQETELIKEKEELIRKEQEKIEREQEEKAKEKMRMmledeakrikwEKTSEDLENSV----NATMGTEEIYMVMMK 736
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL-----------QKKSSELEEMTkfknNKEVELEELKKILAE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 737 RETMAEEQEAWEK------GRMEYWDKVLSEEEQNQHENKMQLRKLR---EEYEKDVENYN------RMKDAQLQKVKNE 801
Cdd:pfam05483 417 DEKLLDEKKQFEKiaeelkGKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKtelekeKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 802 NVLEELQDTFEEKLEAFKKKYQEEARKEAENRNDFLLNYSMNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRK 881
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
330 340 350
....*....|....*....|....*....|....*....
gi 2515696781 882 DFQRLQRKQEEEMNHLLNTIGE-----DNYDNGTEEITQ 915
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNlkkqiENKNKNIEELHQ 615
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
592-753 |
1.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 592 LLRKIKLMVQENQGKSYTSEIFQEAEaaiqKEADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRNITAQETELI 671
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAK----KEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 672 KEKEELIRKEQEKIE-REQEEKAKEKMRMMLEDEAKRIKwEKTSEDLENSvnATMGTEE---IYMVMMKRETMAE----- 742
Cdd:PRK12704 99 DRKLELLEKREEELEkKEKELEQKQQELEKKEEELEELI-EEQLQELERI--SGLTAEEakeILLEKVEEEARHEaavli 175
|
170
....*....|....
gi 2515696781 743 ---EQEAWEKGRME 753
Cdd:PRK12704 176 keiEEEAKEEADKK 189
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
649-831 |
1.68e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.75 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 649 EIEAKIKEMTEQRNITAQETELIKEKEElIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKWEKTsedlensvnatmgte 728
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLE-QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA--------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 729 eiymvmmKRETMAEEQEAWEKgrmeywdKVLSEEEQNQHENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQ 808
Cdd:TIGR02794 111 -------AKQAEEKQKQAEEA-------KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAE 176
|
170 180
....*....|....*....|...
gi 2515696781 809 DTFEEKLEAFKKKYQEEARKEAE 831
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAEEAKAKAE 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-899 |
1.86e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 651 EAKIKEMTeqrnitaQETELIKEKEELIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKWEKTSEDLEnsvnatmgteei 730
Cdd:TIGR02168 676 RREIEELE-------EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA------------ 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 731 ymvmmkRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENKMQLRKLREEYEKDVENynrmKDAQLQKVKNENvleelqDT 810
Cdd:TIGR02168 737 ------RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEEL------KA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 811 FEEKLEAFKKKYQEEARKEAENRNDfllnysmnvLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQ 890
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRER---------LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
....*....
gi 2515696781 891 EEEMNHLLN 899
Cdd:TIGR02168 872 ESELEALLN 880
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
423-515 |
1.98e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 39.63 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 423 VLIGKTGSGKSATANTILGRKCFESNACLSSVTQcCQKETREINGQPIVVVDTPGLFDTKLTDEEIKEELAKcitmLAPG 502
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRA-AQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRR----LLPE 75
|
90
....*....|...
gi 2515696781 503 PHAFLVVVKIDRY 515
Cdd:cd11383 76 ADLVLWLLDADDR 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
653-893 |
2.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 653 KIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKweKTSEDLENSVNATmgTEEIYM 732
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR--LELEELELELEEA--QAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 733 VMMKRETMAEEQEAWEKGRMEYWDKVLSEEEQNQHENKM------QLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEE 806
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEleeleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 807 LQDTFEEKLEAFKKKYQEEARKEAENRNDfLLNYSMNVLDQMENDKRENDVVNQKKQQQKDLIVQQLNKNKFFRKDFQRL 886
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
....*..
gi 2515696781 887 QRKQEEE 893
Cdd:COG1196 452 AELEEEE 458
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
419-535 |
2.34e-03 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 39.75 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 419 CLRIVLIGKTGSGKSATANTILGRKcfesnacLSSVT---QCCQKETREI----NGQpIVVVDTPGLF--DTKL------ 483
Cdd:cd04163 3 SGFVAIIGRPNVGKSTLLNALVGQK-------ISIVSpkpQTTRNRIRGIytddDAQ-IIFVDTPGIHkpKKKLgermvk 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2515696781 484 -----------------TDEEIKEELAKCITMLAP--GPHaFLVVVKIDRYTKEER--EAIKLIKDFFGSKAV 535
Cdd:cd04163 75 aawsalkdvdlvlfvvdASEWIGEGDEFILELLKKskTPV-ILVLNKIDLVKDKEDllPLLEKLKELHPFAEI 146
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
613-899 |
3.15e-03 |
|
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: 41.50 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 613 FQEAEAAIQKEADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEK 692
Cdd:pfam02463 195 LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 693 AKEKMRMMLEDEakrikWEKTSEDLENSVNATMGTEEIYMVMMKRETMAEEQEAwekgrmeywdKVLSEEEQNQHENKMQ 772
Cdd:pfam02463 275 KEEEKEKKLQEE-----ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK----------KKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 773 LRKLREEYE-KDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKkyqeeARKEAENRNDFLLNYSMNVLDQMEND 851
Cdd:pfam02463 340 LEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS-----AAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2515696781 852 KRENDvVNQKKQQQKDLIVQQLNKNKFFRKDFQRLQRKQEEEMNHLLN 899
Cdd:pfam02463 415 RQLED-LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
653-831 |
3.99e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 653 KIKEMTEQRNItaqETELIKEKEELIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKWEKTSEdlensvnatmgteeiym 732
Cdd:COG2268 193 KIAEIIRDARI---AEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAE----------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 733 vmMKRETMAEEQEAwekgrmeywDKVLSEEEQNQhenkmqlrklREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFE 812
Cdd:COG2268 253 --ERREAETARAEA---------EAAYEIAEANA----------EREVQRQLEIAEREREIELQEKEAEREEAELEADVR 311
|
170
....*....|....*....
gi 2515696781 813 EKLEAFKKKYQEEARKEAE 831
Cdd:COG2268 312 KPAEAEKQAAEAEAEAEAE 330
|
|
| 3a0901s02IAP34 |
TIGR00991 |
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ... |
420-531 |
4.29e-03 |
|
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding proteins, Nucleosides, purines and pyrimidines]
Pssm-ID: 130064 Cd Length: 313 Bit Score: 40.27 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 420 LRIVLIGKTGSGKSATANTILGRKC-----FESNACLSSVTqccqkeTREINGQPIVVVDTPGLFDTKLTDEE----IKE 490
Cdd:TIGR00991 39 LTILVMGKGGVGKSSTVNSIIGERIatvsaFQSEGLRPMMV------SRTRAGFTLNIIDTPGLIEGGYINDQavniIKR 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2515696781 491 -ELAKCITMLapgphafLVVVKIDRYTKE--EREAIKLIKDFFG 531
Cdd:TIGR00991 113 fLLGKTIDVL-------LYVDRLDAYRVDtlDGQVIRAITDSFG 149
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
583-834 |
7.29e-03 |
|
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: 40.34 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 583 DRNGDQVRELLRKIKLMvQENQGKSYTSEIFQEAEAAIQKEADRILKEKQEEIEREKREIEEVFTCEIEAKIKEMTEQRN 662
Cdd:pfam02463 268 AQVLKENKEEEKEKKLQ-EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 663 ITAQETELIKEKEELIRKEQEKIEREQEEKAKEKMRMMLEDEAKRIKWEKTSEDLENSVNATMGTEEIYMVMMKRETMAE 742
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 743 EQEAWEKGRMEYWDKVLSEEEQNQHENKMQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKY 822
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
250
....*....|..
gi 2515696781 823 QEEARKEAENRN 834
Cdd:pfam02463 507 SGLKVLLALIKD 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
616-835 |
9.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 616 AEAAIQKEADRILKEKQEEIERekreieevftceIEAKIKEMTEQRNITAQETELIKEKEELIRKEQEKIEREQEEKAKE 695
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAE------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515696781 696 KMRMMLEDEAKRIKWEKTSEDLENSVNA--TMGTEEIYMVMMKRETMAEEQEawekgRMEYWDKV---LSEEEQNQHENK 770
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVR-----RLQYLKYLapaRREQAEELRADL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2515696781 771 MQLRKLREEYEKDVENYNRMKDAQLQKVKNENVLEELQDTFEEKLEAFKKKYQEEARKEAENRND 835
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| |
