|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
196-844 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 568.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 196 ILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGERPAFTQEKRYLHRDGTVLWGRVTVTLIRNEQMH 275
Cdd:COG5001 23 LLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 276 PDYLMVVLENIDPIRRHAEQLKLSHRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFY 355
Cdd:COG5001 103 LLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 356 ADMYHALERVGIWRGEVWNKRKNGKLYPQQLMISAVREGGKISQYIAIFS---DLSQTKLAEQKIAAQANYDNLTGLPNR 432
Cdd:COG5001 183 ALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAiarLITERKRAEERLRHLAYHDPLTGLPNR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 433 WLF----GRCLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGGDEFAFLVPGIV 508
Cdd:COG5001 263 RLFldrlEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLD 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 509 NRRQAEVFAKQVIGGFARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGRplGT---YNASMREEV 585
Cdd:COG5001 343 DPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGR--NRyrfFDPEMDERA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 586 SQRHQMQHDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRD 665
Cdd:COG5001 421 RERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQ 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 666 LARLQQSGFPDLQMSINRSTLEFQtiDPE-ANEWLRVIRHFELDPADIIIEITESLLMETSDQHRVRIDALREAGCKLAI 744
Cdd:COG5001 501 LAAWQDAGLPDLRVAVNLSARQLR--DPDlVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIAL 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 745 DDFGTGYSALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGY 824
Cdd:COG5001 579 DDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGY 658
|
650 660
....*....|....*....|
gi 743523847 825 LLSRPLPFDDLTEYLSLNRQ 844
Cdd:COG5001 659 LFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
279-839 |
2.24e-108 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 344.85 E-value: 2.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 279 LMVVLENIDPIRRHAEQLKLSHRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADM 358
Cdd:COG2200 12 LLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 359 YHALERVGIWRGEVWNKRKNGKLYPQQLMISAVREGGKISQYIAIFSDLSQTKLAEQKIAAQANYDNLTGLPNRWLFGR- 437
Cdd:COG2200 92 LLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLl 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 438 ----CLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGGDEFAFLVPGIVNRRQA 513
Cdd:COG2200 172 llllLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 514 EVFAKQVIGGFARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGRPLGTYNASMREEVSQRHQMQH 593
Cdd:COG2200 252 AAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALES 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 594 DLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQSG 673
Cdd:COG2200 332 ELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 674 FpDLQMSINRSTLEFQtiDPEANEWLR-VIRHFELDPADIIIEITESLLMETSDQHRVRIDALREAGCKLAIDDFGTGYS 752
Cdd:COG2200 412 L-DLRLSVNLSARSLL--DPDFLERLLeLLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYS 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 753 ALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPF 832
Cdd:COG2200 489 SLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPL 568
|
....*..
gi 743523847 833 DDLTEYL 839
Cdd:COG2200 569 EELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
593-834 |
1.96e-97 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 304.08 E-value: 1.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 593 HDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQs 672
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 673 GFPDLQMSINRSTLEFQTIDpEANEWLRVIRHFELDPADIIIEITESLLMETSDQHRVRIDALREAGCKLAIDDFGTGYS 752
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPD-FLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 753 ALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPF 832
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
..
gi 743523847 833 DD 834
Cdd:cd01948 239 EE 240
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
156-837 |
7.62e-89 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 304.67 E-value: 7.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 156 LMYQQRQSQEQPAQPEHHhfLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALY 235
Cdd:PRK09776 267 VMYAFRAERKHISESETR--FRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 236 DALKRGERPAFTQEKRYLHRDGTVLWGRVTVTLIRNEQMHPDYLMVVLENIDPiRRHAEQL--KLSHRV----------- 302
Cdd:PRK09776 345 EKLLSGEINSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINE-LKRTEQVneRLMERItlaneaggigi 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 --------------------------------------------------------------------------------
Cdd:PRK09776 424 wewdlkpniiswdkrmfelyeipphikptwqvwyaclhpedrqrvekeirdalqgrspfklefrivvkdgvrhiralanr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 303 --------------------------------------YDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQrPsm 344
Cdd:PRK09776 504 vlnkdgeverllginmdmtevrqlnealfqekerlhitLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGV-P-- 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 345 lksglHDQTFYA----------DMYHALER---VGIWRGEVWNKRkNGKLYPQQLMISAVR--EGGKISQyIAIFSDLSQ 409
Cdd:PRK09776 581 -----LLTVLHItfgdngplmeNIYSCLTSrsaAYLEQDVVLHCR-SGGSYDVHYSITPLStlDGENIGS-VLVIQDVTE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 410 TKLAEQKIAAQANYDNLTGLPNRWLFGRCLARFC----ERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSR 485
Cdd:PRK09776 654 SRKMLRQLSYSASHDALTHLANRASFEKQLRRLLqtvnSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSM 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 486 VRTEDLVARIGGDEFAFLVPGiVNRRQAEVFAKQVIGGF-ARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQAL 564
Cdd:PRK09776 734 LRSSDVLARLGGDEFGLLLPD-CNVESARFIATRIISAInDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIAC 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 565 FVAKRQGRPLGT-YNASMREEVSQRHQMqhDLAEA---IKLGQLTMAYQPIWDNRSGRVAKL-EALVRWYHPHWGQVSPA 639
Cdd:PRK09776 813 YAAKNAGRGRVTvYEPQQAAAHSEHRAL--SLAEQwrmIKENQLMMLAHGVASPRIPEARNHwLISLRLWDPEGEIIDEG 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 640 DFIPLAEEAGLIQGLGALVLWQSCRDLA-RLQQsgfPDLQMSINRS--TLEFQTIDPEAnewLRVIRHFELDPADIIIEI 716
Cdd:PRK09776 891 AFRPAAEDPALMHALDRRVIHEFFRQAAkAVAS---KGLSIALPLSvaGLSSPTLLPFL---LEQLENSPLPPRLLHLEI 964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 717 TESLLMETSDQHRVRIDALREAGCKLAIDDFGTGYSALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLG 796
Cdd:PRK09776 965 TETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLG 1044
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 743523847 797 MQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPFDDLTE 837
Cdd:PRK09776 1045 MKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLN 1085
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
307-839 |
7.26e-86 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 287.35 E-value: 7.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 307 SEA---ILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLksglhdqtFYADMYHALERVGI---------WRGEVWN 374
Cdd:PRK10060 118 SEAnsvIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKL--------FMSRREAAASRRNIrgffrsgnaYEVERWI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 375 KRKNGklypQQLMI---SAVREG-GKISQY-IAIFSDLSQTKLAEQKIAAQANYDNLTGLPNRWLFGRCLARFCER--GE 447
Cdd:PRK10060 190 KTRKG----QRLFLfrnKFVHSGsGKNEIFlICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAadNN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 448 RFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGGDEFAFLVPgivNRRQA--EVFAKQVIGGFA 525
Cdd:PRK10060 266 QVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAS---HTSQAalEAMASRILTRLR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 526 RPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGRplGTY---NASMREEVSQRHQMQHDLAEAIKLG 602
Cdd:PRK10060 343 LPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGR--GQFcvfSPEMNQRVFEYLWLDTNLRKALEND 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 603 QLTMAYQPIWDNRsGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQSGFpDLQMSIN 682
Cdd:PRK10060 421 QLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NLRVAVN 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 683 RST--LEFQTIdpeANEWLRVIRHFELDPADIIIEITESLLMETSDQHRVRIDALREAGCKLAIDDFGTGYSALNYLRTF 760
Cdd:PRK10060 499 VSArqLADQTI---FTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARF 575
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523847 761 PVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPFDDLTEYL 839
Cdd:PRK10060 576 PIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWY 654
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
593-834 |
3.85e-85 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 271.78 E-value: 3.85e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 593 HDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQS 672
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 673 GFPDLQMSINRSTLEFQtiDPEANEWLR-VIRHFELDPADIIIEITESLLMETSDQHRVRIDALREAGCKLAIDDFGTGY 751
Cdd:smart00052 82 GPPPLLISINLSARQLI--SPDLVPRVLeLLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 752 SALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLP 831
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
...
gi 743523847 832 FDD 834
Cdd:smart00052 240 LDD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
195-840 |
1.66e-82 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 281.66 E-value: 1.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 195 KILWANPAIEKMLGYSQEELQQLTVAEI-NHPDDWQTSIALYDALKRGeRPAFTQEKRYLHRDGTVLWGRVTVTLIRNEQ 273
Cdd:PRK11359 157 RIVQCNRAFTEMFGYCISEASGMQPDTLlNIPEFPADNRIRLQQLLWK-TARDQDEFLLLTRTGEKIWIKASISPVYDVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 274 MHPDYLMVVLENIDpirrhaeqlklSHRVYDNLSEAILVCDADSriisvnPAFEKITGY----SEEEACGQRPSMLKsgL 349
Cdd:PRK11359 236 AHLQNLVMTFSDIT-----------EERQIRQLEGNILAAMCSS------PPFHEMGEIicrnIESVLNESHVSLFA--L 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 350 HDQT--FYADMYHALE--RVGIWRGEVwnKRKNGKlyPQQLMISAVREGGKISQYIAIFSDLSQ--TKLA------EQKI 417
Cdd:PRK11359 297 RNGMpiHWASSSHGAEyqNAQSWSATI--RQRDGA--PAGTLQIKTSSGAETSAFIERVADISQhlAALAleqeksRQHI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 418 AAQANYDNLTGLPNRWLFGRCLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGG 497
Cdd:PRK11359 373 EQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 498 DEFAFLVPGIVNRRqAEVFAKQVIGGFARPFMLANQHLYVTATLGITLcpNDGGDSDELLRNAEQAL-FVAKRQGRPLGT 576
Cdd:PRK11359 453 TQFVLVSLENDVSN-ITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMdYIRKNGGNGWQF 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 577 YNASMREEVSQRHQMQHDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGA 656
Cdd:PRK11359 530 FSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 657 LVLWQSCRDLARLQQSGFPDLQMSINRSTLEFQTiDPEANEWLRVIRHFELDPADIIIEITESLLMETSDQHRVRIDALR 736
Cdd:PRK11359 610 WVIAEACRQLAEWRSQNIHIPALSVNLSALHFRS-NQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 737 EAGCKLAIDDFGTGYSALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQK 816
Cdd:PRK11359 689 DMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKI 768
|
650 660
....*....|....*....|....
gi 743523847 817 GCAFTQGYLLSRPLPFDDLTEYLS 840
Cdd:PRK11359 769 HCRVIQGYFFSRPLPAEEIPGWMS 792
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
594-829 |
4.60e-75 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 244.53 E-value: 4.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 594 DLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQsg 673
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 674 FPDLQMSINRSTLEFQtiDPEANEWLRVI-RHFELDPADIIIEITESLLMETSDQHRVRIDALREAGCKLAIDDFGTGYS 752
Cdd:pfam00563 81 GPDIKLSINLSPASLA--DPGFLELLRALlKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743523847 753 ALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRP 829
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
587-844 |
1.44e-69 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 239.43 E-value: 1.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 587 QRHQMQHDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDL 666
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 667 ARLQQSgFPDLQMSINRSTLEFQtiDPEANEWL-RVIRHFELDPADIIIEITESLLMETsDQHRVRIDALREAGCKLAID 745
Cdd:COG4943 348 GDLLAA-DPDFHISINLSASDLL--SPRFLDDLeRLLARTGVAPQQIVLEITERGFIDP-AKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 746 DFGTGYSALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYL 825
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|....*....
gi 743523847 826 LSRPLPFDDLTEYLSLNRQ 844
Cdd:COG4943 504 FAKPLPAEEFIAWLAAQRA 522
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
427-840 |
9.88e-66 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 232.53 E-value: 9.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 427 TGLPNRWLFGRCLARFC---ERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGGDEFAFL 503
Cdd:PRK11829 238 TELPNRSLFISLLEKEIassTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 504 VPGIVNRRQAEVFAKQVIGGFARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGR-PLGTYNASMR 582
Cdd:PRK11829 318 ARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRnQIMVFEPHLI 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 583 EEVSQRHQMQHDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQS 662
Cdd:PRK11829 398 EKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 663 CRDLARLQQSGFpDLQMSINRSTLefQTIDPEANEWLR-VIRHFELDPADIIIEITESllMETSDQHRV--RIDALREAG 739
Cdd:PRK11829 478 CRILADWKARGV-SLPLSVNISGL--QVQNKQFLPHLKtLISHYHIDPQQLLLEITET--AQIQDLDEAlrLLRELQGLG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 740 CKLAIDDFGTGYSALNYLR---TFPVDLVKIDRSFVRHIPfneQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQK 816
Cdd:PRK11829 553 LLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEH 629
|
410 420
....*....|....*....|....*
gi 743523847 817 GCAFTQGYLLSRPLPFDD-LTEYLS 840
Cdd:PRK11829 630 GIQCGQGFLFSPPLPRAEfEAQYFS 654
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
406-840 |
3.93e-65 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 230.37 E-value: 3.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 406 DLSQTKLAEQ--KIAAQANYDNLTGLPNRWLFGRCLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLV 483
Cdd:PRK13561 214 NLNQQLLQRQyeEQSRNATRFPVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 484 SRVRTEDLVARIGGDEFAFLVPGIVNRRQAEVFAKQVIGGFARPFMLANQHLYVTATLGITLcpNDGGDS-DELLRNAEQ 562
Cdd:PRK13561 294 SVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAM--FYGDLTaEQLYSRAIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 563 ALFVAKRQGR-PLGTYNASMREEVSQRHQMQHDLAEAIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADF 641
Cdd:PRK13561 372 AAFTARRKGKnQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 642 IPLAEEAGLIQGLGALVLWQSCRDLARLQQSGFpDLQMSINRSTLEFQTIDpEANEWLRVIRHFELDPADIIIEITESLL 721
Cdd:PRK13561 452 IDRIESCGLMVTVGHWVLEESCRLLAAWQERGI-MLPLSVNLSALQLMHPN-MVADMLELLTRYRIQPGTLILEVTESRR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 722 METSDQHRVRIDALREAGCKLAIDDFGTGYSALNYL---RTFPVDLVKIDRSFVRHIPfneQDRLLLDGIINIVHNLGMQ 798
Cdd:PRK13561 530 IDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLP---EDDSMVAAIIMLAQSLNLQ 606
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 743523847 799 VVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPFDDLTE-YLS 840
Cdd:PRK13561 607 VIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEErYLE 649
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
397-572 |
1.68e-50 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 179.02 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 397 ISQYIAIFSDLSQTKLAEQKIAAQANYDNLTGLPNRWLFGRCLARFCER----GERFALMVLDLNNFKAVNNSMDHHVGD 472
Cdd:COG2199 90 LLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 473 ALLREVSDRLVSRVRTEDLVARIGGDEFAFLVPGIvNRRQAEVFAKQVIGGFAR-PFMLANQHLYVTATLGITLCPNDGG 551
Cdd:COG2199 170 EVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGD 248
|
170 180
....*....|....*....|.
gi 743523847 552 DSDELLRNAEQALFVAKRQGR 572
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGR 269
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
422-572 |
6.67e-50 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 172.74 E-value: 6.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 422 NYDNLTGLPNRWLF----GRCLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGG 497
Cdd:cd01949 1 YTDPLTGLPNRRAFeerlERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743523847 498 DEFAFLVPGiVNRRQAEVFAKQVIGGFARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGR 572
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGR 154
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
598-840 |
3.45e-47 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 176.34 E-value: 3.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 598 AIKLGQLTMAYQPIWDNRSGRVAKLEALVRWYHPHWGQVSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQSGFPDL 677
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLPVGA 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 678 QMSINRSTLEFQTID--PEANEWLRVI--RHFEldpadIIIEITESLLMETSDQHRVrIDALREAGCKLAIDDFGTGYSA 753
Cdd:PRK10551 351 KLGINISPAHLHSDSfkADVQRLLASLpaDHFQ-----IVLEITERDMVQEEEATKL-FAWLHSQGIEIAIDDFGTGHSA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 754 LNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPFD 833
Cdd:PRK10551 425 LIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLE 504
|
....*..
gi 743523847 834 DLTEYLS 840
Cdd:PRK10551 505 DFVRWLK 511
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
420-572 |
2.86e-43 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 154.33 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 420 QANYDNLTGLPNRWLF----GRCLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARI 495
Cdd:smart00267 2 LAFRDPLTGLPNRRYFeeelEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743523847 496 GGDEFAFLVPGiVNRRQAEVFAKQVIGGFARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGR 572
Cdd:smart00267 82 GGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGR 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
421-572 |
6.71e-42 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 150.48 E-value: 6.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 421 ANYDNLTGLPNRWLF----GRCLARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIG 496
Cdd:pfam00990 1 AAHDPLTGLPNRRYFeeqlEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743523847 497 GDEFAFLVPGIVNRRQAEV--FAKQVIGGFARPFMLANQHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGR 572
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELaeRIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
164-417 |
9.21e-37 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 139.00 E-value: 9.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 164 QEQPAQPEHHHFLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGER 243
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 244 PaFTQEKRYLHRDGTVLWGRVTVTLIRNEQMHPDYLMVVLENIDPIRRHAEQLKLSHRVY----DNLSEAILVCDADSRI 319
Cdd:COG2202 81 V-WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLrllvENAPDGIFVLDLDGRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 320 ISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALER-VGIWRGEVWNKRKNGKLYPQQLMISAVREGGKIS 398
Cdd:COG2202 160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGgRESYELELRLKDGDGRWVWVEASAVPLRDGGEVI 239
|
250
....*....|....*....
gi 743523847 399 QYIAIFSDLSQTKLAEQKI 417
Cdd:COG2202 240 GVLGIVRDITERKRAEEAL 258
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
175-417 |
2.07e-31 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 129.32 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 175 FLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGERPAFTqEKRYLH 254
Cdd:COG5809 16 RFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDEL-EFELRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 255 RDGTVLWGRVTVTLIRNEQMHPDYLMVVLENIDPIRRHAEQLKLSHR----VYDNLSEAILVCDADSRIISVNPAFEKIT 330
Cdd:COG5809 95 KNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEkfrlIFNHSPDGIIVTDLDGRIIYANPAACKLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 331 GYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVGIWRGEVWNKRKNGKLYPQQLMISAVREGGKISQYIAIFSDLSQT 410
Cdd:COG5809 175 GISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITER 254
|
....*..
gi 743523847 411 KLAEQKI 417
Cdd:COG5809 255 KKLEELL 261
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
420-572 |
5.05e-30 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 116.67 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 420 QANYDNLTGLPNR---WLFGRCLARFCERGER-FALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARI 495
Cdd:TIGR00254 1 QAVRDPLTGLYNRrylEEMLDSELKRARRFQRsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523847 496 GGDEFAFLVPGiVNRRQAEVFAKQVIGGF-ARPFMLAN-QHLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGR 572
Cdd:TIGR00254 81 GGEEFVVILPG-TPLEDALSKAERLRDAInSKPIEVAGsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGR 158
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
290-522 |
3.67e-29 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 117.05 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 290 RRHAEQLKLSHRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVGIWR 369
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 370 GEVWNKRKNGKLYPQQLMISAVR-EGGKISQYIAIFSDLSQTKLAEQKIAAQANYDNLTGLPNR---WLF---GRCLaRF 442
Cdd:COG2202 84 GELRNRRKDGSLFWVELSISPVRdEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPdgiFVLdldGRIL-YV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 443 CERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARI-GGDEFAFLVPGIVNRRQAEVFAKQVI 521
Cdd:COG2202 163 NPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLkDGDGRWVWVEASAVPLRDGGEVIGVL 242
|
.
gi 743523847 522 G 522
Cdd:COG2202 243 G 243
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
424-572 |
9.14e-23 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 102.29 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 424 DNLTGLPNRWLFGRCLA----RFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARIGGDE 499
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKnlieRANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743523847 500 FAFLVPGIvNRRQAEVFA---KQVIGGfaRPFMLANQ--HLYVTATLGITLCPNDGGDSDELLRNAEQALFVAKRQGR 572
Cdd:PRK09581 375 FVVVMPDT-DIEDAIAVAeriRRKIAE--EPFIISDGkeRLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGR 449
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
175-296 |
2.60e-21 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 90.04 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 175 FLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGERPAFTQEKRYLH 254
Cdd:TIGR00229 4 RYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRR 83
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 743523847 255 RDGTVLWGRVTVTLIRNEQMHPDYLMVVlENIDPIRRHAEQL 296
Cdd:TIGR00229 84 KDGSEIWVEVSVSPIRTNGGELGVVGIV-RDITERKEAEEAL 124
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
420-572 |
5.28e-20 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 94.70 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 420 QANYDNLTGLPNRWLF---GRCLARFCER-GERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARI 495
Cdd:PRK15426 397 QAWHDPLTRLYNRGALfekARALAKRCQRdQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 496 GGDEFAFLVPGIvNRRQAEVFAKQVIGGFARPFMLA--NQHLYVTATLGITLCPNDG-GDSDELLRNAEQALFVAKRQGR 572
Cdd:PRK15426 477 GGEEFCVVLPGA-SLAEAAQVAERIRLRINEKEILVakSTTIRISASLGVSSAEEDGdYDFEQLQSLADRRLYLAKQAGR 555
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
176-418 |
1.89e-18 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 89.41 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 176 LDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGERPAFTQEKRylHR 255
Cdd:COG5805 36 LETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIY--CK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 256 DGTVLWGRVTVTLIRNEQMHPDYLmvVLENIDPIRRHAEQLKLSHRVY----DNLSEAILVCDADSRIISVNPAFEKITG 331
Cdd:COG5805 114 DGELIYVEVKLFPIYNQNGQAAIL--ALRDITKKKKIEEILQEQEERLqtliENSPDLICVIDTDGRILFINESIERLFG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 332 YSEEEacgqrpsMLKSGLHDQTFYAD---MYHALERVgiwrGEVWNKR--------KNGKLYPQQLMISAVREG-GKISQ 399
Cdd:COG5805 192 APREE-------LIGKNLLELLHPCDkeeFKERIESI----TEVWQEFiiereiitKDGRIRYFEAVIVPLIDTdGSVKG 260
|
250
....*....|....*....
gi 743523847 400 YIAIFSDLSQTKLAEQKIA 418
Cdd:COG5805 261 ILVILRDITEKKEAEELMA 279
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
418-572 |
2.55e-18 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 86.27 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 418 AAQANYDNLTGLPNRWLFGRCL--ARFCERGERFALMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRTEDLVARI 495
Cdd:PRK09894 126 TIRSNMDVLTGLPGRRVLDESFdhQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 496 GGDEFAFLVPGIVNRRQAEVFAK--QVIGgfARPFMLANQHLYVTATLGITLCpnDGGDS-DELLRNAEQALFVAKRQGR 572
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERirQLIA--NHAITHSDGRINITATFGVSRA--FPEETlDVVIGRADRAMYEGKQTGR 281
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
303-417 |
4.83e-18 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 80.80 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 303 YDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALE-RVGIWRGEVWNKRKNGKL 381
Cdd:TIGR00229 9 FESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEgEPEPVSEERRVRRKDGSE 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 743523847 382 YPQQLMISAVREGGKISQYIAIFSDLSQTKLAEQKI 417
Cdd:TIGR00229 89 IWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
417-833 |
3.12e-17 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 86.45 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 417 IAAQANYDNLTGLPNRWLFGRCLARFCERGERFA----LMVLDLNNFKAVNNSMDHHVGDALLREVSDRLVSRVRT--ED 490
Cdd:PRK11059 224 IRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGahgvVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 491 LVARIGGDEFAFLVPGIvNRRQAEVFAKQVIGgfarpfMLANQHLYVTAT------LGITlCPNDGGDSDELLRNAEQAL 564
Cdd:PRK11059 304 LLARYSRSDFAVLLPHR-SLKEADSLASQLLK------AVDALPPPKMLDrddflhIGIC-AYRSGQSTEQVMEEAEMAL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 565 FVAKRQGrplGT----YNASMREE-----VSQRHQMQHDLAEaiklGQLTMAYQPIwDNRSGRVAKLEALVRWYHPHWGQ 635
Cdd:PRK11059 376 RSAQLQG---GNgwfvYDKAQLPEkgrgsVRWRTLLEQTLVR----GGPRLYQQPA-VTRDGKVHHRELFCRIRDGQGEL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 636 VSPADFIPLAEEAGLIQGLGALVLWQSCRDLARLQQSGFpdlqmSINRS--TLefqtIDPEANEWLR--VIRHFELDPAD 711
Cdd:PRK11059 448 LSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEENL-----SINLSvdSL----LSRAFQRWLRdtLLQCPRSQRKR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 712 IIIEITESLLMETSDQHRVRIDALREAGCKLAIDDFGTGYSALNYLRTFPVDLVKIDRSFVRHIPFNEQDRLLLDGIINI 791
Cdd:PRK11059 519 LIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGA 598
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 743523847 792 VHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPLPFD 833
Cdd:PRK11059 599 CAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
293-418 |
2.87e-16 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 81.43 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 293 AEQLKLSHRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSglHDQTFYADMYHAL-ERVGIWRGE 371
Cdd:COG3852 3 RESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALaEGQPVTERE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 743523847 372 VWNKRKNGKLYPQQLMISAVREGGKISQYIAIFSDLSQTKLAEQKIA 418
Cdd:COG3852 81 VTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELR 127
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
183-286 |
8.30e-16 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 73.82 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 183 APVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDwqtSIALYDALKRGER--PAFTQEKRYLHRDGTVL 260
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED---REELRERLENLLSggEPVTLEVRLRRKDGSVI 77
|
90 100
....*....|....*....|....*.
gi 743523847 261 WGRVTVTLIRNEQMHPDYLMVVLENI 286
Cdd:cd00130 78 WVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
707-829 |
8.83e-15 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 77.15 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 707 LDPADIIIEITESllMETSDQHRVRIDALREAGCKLAIDDF--GTGYSALnylrtFP-VDLVKIDrsfVRHIPFNEQDRl 783
Cdd:COG3434 81 LPPERVVLEILED--VEPDEELLEALKELKEKGYRIALDDFvlDPEWDPL-----LPlADIIKID---VLALDLEELAE- 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 743523847 784 lldgIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRP 829
Cdd:COG3434 150 ----LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
171-301 |
2.42e-14 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 75.65 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 171 EHHHFLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSiALYDALKRGeRPAFTQEK 250
Cdd:COG3852 4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRE-LLERALAEG-QPVTEREV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 743523847 251 RYLHRDGTVLWGRVTVTLIRNEQMHpDYLMVVLENIDPIRRHAEQLKLSHR 301
Cdd:COG3852 82 TLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEK 131
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
402-570 |
1.58e-13 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 73.50 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 402 AIFSDLSQTKLAEQKIAAQ----ANYDNLTGLPNRWLFGRCL--------ARFCErgerfALMVLDLNNFKAVNNSMDHH 469
Cdd:PRK09966 225 SLLDEMEEWQLRLQAKNAQllrtALHDPLTGLANRAAFRSGIntlmnnsdARKTS-----ALLFLDGDNFKYINDTWGHA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 470 VGDALLREVSDRLVSRVRTEDLVARIGGDEFAFLVPGIVNRRQAEVFAKQVIGGFARPFMLANQHLyVTATLGITLCPN- 548
Cdd:PRK09966 300 TGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQ-TTMTLSIGYAMTi 378
|
170 180
....*....|....*....|..
gi 743523847 549 DGGDSDELLRNAEQALFVAKRQ 570
Cdd:PRK09966 379 EHASAEKLQELADHNMYQAKHQ 400
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
309-420 |
1.96e-13 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 73.78 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 309 AILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVGIWRGEVWNKRKNGKLYPQQLMI 388
Cdd:TIGR02938 16 AISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTV 95
|
90 100 110
....*....|....*....|....*....|...
gi 743523847 389 SAV-REGGKISQYIAIFSDLSQTKLAEQKIAAQ 420
Cdd:TIGR02938 96 APVlNEAGETTHFLGMHRDITELHRLEQVVANQ 128
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
316-409 |
8.24e-13 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 64.79 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 316 DSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVgiWRGEVWNKRKNGKLYPQQLMISAVR-EG 394
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRdDG 78
|
90
....*....|....*
gi 743523847 395 GKISQYIAIFSDLSQ 409
Cdd:pfam13426 79 GELVGIIAILRDITE 93
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
175-286 |
2.53e-12 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 63.98 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 175 FLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGERPAFTQEKRYLH 254
Cdd:pfam00989 2 DLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 743523847 255 RDGTVLWGRVTVTLIRNEQMHPDYLMVVLENI 286
Cdd:pfam00989 82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
196-283 |
1.31e-10 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 58.50 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 196 ILWANPAIEKMLGYSQEELQQL--TVAEINHPDDW-QTSIALYDALKRGERpaFTQEKRYLHRDGTVLWGRVTVTLIRNE 272
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDReRVREALWEALKGGEP--YSGEYRIRRKDGEYRWVEARARPIRDE 78
|
90
....*....|.
gi 743523847 273 QMHPDYLMVVL 283
Cdd:pfam08447 79 NGKPVRVIGVA 89
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
174-227 |
1.41e-10 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 57.79 E-value: 1.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 743523847 174 HFLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDD 227
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPED 54
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
302-420 |
1.69e-10 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 64.02 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 302 VYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHdqtfyadMYHALERVGIWRGEVWNKRKNGKl 381
Cdd:COG3829 16 ILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSP-------LLEVLKTGKPVTGVIQKTGGKGK- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 743523847 382 ypqQLMISA--VREGGKISQYIAIFSDLSQTKLAEQKIAAQ 420
Cdd:COG3829 88 ---TVIVTAipIFEDGEVIGAVETFRDITELKRLERKLREE 125
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
608-835 |
2.75e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 61.56 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 608 YQPIWdNRSGRVAKLEALVRWYHPHWGQ--VSPADF---IPLAEEAGLIQ-GLGALVLWQscrdlARLQQSGfpdLQMSI 681
Cdd:PRK11596 34 FQPIY-RTSGRLMAIELLTAVTHPSNPSqrLSPERYfaeITVSHRLDVVKeQLDLLAQWA-----DFFVRHG---LLASV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 682 N--RSTLEFQTIDPEANE------WLRvirhFELdpadiiieiTESLLMETSDQhrvrIDALREAGcKLAIDDFGTG--- 750
Cdd:PRK11596 105 NidGPTLIALRQQPAILRlierlpWLR----FEL---------VEHIRLPKDSP----FASMCEFG-PLWLDDFGTGman 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 751 YSALNYLRtfpVDLVKIDRSFVRHIPFNEQDRLLLDGIINIVHNLGMQVVIEGVETREQLNFLCQKGCAFTQGYLLSRPL 830
Cdd:PRK11596 167 FSALSEVR---YDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
|
....*
gi 743523847 831 PFDDL 835
Cdd:PRK11596 244 PFETL 248
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
400-506 |
3.87e-10 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 62.54 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 400 YIAIFSDLSQ---TKLAEQK--IAAQANYDNLTGLPNR--W-LFGRCLARFCERGERFA-LMVLDLNNFKAVNNSMDHHV 470
Cdd:PRK10245 179 YPLLFAWVSYqtaTKLAEHKrrLQVMSTRDGMTGVYNRrhWeTLLRNEFDNCRRHHRDAtLLIIDIDHFKSINDTWGHDV 258
|
90 100 110
....*....|....*....|....*....|....*.
gi 743523847 471 GDALLREVSDRLVSRVRTEDLVARIGGDEFAFLVPG 506
Cdd:PRK10245 259 GDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSG 294
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
194-286 |
4.52e-10 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 57.09 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 194 GKILWANPAIEKMLGYSQEELQQLTVAEINHPDDwqTSIALYDALKRGeRPAFTQEKRYLHRDGTVLWGRVTVTLIRNEQ 273
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPE--DSERLREALREG-KAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
|
90
....*....|...
gi 743523847 274 MHPDYLMVVLENI 286
Cdd:pfam13426 79 GELVGIIAILRDI 91
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
286-420 |
1.28e-09 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 61.78 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 286 IDPIRRHAEQLKLSHRVYDNLSEAILVCDA---DSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHAL 362
Cdd:PRK13558 137 PISDLTVESDRRLKERALDEAPVGITIADAtlpDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAI 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 743523847 363 ERVGIWRGEVWNKRKNGKLYPQQLMISAVR-EGGKISQYIAIFSDLSQTKLAEQKIAAQ 420
Cdd:PRK13558 217 DEERPTSVELRNYRKDGSTFWNQVDIAPIRdEDGTVTHYVGFQTDVTERKEAELALQRE 275
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
306-407 |
1.39e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 56.10 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 306 LSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVGIWRGEVWNKRKNGKLYPQQ 385
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 743523847 386 LMISAVR-EGGKISQYIAIFSDL 407
Cdd:cd00130 81 VSLTPIRdEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
301-406 |
3.69e-09 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 55.12 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 301 RVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVGIWR-GEVWNKRKNG 379
Cdd:pfam00989 5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRgFEVSFRVPDG 84
|
90 100
....*....|....*....|....*...
gi 743523847 380 KLYPQQLMISAVR-EGGKISQYIAIFSD 406
Cdd:pfam00989 85 RPRHVEVRASPVRdAGGEILGFLGVLRD 112
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
151-294 |
1.48e-08 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 58.05 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 151 GRELALMYQQRQSQEQPAQpEHHHFLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDwqt 230
Cdd:COG5000 68 ARAFNRMTDQLKEQREELE-ERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELD--- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743523847 231 siaLYDALKRGERPAFTQEKRyLHRDGTVLWgRVTVTLIRNEQmhpdyLMVVLENIDPIRRHAE 294
Cdd:COG5000 144 ---LAELLREALERGWQEEIE-LTRDGRRTL-LVRASPLRDDG-----YVIVFDDITELLRAER 197
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
158-422 |
3.44e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 57.37 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 158 YQQRQSQEQPAQPEHHHFLDTMMSHAPVGIGKVDLGGK-------ILWANPAIEKMLGYSQEELQQLtVAEINHPDD--- 227
Cdd:PRK13560 52 YDARAIAEAEAQDCREQCERNLKANIPGGMFLFALDGDgtfsfpsLLDANGELAAIAKHDLMADKGL-LAMLIGGDDgdf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 228 -----WQTSIALYDALKrgERPAFTQEKRYLHRDGtvlwgRVTVTLIRNEQmHPD-------YLMVVLENIDPIRRHAEQ 295
Cdd:PRK13560 131 ffanpFRSAETIAMALQ--SDDWQEEEGHFRCGDG-----RFIDCCLRFER-HAHaddqvdgFAEDITERKRAEERIDEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 296 LKLSHRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLksglhDQTFYADMYHALERV-----GIWRG 370
Cdd:PRK13560 203 LHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDF-----APAQPADDYQEADAAkfdadGSQII 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 743523847 371 EVWNKRKNGKLYPQQLMISAVREGGK---ISQYIAIFSDLSQTKLAEQKIAAQAN 422
Cdd:PRK13560 278 EAEFQNKDGRTRPVDVIFNHAEFDDKenhCAGLVGAITDISGRRAAERELLEKED 332
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
181-286 |
6.79e-07 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 48.56 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 181 SHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDDWQTSIALYDALKRGERPAFTQEkrYLHRDGTVL 260
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLE--ELLLNGEER 79
|
90 100
....*....|....*....|....*.
gi 743523847 261 WGRVTVTLIRNEQMHPDYLMVVLENI 286
Cdd:pfam08448 80 HYELRLTPLRDPDGEVIGVLVISRDI 105
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
164-329 |
1.35e-06 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 51.70 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 164 QEQPAQPEHHHFLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHpddwqtSIALYDALKRGER 243
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP------NSPLLEVLKTGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 244 paftQEKRYLHRDGTVLWGRVTVTLIRNEQMhPDYLMVVLENIDPIRRHAEQLKLshrvyDNLSEAILVCDADSRIISVN 323
Cdd:COG3829 75 ----VTGVIQKTGGKGKTVIVTAIPIFEDGE-VIGAVETFRDITELKRLERKLRE-----EELERGLSAKYTFDDIIGKS 144
|
....*.
gi 743523847 324 PAFEKI 329
Cdd:COG3829 145 PAMKEL 150
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
300-340 |
1.90e-06 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 45.85 E-value: 1.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 743523847 300 HRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQ 340
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGK 44
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
482-568 |
2.21e-06 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 48.75 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 482 LVSRVrteDLVARIGGDEFAFLVPGIvNRRQAEVFAKQVIGGFARPfmlanQHLYVTATLGITlcpndggdSDELLRNAE 561
Cdd:COG3706 111 LLARV---DLVARYGGEEFAILLPGT-DLEGALAVAERIREAVAEL-----PSLRVTVSIGVA--------GDSLLKRAD 173
|
....*..
gi 743523847 562 qALFVAK 568
Cdd:COG3706 174 -ALYQAR 179
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
289-419 |
3.55e-06 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 50.35 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 289 IRRHAEQLKLSHR----VYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRpsmLKSGLHDQTFYADMYHALER 364
Cdd:COG5000 78 LKEQREELEERRRyletILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKP---LEELLPELDLAELLREALER 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 743523847 365 VgiWRGEVWNKRKNGKLYpqQLMISAVREGGkisqYIAIFSDLSQTkLAEQKIAA 419
Cdd:COG5000 155 G--WQEEIELTRDGRRTL--LVRASPLRDDG----YVIVFDDITEL-LRAERLAA 200
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
300-337 |
7.73e-06 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 44.08 E-value: 7.73e-06
10 20 30
....*....|....*....|....*....|....*...
gi 743523847 300 HRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEA 337
Cdd:pfam13188 4 RALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGE 41
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
277-417 |
1.78e-05 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 48.19 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 277 DYLMVVLENIDPIRRHAEQLKLS-------HRVYDNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQR-PSMLKSG 348
Cdd:COG5805 7 DFIHEVKKDGTPIWINNEVLRMAieiteelETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTiFDFLEKE 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 349 LHDQ-TFYADMYHALERVGIWRgEVWNkrKNGKLYPQQLMISAVREGGKISQYIAIFsDLSQTKLAEQKI 417
Cdd:COG5805 87 YHYRvKTRIERLQKGYDVVMIE-QIYC--KDGELIYVEVKLFPIYNQNGQAAILALR-DITKKKKIEEIL 152
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
304-411 |
1.95e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 44.33 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 304 DNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALE-RVGIWRGEVwnKRKNGKLY 382
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEgEEPIDFLEE--LLLNGEER 79
|
90 100 110
....*....|....*....|....*....|
gi 743523847 383 PQQLMISAVR-EGGKISQYIAIFSDLSQTK 411
Cdd:pfam08448 80 HYELRLTPLRdPDGEVIGVLVISRDITERR 109
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
319-403 |
2.08e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 43.87 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 319 IISVNPAFEKITGYSEEEACGQRPSMLKSgLH--DQT-FYADMYHALERVGIWRGEVWNKRKNGKLYPQQLMISAVR-EG 394
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLDL-VHpdDRErVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdEN 79
|
....*....
gi 743523847 395 GKISQYIAI 403
Cdd:pfam08447 80 GKPVRVIGV 88
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
247-286 |
5.90e-05 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 41.01 E-value: 5.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 743523847 247 TQEKRYLHRDGTVLWGRVTVTLIRNEQMHPDYLMVVLENI 286
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDI 40
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
175-227 |
2.50e-04 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 39.84 E-value: 2.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 743523847 175 FLDTMMSHAPVGIGKVDLGGKILWANPAIEKMLGYSQEELQQLTVAEINHPDD 227
Cdd:pfam13188 2 RLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLL 54
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
309-420 |
1.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 42.11 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 309 AILVCDA---DSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHALERVGIWRGEVWNKRKNGKLYPQQ 385
Cdd:PRK13559 55 AMCITDPhqpDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNA 134
|
90 100 110
....*....|....*....|....*....|....*.
gi 743523847 386 LMISAVR-EGGKISQYIAIFSDLSQTKLAEQKIAAQ 420
Cdd:PRK13559 135 LHLGPVYgEDGRLLYFFGSQWDVTDIRAVRALEAHE 170
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
316-415 |
3.16e-03 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 41.19 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523847 316 DSRIISVNPAFEKITGYSEEEACGQRPSMLKSGLHDQTFYADMYHAL-ERVGIwRGEVWNKRKNGKLYPQQLMISAV-RE 393
Cdd:PRK13557 52 DNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIaERREI-ATEILNYRKDGSSFWNALFVSPVyND 130
|
90 100
....*....|....*....|..
gi 743523847 394 GGKISQYIAIFSDLSQTKLAEQ 415
Cdd:PRK13557 131 AGDLVYFFGSQLDVSRRRDAED 152
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
304-340 |
3.91e-03 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 40.72 E-value: 3.91e-03
10 20 30
....*....|....*....|....*....|....*..
gi 743523847 304 DNLSEAILVCDADSRIISVNPAFEKITGYSEEEACGQ 340
Cdd:PRK11360 269 ESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGK 305
|
|
| |
