|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-1309 |
8.63e-152 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 492.64 E-value: 8.63e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 2 STVDKMLIKGIRSFDPENKNV--VTFFRPLTLIVGANGAGKTTIIECLKVSCTGELPPNARsGHSFIHDPKVAGETETKA 79
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKqiIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTK-GNTFVHDPKVAQETDVRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 80 QIKLRFKTAAGKDVVCIRSFQLTQKASKMEYKAIESVLqTINPHtGEKVCLSYRCADMDREIPALMGVSKAILENVIFVH 159
Cdd:TIGR00606 80 QIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVI-TRYKH-GEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 160 QDESNWPLQDPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEIKTFKLKLENLQTLKDAAYKLRESIAQDQERTESSK 239
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 240 VQMLELETSVQKVDAEVHNKEMMLKDLRKLQDQVSIKTAERSTLFKEQQRQYAALPEENEDTIEELKEWKSKFEERLALL 319
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 320 GTKIRKMEREMVDTETTISSLHNAKTNYMLEISKLQTEAEAHMLLKNERDSTIQNIFFHYNLGNVPSTPFSTEVVLN--- 396
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNfht 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 397 LTNRIKSRLGELEMDLLDKKKSNETALSTAWDcymDANDRWKSIEAQKRAKDEIkmgISKRIEE-KEIERDSFEFEISTV 475
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQAD---EIRDEKKGLGRTIELKKEI---LEKKQEElKFVIKELQQLEGSSD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 476 DVKQTDEREKQVQVELERKTKQnsergfeSKIEQKQHEIYSLEHKIKTLNRERDVMAGDAE--DRVKLSLKKTEQENLKK 553
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKN-------SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlNHHTTTRTQMEMLTKDK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 554 KHK-KIIDECKDRIRGVLKGRLPpEKDMKREIVQALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSLfkhNKDTES 632
Cdd:TIGR00606 545 MDKdEQIRKIKSRHSDELTSLLG-YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL---ESKEEQ 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 633 RKRYIESKLQALKQESVTIDaypklLESAKDKRDDRKREYNMANGMRQMFEPFEKRARQEHS--CPCCERSF-TADEEAS 709
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESD-----LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQscCPVCQRVFqTEAELQE 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 710 FIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLRAVFEEYSKLTTEIIPLAEKTLQEHTEELGQKSEALDDVLGISA 789
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 790 QIKADKDSIEALVQPLENADRIFQEIVSYQKQIEDLEYKLDFRGlGVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIY 869
Cdd:TIGR00606 776 TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD-LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 870 MERDISCLQARWHAVREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQ 949
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 950 EYEELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLR 1029
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1030 RNIEDNLNYRTTKAKVEELTREIESLEEQIlNIGGIAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQ 1109
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVEEELKQHLKEM-GQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1110 AQYKDIDKRHFDQLIQLKTTEMANKDLDRYYNALDKALMRFHTMKMEEINKIIRELWQQTYRGQDMDYIRIHSD-----S 1184
Cdd:TIGR00606 1094 PQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDadenvS 1173
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1185 EGAGTRSYSYKVLMQTGDTELEMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIME 1264
Cdd:TIGR00606 1174 ASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIK 1253
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*
gi 18402837 1265 DRKGQENFQLIVITHDERFAQMIGQRQHAEKYYRVAKDDMQHSII 1309
Cdd:TIGR00606 1254 SRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEI 1298
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1205-1308 |
2.19e-42 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 153.92 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1205 LEMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDgpnSESLAGALLRIMEDRKGQENFQLIVITHDERFa 1284
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQKNFQLIVITHDEEL- 185
|
90 100
....*....|....*....|....
gi 18402837 1285 qmigqRQHAEKYYRVAKDDMQHSI 1308
Cdd:cd03240 186 -----VDAADHIYRVEKDGRQKSR 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-170 |
1.27e-38 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 143.13 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 4 VDKMLIKGIRSFDpeNKNVVTFFRPLTLIVGANGAGKTTIIECLKVSCTGELPPNARSGHsfiHDPKVAGETETKAQIKL 83
Cdd:cd03240 1 IDKLSIRNIRSFH--ERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGA---HDPKLIREGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 84 RFKTAAGKDVVCIRSFqltqkaskmeykaiesvlqtinphtgekvclsyrcadmdreipalmgvskAILENVIFVHQDES 163
Cdd:cd03240 76 AFENANGKKYTITRSL--------------------------------------------------AILENVIFCHQGES 105
|
....*..
gi 18402837 164 NWPLQDP 170
Cdd:cd03240 106 NWPLLDM 112
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-220 |
3.78e-23 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 98.34 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 9 IKGIRSFDPENknvVTFFRPLTLIVGANGAGKTTIIECLKVSCTGELP--PNARSGHSFIHDPKVAGETETKAQIKLRFK 86
Cdd:pfam13476 3 IENFRSFRDQT---IDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlKRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 87 TAAGKDVVCI-RSFQLTQKASKMEYKAIESVLQTinphtgekvclsyrcADMDREIPALMGVSKAILENVIFVHQDEsnw 165
Cdd:pfam13476 80 NNDGRYTYAIeRSRELSKKKGKTKKKEILEILEI---------------DELQQFISELLKSDKIILPLLVFLGQER--- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18402837 166 plQDPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEiktfKLKLENLQTLKDA 220
Cdd:pfam13476 142 --EEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQL----KEKKKELEELKEE 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
436-1170 |
1.58e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 436 RWKSIEAQKRAKDEIKMGISKRIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELERKTKQNSERgfESKIEQKQHEIY 515
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL--EEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 516 SLEHKIKTLNRE----RDVMAGDAEDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGV------LKGRLPPEKDMKREIV 585
Cdd:TIGR02168 292 ALANEISRLEQQkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 586 QALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSL--FKHNKD------TESRKRYIESKLQALKQESVTIDAypKL 657
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerLEDRRErlqqeiEELLKKLEEAELKELQAELEELEE--EL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 658 LESAKDKRDDRKREYNMANGMRQMFEPFEKRARQEHS----CPCCERSFTADEEASFIKKQRVKASST------------ 721
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQlqarLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseli 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 722 --------------GEHLKALAVEssNADSVFQQLDKLravfEEYSKLTTEIIPLAEKTLQEHTEELGQKSEALDDVLGI 787
Cdd:TIGR02168 530 svdegyeaaieaalGGRLQAVVVE--NLNAAKKAIAFL----KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 788 SAQIKADKDSIEALVQP----------LENADRIFQE-------------------------------IVSYQKQIEDLE 826
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYllggvlvvddLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 827 YKLDFrgLGVKTmEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARwhaVREEKAKAANLLRDVTKAEEDLE 906
Cdd:TIGR02168 684 EKIEE--LEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD---LARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 907 RLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKI----NEYHDLK 982
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLesleRRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 983 KG-----ERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLRRNIEDNLN-----YRTTKAKVEELTREI 1052
Cdd:TIGR02168 838 RRledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelseeLRELESKRSELRREL 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1053 ESLEEQI----LNIGGIAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQAQYKDIDKRHFDQLIQLKT 1128
Cdd:TIGR02168 918 EELREKLaqleLRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 18402837 1129 TEMANKDLDRYYNALDKA---LMRfhtmKMEEINKIIRELWQQTY 1170
Cdd:TIGR02168 998 LKERYDFLTAQKEDLTEAketLEE----AIEEIDREARERFKDTF 1038
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1207-1301 |
5.60e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 62.38 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1207 MRGRCSAGQKVLASLIIRLALAEtfCLNCGILALDEPTTNLDGPNSESLAGALLRIMedrkgQENFQLIVITHDERFAQM 1286
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS--LKPRPLYILDEIDRGLDPRDGQALAEAILEHL-----VKGAQVIVITHLPELAEL 146
|
90
....*....|....*
gi 18402837 1287 igqrqhAEKYYRVAK 1301
Cdd:cd03227 147 ------ADKLIHIKK 155
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1211-1290 |
9.84e-10 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 59.96 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1211 CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRKGqenfqLIVITHDERFAQMIGQR 1290
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA-----VIVITHDYEFLAKVCDR 195
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1212-1290 |
1.16e-09 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 58.41 E-value: 1.16e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMedrkgQENFQLIVITHDERFAQMIGQR 1290
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-----EEGRTVIIVTHDPELAELAADR 149
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
553-1279 |
1.71e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 553 KKHKKIIDECKDrirgvlKGRLPPEKDMKREIVQALRSIEREYDDLSlksreaekevNMLQMKIQEVNNsLFKHNKDTES 632
Cdd:PRK01156 149 AQRKKILDEILE------INSLERNYDKLKDVIDMLRAEISNIDYLE----------EKLKSSNLELEN-IKKQIADDEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 633 RKRYIESKLQALKQEsvtidaypklLESAKDKRDDRKREYNMANGMRQMFEPFEKRARqehscpccersfTADEEASFIK 712
Cdd:PRK01156 212 SHSITLKEIERLSIE----------YNNAMDDYNNLKSALNELSSLEDMKNRYESEIK------------TAESDLSMEL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 713 KQRVKASSTGEHLKALAvessnADSVFQQLDKLRavfeEYSKLTTEIIplaekTLQEHTEELGQKSEALDDVLGISAQIK 792
Cdd:PRK01156 270 EKNNYYKELEERHMKII-----NDPVYKNRNYIN----DYFKYKNDIE-----NKKQILSNIDAEINKYHAIIKKLSVLQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 793 ADKDSIEALVQPLENADRIFQEI-------VSYQKQIEDLEYKLDFRGLGVKTM-EEIQSELSSLQSSKDKLHGELEKLR 864
Cdd:PRK01156 336 KDYNDYIKKKSRYDDLNNQILELegyemdyNSYLKSIESLKKKIEEYSKNIERMsAFISEILKIQEIDPDAIKKELNEIN 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 865 DDQIYMERDISCLQARWHAVRE---EKAKAANLL-------------------RDVTKAEEDLERLAEEKSQLDLDVKYL 922
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALREnldELSRNMEMLngqsvcpvcgttlgeeksnHIINHYNEKKSRLEEKIREIEIEVKDI 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 923 TEALGPL--------SKEKEQLLSDYNDMKIRRNQ------EYEELAEKKRNYQQEVEA-----LLKASYKINEYHDLKK 983
Cdd:PRK01156 496 DEKIVDLkkrkeyleSEEINKSINEYNKIESARADledikiKINELKDKHDKYEEIKNRykslkLEDLDSKRTSWLNALA 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 984 GERLDDIQEKQRLSD---SQLQSCEARKNELAGEL----NRNKDLMRNQDQLRRNIEDNLN-YRTTKAKVEELTREIESL 1055
Cdd:PRK01156 576 VISLIDIETNRSRSNeikKQLNDLESRLQEIEIGFpddkSYIDKSIREIENEANNLNNKYNeIQENKILIEKLRGKIDNY 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1056 EEQILNIGGIAAVEAEIVKILRERE----RLLSELNRCRGTVSVYESSISKNRVELKQAQYKDIDKRhfDQLIQLKTTEM 1131
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEdnlkKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN--ETLESMKKIKK 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1132 ANKDLDRYYNALDKALMRfhTMKMEEINKIIRELWQQTYRGQDMDYIRIHSDSEGAGTrsySYKVLMQTGDTELemrgrc 1211
Cdd:PRK01156 734 AIGDLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVDQDFNIT---VSRGGMVEGIDSL------ 802
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18402837 1212 SAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRKGQEnfQLIVITH 1279
Cdd:PRK01156 803 SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIP--QVIMISH 868
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
188-922 |
3.63e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 188 KALEVIKKLHKDQA----QEIKTFKLKLENLQTLKDAAYKLRESIAQDQERTESskvqmlELETSVQKVDAEVHNKEMML 263
Cdd:pfam15921 92 RRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 264 KDLRKLQDQVSIKTAERSTLFKEQQrqyAALPEENEDTIEELKEWKSKFEERLALLGTKIRKMEREMvDTETTISSLHNA 343
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEGVLQEIR---SILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILREL-DTEISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 344 KTNYMLEISKLQTEAEAHMLLKNERDSTIQNIFFHynlgNVPSTPFSTEV--VLNLTNRIKSrlgelEMDLLDKKKSNET 421
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLLQQHQDRIEQLISEH----EVEITGLTEKAssARSQANSIQS-----QLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 422 ALstawdcYMDANDRWKSIEAQKRAK-DEIKMGISKRIEEKE--------------IERDSFEFEISTVD------VKQT 480
Cdd:pfam15921 313 SM------YMRQLSDLESTVSQLRSElREAKRMYEDKIEELEkqlvlanseltearTERDQFSQESGNLDdqlqklLADL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 481 DEREKQVQVELER-KTKQNSERGFESKIEQKQHEIYSLEHKIKTLNRERDVMAGDAEDRVKLSLKKTEQENlkkkhkkii 559
Cdd:pfam15921 387 HKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN--------- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 560 dECKDRIRGvLKGRLPPEKDMKREIVQ-------ALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSL------FKH 626
Cdd:pfam15921 458 -ESLEKVSS-LTAQLESTKEMLRKVVEeltakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklqeLQH 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 627 NKDTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKRDDRKREYNMANGMRQMFEPFEKRARQEHSCPCCERSFTADE 706
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDK 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 707 EASFIKK----------QRVKASSTG-EHLKALAVESSNADSVFQQL----DKLRAVFEEYSKL-------------TTE 758
Cdd:pfam15921 616 KDAKIRElearvsdlelEKVKLVNAGsERLRAVKDIKQERDQLLNEVktsrNELNSLSEDYEVLkrnfrnkseemetTTN 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 759 IIPLAEKTLQEHTEEL--------GQKSEALDDVLGISAQIKADKDSIEAL---VQPLENAdrifqeIVSYQKQIEDLEy 827
Cdd:pfam15921 696 KLKMQLKSAQSELEQTrntlksmeGSDGHAMKVAMGMQKQITAKRGQIDALqskIQFLEEA------MTNANKEKHFLK- 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 828 kldfrglgvKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEKAKAANLLRdvtKAEEDLER 907
Cdd:pfam15921 769 ---------EEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ---RQEQESVR 836
|
810
....*....|....*
gi 18402837 908 LaeeKSQLDLDVKYL 922
Cdd:pfam15921 837 L---KLQHTLDVKEL 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
271-1057 |
8.34e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 271 DQVSIKTAERSTLFKEQQRQYAALPEENEDTIEELKEWKSKFEERLALLGTKIRKMEREMVDTETTISSLHNAKTNYMLE 350
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 351 ISKLQTEAEAHMLLKNERDSTIQniffhynlgnvpstpfstEVVLNLTNRIKSRLGELEMDLldkkKSNETALSTAWDCY 430
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIK------------------DLGEEEQLRVKEKIGELEAEI----ASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 431 MDANDRWKSIEAQKRAKDEIKMGISKRIEEKEIERDSFEFEIStvdvKQTDEREKQVQvELERKTKQNSERGFESKieQK 510
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA----ELKEELEDLRA-ELEEVDKEFAETRDELK--DY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 511 QHEIYSLEHKIKTLNRERDVMAGDAED-RVKLSLKKTEQENLKKKHKKIIDECKDRIRGVLK--GRLPPEKDMKREIVQA 587
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRlSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqeWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 588 LRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSLFKHNKDTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKR-- 665
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRln 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 666 -------DDRKREYNMA---NGMRQMFEPFEKRARQEHSCPCCERSFTADEEASFIKKQRVKASSTGEHLKALAVeSSNA 735
Cdd:TIGR02169 551 nvvveddAVAKEAIELLkrrKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLV-VEDI 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 736 DSVFQQLDKLRAV------FEEYSKLT-----TEIIPLAEKTLQEHTEELGQKSEALDDVLgisAQIKADKDSIEALV-Q 803
Cdd:TIGR02169 630 EAARRLMGKYRMVtlegelFEKSGAMTggsraPRGGILFSRSEPAELQRLRERLEGLKREL---SSLQSELRRIENRLdE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 804 PLENADRIFQEIVSYQKQIEDLEYKLD-FRGLGVKTMEEIQSELSSLQSSKDklhgELEKLRDDQIYMERDISCLQARWH 882
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEkLKERLEELEEDLSSLEQEIENVKS----ELKELEARIEELEEDLHKLEEALN 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 883 AV--REEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRN---QEYEELAEK 957
Cdd:TIGR02169 783 DLeaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsieKEIENLNGK 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 958 KRNYQQEVEallKASYKINEYhdlkkGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLRRNIEDNL- 1036
Cdd:TIGR02169 863 KEELEEELE---ELEAALRDL-----ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELs 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 18402837 1037 -----------------NYRTTKAKVEELTREIESLEE 1057
Cdd:TIGR02169 935 eiedpkgedeeipeeelSLEDVQAELQRVEEEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
436-1113 |
8.56e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 436 RWKSIEAQKRAkdeikmgISKRIEEKEIERDSFEFEIStvDVKQTDEREKQVQVELERKTKQNSE---RGFESKIEQKQH 512
Cdd:TIGR02169 231 EKEALERQKEA-------IERQLASLEEELEKLTEEIS--ELEKRLEEIEQLLEELNKKIKDLGEeeqLRVKEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 513 EIYSLEHKIKTLNRE-RDVMAGDAEDRVKLSLKKTEQENLKKKhkkIIDECKDRIRgvLKGRLPPEKDMKREIVQALRSI 591
Cdd:TIGR02169 302 EIASLERSIAEKERElEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDK--LTEEYAELKEELEDLRAELEEV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 592 EREYDDLSLKSREAEKEVNMLQMKIQEVNNSLFKhnkdTESRKRYIESKLQALKQE-SVTIDAYPKLLESAKDKRDDRKR 670
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDR----LQEELQRLSEELADLNAAiAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 671 EYNMANGMRQMFEPFEKRARQ-EHSCPCCERSFTADEEASFIKKQRVKASSTGEHLKALAVE--SSNADSVFQQLDKLRA 747
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlKASIQGVHGTVAQLGS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 748 VFEEYSKLTTEIIPLAEKTLQEHTEELGQKS-EALDDVLGISA------QIKADKDSIEALVQP--------LENADRIF 812
Cdd:TIGR02169 533 VGERYATAIEVAAGNRLNNVVVEDDAVAKEAiELLKRRKAGRAtflplnKMRDERRDLSILSEDgvigfavdLVEFDPKY 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 813 QEIVSYQKQ----IEDLEYKLDFRG-LGVKTME-EI----------QSELSSLQSSKDKLHGELEKLRDDQIYMERDISC 876
Cdd:TIGR02169 613 EPAFKYVFGdtlvVEDIEAARRLMGkYRMVTLEgELfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 877 LQARWHAVREEKAKAANLLRDVTK----AEEDLERLAEEKSQLDLDVKYLTEALgplsKEKEQLLSDYNDMKIRRNQEYE 952
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDL----SSLEQEIENVKSELKELEARIE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 953 ELAEKKRNYQQEVEALlKASYKineyhdlkkGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRN-------KDLMRNQ 1025
Cdd:TIGR02169 769 ELEEDLHKLEEALNDL-EARLS---------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQEL 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1026 DQLRRNIEDNLNYRttKAKVEELTREIESLEEQILNI-GGIAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNR 1104
Cdd:TIGR02169 839 QEQRIDLKEQIKSI--EKEIENLNGKKEELEEELEELeAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
....*....
gi 18402837 1105 VELKQAQYK 1113
Cdd:TIGR02169 917 KRLSELKAK 925
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-120 |
5.72e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.63 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 9 IKGIRSFdpENKNVVTFFRPLTLIVGANGAGKTTIIECLKVSCTGELPPNARSGHSFIHDPkvagetETKAQIKLRFkTA 88
Cdd:COG0419 7 LENFRSY--RDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVG------SEEASVELEF-EH 77
|
90 100 110
....*....|....*....|....*....|..
gi 18402837 89 AGKDVVCIRSFQLTQKASKMEYKAIESVLQTI 120
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEAKPSERKEALKRL 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
12-673 |
8.96e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 12 IRSFDPENKNVVTFFRPLTLIVGANGAGKTTIIECLKVSCTGELPPNARSGHsfIHDPKVAGETETKAQIKLRFKtaaGK 91
Cdd:PRK03918 8 IKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLK--KDDFTRIGGSGTEIELKFEKN---GR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 92 DVVCIRSFqlTQKASKMEYKAIESVLqtinpHTGEKVCLSYrcadMDREIPAlmgvskAILENVIFVHQDESNWPLQDPS 171
Cdd:PRK03918 83 KYRIVRSF--NRGESYLKYLDGSEVL-----EEGDSSVREW----VERLIPY------HVFLNAIYIRQGEIDAILESDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 172 TLKKKFDDIFSATRYTKALEVIKKLhkdqaqeIKTFKLKLENLQTLKDAAYKLRESIAQDQERTESSKVQMLELETSVQK 251
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEV-------IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 252 VDAEVHNKEMMLKDLRKLQDQVSIKTAERSTLFKEQQRQYAALpEENEDTIEELKEWKSKFEERLALL------GTKIRK 325
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELkelkekAEEYIK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 326 MEREMVDTETTISSLHNAKTNYMLEISKLQ---TEAEAHMLLKNERDSTIQNIFFHYNLGNVPSTPFST-EVVLNLTNRI 401
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 402 KSRLGELEMDLLDKK------------KSNETALSTAWDCYMDANDRWKSIEAQKRAKDE---IKMGISKRIEEKEIERD 466
Cdd:PRK03918 378 KKRLTGLTPEKLEKEleelekakeeieEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKELLEEY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 467 SFEFEISTVDVKQTDEREKQVQVELERKTKQNSERGFESKIEQKQHEIYSLEHKIKTLNRErdvmagdaedrvKLSLKKT 546
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE------------ELEKKAE 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 547 EQENLKKKHKKIidecKDRIRGVLK--GRLPPEKDMKREIVQALRSIEREYDDLSLKSRE-AEKEVNMLQMKIQEVNNSL 623
Cdd:PRK03918 526 EYEKLKEKLIKL----KGEIKSLKKelEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFY 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 18402837 624 FKHN--KDTESRKRYIESKLQALKQESVTIDAY----PKLLESAKDKRDDRKREYN 673
Cdd:PRK03918 602 NEYLelKDAEKELEREEKELKKLEEELDKAFEElaetEKRLEELRKELEELEKKYS 657
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1212-1283 |
1.35e-07 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 52.07 E-value: 1.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALlrimedrkgqENFQ--LIVITHDERF 1283
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYF 129
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1202-1280 |
4.92e-07 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 53.99 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1202 DTELEMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRkgqenfQLIVITHD 1280
Cdd:COG4988 464 DTPLGEGGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR------TVILITHR 531
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
438-1053 |
5.82e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 438 KSIEAQKRAKDEIKMGISKRIEE-KEIE--RDSFEFEISTVDVKQTDER--EKQVQVELERKTKQNSERGFESKIE--QK 510
Cdd:PTZ00121 1152 KRVEIARKAEDARKAEEARKAEDaKKAEaaRKAEEVRKAEELRKAEDARkaEAARKAEEERKAEEARKAEDAKKAEavKK 1231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 511 QHEIYSLEHKIKTLNRERDVMAGDAEDRVKLSLKKTEQENLKKKHKKIIDECKdRIRGVLKGRLPPEKDMKREIVQALRS 590
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKK 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 591 IE--REYDDLSLKSREAEKEVNMLQMKIQEVNnslfkhnKDTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKRDDR 668
Cdd:PTZ00121 1311 AEeaKKADEAKKKAEEAKKKADAAKKKAEEAK-------KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 669 KR---EYNMANGMRQMFEPFEKRARQehscpcCERSFTADEEASFIKKqRVKASSTGEHLKALAVESSNADSVFQQLDKL 745
Cdd:PTZ00121 1384 KKkaeEKKKADEAKKKAEEDKKKADE------LKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 746 RAVFEEYSKLTteiiplaEKTLQEHTEELGQKSEALDDVLGISAQIKADKDSIEALVQPLENADRIFQeiVSYQKQIEDL 825
Cdd:PTZ00121 1457 KKAEEAKKKAE-------EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEA 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 826 EYKLDFRGLG-VKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEKAKaanlLRDVTKAEED 904
Cdd:PTZ00121 1528 KKAEEAKKADeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEE 1603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 905 LERLAEEKSQLDLDVKYLTEALgplsKEKEQLLSDYNDMKIRRNQEYEELAEKKRnyQQEVEALLKASYKINEYHDLKKG 984
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKA 1677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 985 ERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLRRNIEDNlnyrttKAKVEELTREIE 1053
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN------KIKAEEAKKEAE 1740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
193-1059 |
7.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 193 IKKLHKDQAQEIKTFKLKLEnlQTLKDAAYK-LRESIAQDQERTESSKVQMLELETSVQKVDAEVHNKEMMLKDLRKlqd 271
Cdd:TIGR02169 205 REREKAERYQALLKEKREYE--GYELLKEKEaLERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 272 QVSIKTAERSTLFKEQQRQYAALPEENEDTIEELKEWKSKFEERLALLGTKIRKMEREMVDTETTISSLHNAKTNYMLEI 351
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 352 SKLQTEAEAhmllknerdstiqniffhynlgnvpstpfstevvlnltnrIKSRLGELEMD---LLDKKKSNETALStawd 428
Cdd:TIGR02169 360 AELKEELED----------------------------------------LRAELEEVDKEfaeTRDELKDYREKLE---- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 429 cymDANDRWKSIEAQKRAKDEIKMGISKRIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELERKTKQNSERGFESKIE 508
Cdd:TIGR02169 396 ---KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 509 QKQHEIYSLEHKIKTLNRERdvmagdaeDRVKLSLKKTEQEnlKKKHKKIIDECKDRIRGVLK-----GRLPPEKDMKRE 583
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQREL--------AEAEAQARASEER--VRGGRAVEEVLKASIQGVHGtvaqlGSVGERYATAIE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 584 IV--QALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNnslfkhnkdtesRKRYIESKLQALKQESVT------IDAYP 655
Cdd:TIGR02169 543 VAagNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLN------------KMRDERRDLSILSEDGVIgfavdlVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 656 KLLESAKDKRDDRKREYNMANGMRQMF---------EPFEKrarqehSCPCCERSFTADEEASFIKKQRVKASSTGEHLK 726
Cdd:TIGR02169 611 KYEPAFKYVFGDTLVVEDIEAARRLMGkyrmvtlegELFEK------SGAMTGGSRAPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 727 ALAVESSNA----DSVFQQLDKLRAVFEEYSKLTTEIIPLAEKTLQEHTEELGQKSEALDDVLGISAQIKADKDSIEALV 802
Cdd:TIGR02169 685 GLKRELSSLqselRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 803 QPLENADRifqEIVSYQKQIEDLEYKLDFRGLG--VKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQAR 880
Cdd:TIGR02169 765 ARIEELEE---DLHKLEEALNDLEARLSHSRIPeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 881 whaVREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRN 960
Cdd:TIGR02169 842 ---RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 961 YQQEVEALLKASYKINEYHDLKKGER--------LDDIQEkqrlsdsQLQSCEARKNELaGELNrnkdlMRNQDQLRRNI 1032
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEeipeeelsLEDVQA-------ELQRVEEEIRAL-EPVN-----MLAIQEYEEVL 985
|
890 900
....*....|....*....|....*..
gi 18402837 1033 EDNLNYrttKAKVEELTREIESLEEQI 1059
Cdd:TIGR02169 986 KRLDEL---KEKRAKLEEERKAILERI 1009
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-85 |
8.47e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 8.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 20 KNVVTFFRP-LTLIVGANGAGKTTIIECLKVSCTGElppnarsgHSFIHDPKVAGETETKAQIKLRF 85
Cdd:cd03227 13 PNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGA--------QSATRRRSGVKAGCIVAAVSAEL 71
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
436-1078 |
1.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 436 RWKSIEAQKRAKDEikmgiskRIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELERKTKQNSERGFESKIEQKQHEIY 515
Cdd:COG1196 233 KLRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 516 SLEHKIKTLNRERDVMAGD-AEDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGVLKgrlppEKDMKREIVQALRSIERE 594
Cdd:COG1196 306 RLEERRRELEERLEELEEElAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-----AEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 595 YDDLSLKSREAEKEVNMLQMKIQEVNNSLFKHNKDTESRKRYIESKLQALKQESVTIDAypkLLESAKDKRDDRKREYNM 674
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---EEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 675 ANGMRQMFEPFEKRARQEHSCPCCERSFTADEEASFIKKQRVKASSTGEHLKALAVE-SSNADSVFQQLDKLRAVFEEYS 753
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALlLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 754 klTTEIIPLAEKTLQEHTEELGQKSEA----LDDVLGISAQIKADKDSIEALVQPLENADRIFQEIVSYQkqiEDLEYKL 829
Cdd:COG1196 538 --AALEAALAAALQNIVVEDDEVAAAAieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA---SDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 830 DFRGLGVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDiscLQARWHAVREEKAKAANLLRDVTKAEEDLERLA 909
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG---SAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 910 EEKSQLDLDVKyltealgpLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDD 989
Cdd:COG1196 690 EEELELEEALL--------AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 990 IQEKQRlsdsQLQSCEARKNELaGELNrnkdlMRNQDQLRRnIEDNLNYRTtkAKVEELTREIESLEEqilnigGIAAVE 1069
Cdd:COG1196 762 LEELER----ELERLEREIEAL-GPVN-----LLAIEEYEE-LEERYDFLS--EQREDLEEARETLEE------AIEEID 822
|
....*....
gi 18402837 1070 AEIVKILRE 1078
Cdd:COG1196 823 RETRERFLE 831
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
871-1314 |
2.47e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 871 ERDISCLQARWHAVREEKAKAANLLRDVTKAEEDLERLaEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDMKiRRNQE 950
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDASSDDLA-ALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 951 YEELAEKKRNYQQEVEALLKASYKINEyhdlkkgeRLDDIQEKQRLSDSQLQSCEARK----NELAGELNRNKDLMRNQD 1026
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEK--------ELEQAEEELDELQDRLEAAEDLArlelRALLEERFAAALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1027 QLRRNIEDNLnyRTTKAKVEELTREIESLEEQILN------IGGIAAVEA--EIVKILRE---------RERLLSELNRC 1089
Cdd:COG4913 766 ELRENLEERI--DALRARLNRAEEELERAMRAFNRewpaetADLDADLESlpEYLALLDRleedglpeyEERFKELLNEN 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1090 RGT-----VSVYESSIS--KNRVE-----LKQAQYKDidkrhfDQLIQLKTTEMANKDLDRYYNALDKALM--------- 1148
Cdd:COG4913 844 SIEfvadlLSKLRRAIReiKERIDplndsLKRIPFGP------GRYLRLEARPRPDPEVREFRQELRAVTSgaslfdeel 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1149 ---RFHTMKmEEINKIIR--ELWQQTYRGQDMDY-------IRIHSDSEGagTRSYSYKVlmqtgdteleMRGRcSAGQK 1216
Cdd:COG4913 918 seaRFAALK-RLIERLRSeeEESDRRWRARVLDVrnhlefdAEEIDREDG--EEVETYSS----------SGGK-SGGEK 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1217 -------VLASLIIRLALAE----TFCLncgiLALDEPTTNLDgpnsESLAGALLRIMEdrkgQENFQLIVITHDERfAQ 1285
Cdd:COG4913 984 qklayfiLAAALAYQLGLEGrgrpSFRT----VVLDEAFSKMD----EEFARRALRLFK----ELGLQLLIATPLDK-IQ 1050
|
490 500
....*....|....*....|....*....
gi 18402837 1286 MIgqRQHAEKYYRVAKDDMQHSIIEAQEI 1314
Cdd:COG4913 1051 AI--EPYVGSVLVVHKDDGRRSRVRELTI 1077
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
440-955 |
3.00e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 440 IEAQKRAKDEIKMGISKRIEEKEIERDSFEFEISTV--DVKQTDE-REKQVQVELERKTKQNSERGFESKIEQKQHEIYS 516
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLekEVKELEElKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 517 LEHKIKTLnrerdvmagdaEDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGV--LKGRLPPEKDMKREIVQALRSIERE 594
Cdd:PRK03918 271 LKKEIEEL-----------EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIekRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 595 YDDLSLKSREAEKEVNMLQMKIQEVNNSLFKHNKDTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKRDDRKREynM 674
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--L 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 675 ANGMRQMFEPFEKRARQEHSCPCCERSFTADEEASFIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLRAVFEEYSK 754
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 755 LTT---EIIPLAEKTLQEHTEELGQKSEALDDV----LGISAQIKADKDSIEAL-------------------------- 801
Cdd:PRK03918 498 LKElaeQLKELEEKLKKYNLEELEKKAEEYEKLkeklIKLKGEIKSLKKELEKLeelkkklaelekkldeleeelaellk 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 802 ----------------VQPLENADRIFQEIVSYQKQIEDLEYKLD-FRGLGVKTMEEIQSELSSLQSSKDKLHgELEKLR 864
Cdd:PRK03918 578 eleelgfesveeleerLKELEPFYNEYLELKDAEKELEREEKELKkLEEELDKAFEELAETEKRLEELRKELE-ELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 865 DDQIY--MERDISCLQARWHAVREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYND 942
Cdd:PRK03918 657 SEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
570
....*....|...
gi 18402837 943 MKIRRNQEYEELA 955
Cdd:PRK03918 737 LKERALSKVGEIA 749
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
743-1088 |
3.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 743 DKLRAVFEEYSKLTTEIIPLAE---------KTLQEHTEELGQKSEALDDVLGISAQIKADKDSIEALVQPLENADRIFQ 813
Cdd:PRK03918 200 KELEEVLREINEISSELPELREeleklekevKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 814 EIVsyqKQIEDLEYKldfrglgVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEKAKAAN 893
Cdd:PRK03918 280 EKV---KELKELKEK-------AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 894 LLRDVTKAEEDLERLAEEKSQLD-----------LDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNyq 962
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA-- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 963 qeVEALLKASYK-------INEYHDL----KKGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLR-- 1029
Cdd:PRK03918 428 --IEELKKAKGKcpvcgreLTEEHRKelleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEql 505
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18402837 1030 RNIEDNLN-------------YRTTKAKVEELTREIESLEEQILNIGGIAAVEAEIVKILRERERLLSELNR 1088
Cdd:PRK03918 506 KELEEKLKkynleelekkaeeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1212-1290 |
4.52e-06 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 49.00 E-value: 4.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSEslagALLRIMEDRKgQENFQLIVITHDERFAQMIGQR 1290
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRR----ELLELLKKLK-AEGKTIIIVTHDLDLLLELADR 203
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
855-1086 |
6.13e-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: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 855 KLHGELEKLRDDQIYMERDIscLQARWHAVREE----KAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLS 930
Cdd:COG1196 217 ELKEELKELEAELLLLKLRE--LEAELEELEAEleelEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 931 KEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDDIQEKQRLSDSQLQSCEARKNE 1010
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18402837 1011 LAGELNRNKDLMRNQDQLRRNIEDNLNYRTTKAKVEELTREIESLEEQilniggIAAVEAEIVKILRERERLLSEL 1086
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE------LEELEEALAELEEEEEEEEEAL 444
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1195-1281 |
6.99e-06 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 50.36 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1195 KVLMQTGDTELEMRGR-CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRkgqenfQ 1273
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAgLSGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR------T 509
|
....*...
gi 18402837 1274 LIVITHDE 1281
Cdd:TIGR02857 510 VLLVTHRL 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
217-671 |
7.63e-06 |
|
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: 50.49 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 217 LKDAAYKLRESIAQDQERTESSKVQMLELETSVQKVDAEvhnkemmLKDLRKLQDQVSIKTAERSTLFKEQQRqyaaLPE 296
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSE-------LEEMTKFKNNKEVELEELKKILAEDEK----LLD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 297 ENEDTIEELKEWKSKFEERLALLGTKirkmEREMVDTETTISSLHNAKTNYMLEISKLQTEAEAHMLLKNERDSTIQNIF 376
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQELIFLLQAR----EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 377 fhynLGNVPSTPFSTEVVLNLTNRiksrlgelEMDLLDKKKSNETALstawdcymdandrwKSIEAQKRAKDEIKMGISK 456
Cdd:pfam05483 499 ----LENKELTQEASDMTLELKKH--------QEDIINCKKQEERML--------------KQIENLEEKEMNLRDELES 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 457 RIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELERKTKQNSERGFESKIEQKQHEIYSLEHKIKTLNRErdvmaGDAE 536
Cdd:pfam05483 553 VREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-----GSAE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 537 DR------VKLSLKKTEQENLKKKHKKIIDECKDRI--RGVLKGRLPPEKDMKREIVQALRSIEREYdDLSLKSREAEKE 608
Cdd:pfam05483 628 NKqlnayeIKVNKLELELASAKQKFEEIIDNYQKEIedKKISEEKLLEEVEKAKAIADEAVKLQKEI-DKRCQHKIAEMV 706
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18402837 609 VNMLQMK------IQEVNNSL-FKHNKDTE--SRKRYIESKLQALKQESVTIDaypKLLESAKDKRDDRKRE 671
Cdd:pfam05483 707 ALMEKHKhqydkiIEERDSELgLYKNKEQEqsSAKAALEIELSNIKAELLSLK---KQLEIEKEEKEKLKME 775
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1190-1259 |
8.29e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 45.30 E-value: 8.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1190 RSYSYKVLMQTGDTEL--EMRGRCSAGQK-VLASLIIRLALAETFCLN------CGILALDEPTTNLDGPNSESLAGAL 1259
Cdd:pfam13558 10 LSFEVEVRDEDGSEVEtyRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1212-1290 |
1.38e-05 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 47.18 E-value: 1.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDgpnsESLAGALLRIMEDRKGQENFQLIVITHDERFAQMIGQR 1290
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALD----PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADR 170
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
454-1295 |
2.21e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 454 ISKRIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELERKTKQNSERGFESKieQKQHEIYSLEHKIKTLNRERDVMAG 533
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL--HSQEIHIRDAHEVATSIREISCQQH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 534 DAEDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGVLKGRLPPEKDMKREIVQALRSIEREYDDLSLKSREAEKEVNMLQ 613
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 614 MKIQEVNNSLFKhnkdTESRKRYIESKLQALKQESVTIDAYPK-LLESAKDKRDDRKREYNMANGMRQMFEPfekrarQE 692
Cdd:TIGR00618 456 LEKIHLQESAQS----LKEREQQLQTKEQIHLQETRKKAVVLArLLELQEEPCPLCGSCIHPNPARQDIDNP------GP 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 693 HSCPCCERSFTADEEASFIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLRAVFEEYSKLTTEIIPLAEKTLQEHTE 772
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 773 ELGQKSEALDDVLgISAQIKADKdsiealvqplenadrifQEIVSYQKQIEDLEYKLdfrglgvktmeeiqselsslqss 852
Cdd:TIGR00618 606 AEDMLACEQHALL-RKLQPEQDL-----------------QDVRLHLQQCSQELALK----------------------- 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 853 KDKLHGELEKL-RDDQIYMERDISCLQARWHAVREEKAKAA-NLLRDVTKAEEDLErlaeeksQLDLDVKYLTEALGPLS 930
Cdd:TIGR00618 645 LTALHALQLTLtQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLA-------QCQTLLRELETHIEEYD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 931 KEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKIneyHDLKKGERLDDIQEKQRLSdsQLQSCEARKNE 1010
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA---HFNNNEEVTAALQTGAELS--HLAAEIQFFNR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1011 LAGElnRNKDLMRNQDQLRRNIEDNLNYRTtkAKVEELTREIESLEEQIlniggiaaveAEIVKILRERERLLSELNRCR 1090
Cdd:TIGR00618 793 LREE--DTHLLKTLEAEIGQEIPSDEDILN--LQCETLVQEEEQFLSRL----------EEKSATLGEITHQLLKYEECS 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1091 GTVSVYESSISKNRVELKQAQYKDIDKRHF--DQLIQLKTTEMANKDLDRYynalDKALMRFHTMKMEEInkiirelwQQ 1168
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLSDKLNGINQIKIQFdgDALIKFLHEITLYANVRLA----NQSEGRFHGRYADSH--------VN 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1169 TYRGQDMDYIRIhsDSEGAGTRSYSykvlmqtgdtelemrgRCSAGQKVLASLIIRLALAETFCLNCGI----LALDEPT 1244
Cdd:TIGR00618 927 ARKYQGLALLVA--DAYTGSVRPSA----------------TLSGGETFLASLSLALALADLLSTSGGTvldsLFIDEGF 988
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 18402837 1245 TNLDGPNSESLAGALLRIMEDRKgqenfQLIVITHDERFAQMIGQRQHAEK 1295
Cdd:TIGR00618 989 GSLDEDSLDRAIGILDAIREGSK-----MIGIISHVPEFRERIPHRILVKK 1034
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
886-1187 |
2.35e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 886 EEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLsdyndmkirrnqEYEELAEKKRNYQQev 965
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE------------RYQALLKEKREYEG-- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 966 eALLKASYKINEyHDLKKGER-LDDIQEKQRLSDSQLQSCEARKNELAGELNrnkdlmrnqdQLRRNIED--NLNYRTTK 1042
Cdd:TIGR02169 226 -YELLKEKEALE-RQKEAIERqLASLEEELEKLTEEISELEKRLEEIEQLLE----------ELNKKIKDlgEEEQLRVK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1043 AKVEELTREIESLEEQilniggIAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQAQYKDIDKRHFDQ 1122
Cdd:TIGR02169 294 EKIGELEAEIASLERS------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 1123 LIQLKTTEMAnKDLDRYYNALDKALMRFHTMKmEEINKIIREL--WQQTYRGQDMDYIRIHSDSEGA 1187
Cdd:TIGR02169 368 DLRAELEEVD-KEFAETRDELKDYREKLEKLK-REINELKRELdrLQEELQRLSEELADLNAAIAGI 432
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1212-1279 |
2.48e-05 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 46.22 E-value: 2.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRkgqenfQLIVITH 1279
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK------TVIVIAH 153
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
565-1079 |
2.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 565 RIRGVLKGRLPPEKDMKREIVQALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSLFKHNKDTESRKRYIEskLQAL 644
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 645 KQEsvtIDAYPKLLESAKDKRDDRKreynmaNGMRQMfepfeKRARQEHscpccersftADEEASFIKKQRVKASSTGEH 724
Cdd:COG4717 138 EAE---LAELPERLEELEERLEELR------ELEEEL-----EELEAEL----------AELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 725 LKALAVESSNADSVFQQLDK-LRAVFEEYSKLTTEIIPLAEKTLQEHTEELGQKSEALDDVLGISAQIKADKDSIEALVQ 803
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEeLEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 804 PLENADRIFQEIVSYqkqiedleykldfrGLGVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIymerdiscLQARWHA 883
Cdd:COG4717 274 TIAGVLFLVLGLLAL--------------LFLLLAREKASLGKEAEELQALPALEELEEEELEEL--------LAALGLP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 884 VREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVkyltealgpLSKEKEQLLSDYN-------DMKIRRNQEYEELAE 956
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEE---------LEQEIAALLAEAGvedeeelRAALEQAEEYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 957 KKRNYQQEVEALLKASYKINEYHDLKK-GERLDDIQEKQRLSDSQLQSCEARKNELAGELnrnkdlmrnqdqlrRNIEDN 1035
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAELEAEL--------------EQLEED 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 18402837 1036 LNYRTTKAKVEELTREIESLEEQILNIGGIAAVEAEIVKILRER 1079
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
877-1168 |
2.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 877 LQARWHAVREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALG--PLSKEKEQLLSDYNDMKIRRN---QEY 951
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEeleERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 952 EELAEKKRNYQQEVEALLKASYKINEYHDLKKG----------ERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDL 1021
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLateeelqdlaEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1022 MRNQDQLRRnIEDNLNYRTTKAKVEELTREIESLEEQILNIGGIAAVEAEIVKILrereRLLSELNRCRGTVSVYESSIS 1101
Cdd:COG4717 236 LEAAALEER-LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL----FLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18402837 1102 KNRVELKQAQYKDI-DKRHFDQLIQLKTTEMANKDLDRYYNALDKALMRFHTMKMEEINKIIRELWQQ 1168
Cdd:COG4717 311 PALEELEEEELEELlAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
742-1281 |
2.59e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 742 LDKLRAVFEEYSKLTTEIiplaeKTLQEHTEELGQKSEALDdvlgisaQIKADKDSIEALVQPLENADRIFQEIVSYQKQ 821
Cdd:PRK03918 306 LDELREIEKRLSRLEEEI-----NGIEERIKELEEKEERLE-------ELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 822 IEDLEYKLdfrglGVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEKAKAANLLRDVTKA 901
Cdd:PRK03918 374 LERLKKRL-----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 902 EED--LERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNdmKIRRNQEYEELAEKKRNYQQEVEA--LLKASYKINE 977
Cdd:PRK03918 449 HRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK--KESELIKLKELAEQLKELEEKLKKynLEELEKKAEE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 978 YHDLKkgERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLRRNIEdNLNYRTtkakVEELTREIESLEE 1057
Cdd:PRK03918 527 YEKLK--EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE-ELGFES----VEELEERLKELEP 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1058 QILNIGGIAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQAQYKDIDKRH------------------ 1119
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeelreeylelsrelaglr 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1120 --FDQLIQLKTTEMAN-KDLDRYYNALDKALMRFHTM-----KMEEINKIIRELWQQTYRGQDMDYIRIHSDS-EGAGTR 1190
Cdd:PRK03918 680 aeLEELEKRREEIKKTlEKLKEELEEREKAKKELEKLekaleRVEELREKVKKYKALLKERALSKVGEIASEIfEELTEG 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1191 SYS------------YKVLMQTGDTELemrGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDgpnsESLAGA 1258
Cdd:PRK03918 760 KYSgvrvkaeenkvkLFVVYQGKERPL---TFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLD----EERRRK 832
|
570 580
....*....|....*....|...
gi 18402837 1259 LLRIMEdRKGQENFQLIVITHDE 1281
Cdd:PRK03918 833 LVDIME-RYLRKIPQVIIVSHDE 854
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1209-1284 |
4.45e-05 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 45.93 E-value: 4.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 1209 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDgpnSESLAgALLRIMEDRKGQEnfQLIVI-THDERFA 1284
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALD---AAGVA-LLAELIAAHLARG--GAVLLtTHQPLEL 194
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
441-1127 |
4.71e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 441 EAQKRAKDEIKMGISKRIEEKEIERDSFEfEISTVDVKQTDEREKQVQ-----VELERKTKQNSERGFESKIEQKQHEIY 515
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQLQntvheLEAAKCLKEDMLEDSNTQIEQLRKMML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 516 SLE---HKIKTLNRERDVMAGDaedrvklslKKTEQENLKKKH--------KKIIDECKDRIrGVLKGRLPPEKD----M 580
Cdd:pfam15921 181 SHEgvlQEIRSILVDFEEASGK---------KIYEHDSMSTMHfrslgsaiSKILRELDTEI-SYLKGRIFPVEDqleaL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 581 KRE---------------IVQALRSIEREYDDLSLKSREAEKEVNMLQMK---IQEV---NNSLF-KHNKDTESR----- 633
Cdd:pfam15921 251 KSEsqnkielllqqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQleiIQEQarnQNSMYmRQLSDLESTvsqlr 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 634 ------KRYIESKLQALKQESVTIDAYpklLESAKDKRDDRKREY-NMANGMRQMFEPFEKRARQ-----EHSCPCCER- 700
Cdd:pfam15921 331 selreaKRMYEDKIEELEKQLVLANSE---LTEARTERDQFSQESgNLDDQLQKLLADLHKREKElslekEQNKRLWDRd 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 701 ---SFTADEEASFIKKQRVKASSTGEHLKAL-------------AVESSN-----ADSVFQQLDK----LRAVFEEYS-- 753
Cdd:pfam15921 408 tgnSITIDHLRRELDDRNMEVQRLEALLKAMksecqgqmerqmaAIQGKNeslekVSSLTAQLEStkemLRKVVEELTak 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 754 KLTTEIiplAEKTLQEHTEELGQKSEALDdvlGISAQIKADKDSIEALVQPLENADRIFQEIVSYQKQIEDLEYKLDFRG 833
Cdd:pfam15921 488 KMTLES---SERTVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 834 LGVKTMEEIQSELSSLQSSKDKLHGELEKlrdDQIYMERDISCLQARWHAVREEKAKAANLLRDVTKAEEDLERlaeEKS 913
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQV---EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL---EKV 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 914 QLDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKINEYHDLKKGErlddiQEK 993
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE-----LEQ 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 994 QRLSDSQLQSCEARKNELAGELNRNKDLMRNQ-DQLRRNIEdNLNYRTTKAKVEE--LTREIESLEEQILNIGGIAAVEA 1070
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQiDALQSKIQ-FLEEAMTNANKEKhfLKEEKNKLSQELSTVATEKNKMA 789
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 1071 EIVKILRERERLLSElnrcrgtvSVYESSISKNRVELKQAQYKDIDKRHFDQLIQLK 1127
Cdd:pfam15921 790 GELEVLRSQERRLKE--------KVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1224-1285 |
4.84e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 46.27 E-value: 4.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18402837 1224 RLALAETFCLNCGILALDEPTTNLDGPNSESLAGaLLRIMEDRKGQenfQLIVITHDERFAQ 1285
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIID-LLFELNRERGT---TLVLVTHDPALAA 211
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
678-725 |
5.03e-05 |
|
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. The Rad50 coiled-coil region contains a dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn ion. This alignment includes the zinc hook motif and a short stretch of coiled-coil on either side.
Pssm-ID: 427940 [Multi-domain] Cd Length: 52 Bit Score: 42.18 E-value: 5.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18402837 678 MRQMFEPFEKRARQ----EHSCPCCERSFTADEEASFIKKQRVKASSTGEHL 725
Cdd:pfam04423 1 LHQETLELNKKIEElkeaEGCCPLCGRPLDEEHRSELIKELQSKLERLPEEL 52
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-381 |
9.74e-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: 46.97 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 185 RYTKALEVIKKLHKDQAQEIKTFKLKLENLQTLKDAAY----KLRESIAQDQERTESSKVQMLELETSVQKVDAEVHNKE 260
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 261 MMLKDLRK-----------LQDQVSIKTAERSTLfKEQQRQYAALPEENEDTIEELKEWKSKFEERLALLGTKIRKMERE 329
Cdd:TIGR02168 824 ERLESLERriaaterrledLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18402837 330 MVDTETTISSLHNAKTNYMLEISKLQTEAEAhmlLKNERDSTIQNIFFHYNL 381
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQERLSEEYSL 951
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
794-1310 |
9.78e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 46.65 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 794 DKDSIEALVQPLENADRIF---QEIVSYQKQIEDLEYKLDfrglgvKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYM 870
Cdd:COG4694 77 NRDFVEENLRSGEEIKGIFtlgEENIELEEEIEELEKEIE------DLKKELDKLEKELKEAKKALEKLLEDLAKSIKDD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 871 ERDISCLQARwhavreeKAKAANLLRDVTK-AEEDLERLAEEKSQL------DLDVKYLTEALGPLSKEKEQLLSdyndm 943
Cdd:COG4694 151 LKKLFASSGR-------NYRKANLEKKLSAlKSSSEDELKEKLKLLkeeepePIAPITPLPDLKALLSEAETLLE----- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 944 KIRRNQEYEELAEKKRNYQQE--VEALLKasykineYHDLKKG------------ERLDDIQEKqrLSDSQLQSCEARKn 1009
Cdd:COG4694 219 KSAVSSAIEELAALIQNPGNSdwVEQGLA-------YHKEEEDdtcpfcqqelaaERIEALEAY--FDDEYEKLLAALK- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1010 ELAGELNRNKDLMRNQDQLRRNIEDNLNYRTTKAKVEELTREIESLEEQILN--------------------IGGIAAVE 1069
Cdd:COG4694 289 DLLEELESAINALSALLLEILRTLLPSAKEDLKAALEALNALLETLLAALEEkianpstsidlddqelldelNDLIAALN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1070 AEIVKILRERERLLSELNRCRGTVSVYEssisKNRVELKQAQYKDIDKRHFDQLIQLKTTEMANKDLDRYYNALDKALMR 1149
Cdd:COG4694 369 ALIEEHNAKIANLKAEKEEARKKLEAHE----LAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSS 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1150 FHTMKmEEINKIIRELwqqtyrgqDMDYIRIHSDSEGagtrSYSYKVLMQTGDTElEMRGRCSAGQKVLASLIIRLAL-- 1227
Cdd:COG4694 445 VDEAA-DEINEELKAL--------GFDEFSLEAVEDG----RSSYRLKRNGENDA-KPAKTLSEGEKTAIALAYFLAEle 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1228 AETFCLNCGILALDEPTTNLDGPNSESLAGaLLRimedRKGQENFQLIVITHDERFAQMI------GQRQHAEKYYRVAK 1301
Cdd:COG4694 511 GDENDLKKKIVVIDDPVSSLDSNHRFAVAS-LLK----ELSKKAKQVIVLTHNLYFLKELrdladeDNKKKNCAFYEIRK 585
|
....*....
gi 18402837 1302 DDmQHSIIE 1310
Cdd:COG4694 586 DN-RGSKII 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
740-1291 |
1.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 740 QQLDKLRAVFEEYSKLTTEIIPLAEK--TLQEHTEELGQKSEALDDVLGIS---AQIKADKDSIEALVQPLENADRIFQE 814
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQLLplyQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 815 IVSYQKQIEDLEYKLDfrglgvKTMEEIQSELSSLQSSKdklHGELEKLRDDQIYMERDISCLQARWHAVREEKAKAAN- 893
Cdd:COG4717 158 LRELEEELEELEAELA------ELQEELEELLEQLSLAT---EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEe 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 894 --LLRDVTKAEEDLERLAEEKSQL------------DLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRN-------QEYE 952
Cdd:COG4717 229 leQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKaslgkeaEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 953 ELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDDIQEKQRL--------SDSQLQSCEARKNELAGELNrnkdlMRN 1024
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlreaeeleEELQLEELEQEIAALLAEAG-----VED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1025 QDQLRRNIEDNLNYRTTKAKVEELTREIESL---EEQILNIGGIAAVEAEIVKILRERERLLSELNRCRgtvsvyeSSIS 1101
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEELR-------EELA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1102 KNRVELKQA----QYKDIDKRHFDQLIQLKTTEMANKDLDRYYNALDKALMRFHTMKMEEINKIIRELWQQTYRGQdmdY 1177
Cdd:COG4717 457 ELEAELEQLeedgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASEYFSRLTDGR---Y 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1178 IRIHSDSegagtrSYSYKVLMQTGDT----ELemrgrcSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDgpnsE 1253
Cdd:COG4717 534 RLIRIDE------DLSLKVDTEDGRTrpveEL------SRGTREQLYLALRLALAELLAGEPLPLILDDAFVNFD----D 597
|
570 580 590
....*....|....*....|....*....|....*...
gi 18402837 1254 SLAGALLRIMEDRkgQENFQLIVITHDERFAQMIGQRQ 1291
Cdd:COG4717 598 ERLRAALELLAEL--AKGRQVIYFTCHEELVELFQEEG 633
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1202-1280 |
1.18e-04 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 46.28 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1202 DTELEMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRiMEDRKGqenfQLIVITHD 1280
Cdd:COG4618 458 DTRIGEGGARlSGGQRQ------RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARGA----TVVVITHR 526
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
9-48 |
1.50e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.69 E-value: 1.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18402837 9 IKGIRSFdpenKNVVTFFRPLTLIVGANGAGKTTIIECLK 48
Cdd:COG4637 7 IKNFKSL----RDLELPLGPLTVLIGANGSGKSNLLDALR 42
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
877-1088 |
1.61e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 877 LQARWHAVREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDM--KIRRNQ-EYEE 953
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaELAELEkEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 954 LAEKKRNYQQEVEALLKASYKINEYHDLK---KGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLRR 1030
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1031 NIEDNLNyrTTKAKVEELTREIESLEEQILNIGG-IAAVEAEIVKILRERERLLSELNR 1088
Cdd:COG4942 175 ELEALLA--ELEEERAALEALKAERQKLLARLEKeLAELAAELAELQQEAEELEALIAR 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
455-993 |
1.87e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 455 SKRIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELERKTKQNSE----RGFESKIEQKQHEIYSLEHKIKTL------ 524
Cdd:PRK01156 212 SHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEiktaESDLSMELEKNNYYKELEERHMKIindpvy 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 525 -NRERDV----MAGDAEDRVK-LSLKKTEQENLKKKHKKIIDECKDRIRGVLKGR----LPPEKDMKREIVQALRSIERE 594
Cdd:PRK01156 292 kNRNYINdyfkYKNDIENKKQiLSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSryddLNNQILELEGYEMDYNSYLKS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 595 YDDLSLKSREAEKEVNMLQMKIQEVNNSLFKHNKDTESRKRYIESKLQALKQESVTIDAYpklLESAKDKRDDRKREYNM 674
Cdd:PRK01156 372 IESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQR---IRALRENLDELSRNMEM 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 675 ANGmrqmfepfekrarqEHSCPCCERSFTADEEASFIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLravfEEYsk 754
Cdd:PRK01156 449 LNG--------------QSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR----KEY-- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 755 ltteiipLAEKTLQEHTEELGQKSEAlddvlgiSAQIKADKDSIEALVQPLENADRIFQEIVSYQKQIEDLEYKLDFRGL 834
Cdd:PRK01156 509 -------LESEEINKSINEYNKIESA-------RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 835 GVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEkakaANLLRDVTKAEEDLERLAEEKSQ 914
Cdd:PRK01156 575 AVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE----ANNLNNKYNEIQENKILIEKLRG 650
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 915 LDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNyqqevEALLKASYKINEYHDLKKGERLDDIQEK 993
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAN-----RARLESTIEILRTRINELSDRINDINET 724
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-621 |
1.96e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 260 EMMLKDLRKLQDQVSIKTAERSTLFKEQQRQYAALPEENEDT------IEELKEWKSKFEERLALLGTKIRKMEREMVDT 333
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 334 ETTISSLHNAKTNYMLEISKLQTEAEAhmLLKNERDSTIQNIFFHYNlgnvpstPFSTEVVlnltnRIKSRLGELEMDLl 413
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELS-------KLEEEVS-----RIEARLREIEQKL- 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 414 dKKKSNETALstawdcymdANDRWKSIEAQKRAKDEIKMGISKRIEEKEIERDSFEFEISTVDVKQTDEREKQVQVELER 493
Cdd:TIGR02169 822 -NRLTLEKEY---------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 494 KTKQNSERGFESKIEQKQHEIYSLEHKIKTLNRERDVMAGDA---EDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGVl 570
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL- 970
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 18402837 571 kgrlppeKDMKREIVQALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNN 621
Cdd:TIGR02169 971 -------EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1202-1279 |
2.32e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 45.54 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1202 DTELEMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDgPNSESL-AGALLRIMEDRkgqenfQLIVITH 1279
Cdd:COG1132 467 DTVVGERGvNLSGGQRQ------RIAIARALLKDPPILILDEATSALD-TETEALiQEALERLMKGR------TTIVIAH 533
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-810 |
2.57e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 457 RIEEKEIERDSFEFEISTVDV-KQTDEREKQVQvELERKTKQNSERgfeskIEQKQHEIYSLEHKIKTLNRERDVMAGDA 535
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDAsRKIGEIEKEIE-QLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 536 EDrvklslKKTEQENLKKKHKKIIDECKDRIRGVLKGRLPPEKDMKREIVQALRSIEREYDDLSLKSREAEKEVNMLQMK 615
Cdd:TIGR02169 768 EE------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 616 IQEVNNSLFKHNKDTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKRDDRKREynmangMRQMfepfeKRARQehsc 695
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ------LREL-----ERKIE---- 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 696 pccERSFTADEEASFIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLRAVFEEYSKLTTEIIPLAE---KTLQEHTE 772
Cdd:TIGR02169 907 ---ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvnmLAIQEYEE 983
|
330 340 350
....*....|....*....|....*....|....*...
gi 18402837 773 ELgqksEALDDVLGISAQIKADKDSIEALVQPLENADR 810
Cdd:TIGR02169 984 VL----KRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1224-1290 |
2.59e-04 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 44.03 E-value: 2.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 1224 RLALAETFCLNCGILALDEPTTNLDgpnsESLAGALLRIMEDRKGQENFQLIVITHDERFAQMIGQR 1290
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALD----VSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADR 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
888-1093 |
2.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 888 KAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTEalgplSKEKEQLLSDYNDMKIRRNQEYEELAEKkrnyQQEVEA 967
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE-----RREALQRLAEYSWDEIDVASAEREIAEL----EAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 968 LLKASYKINEyhdLKkgERLDDIQEKQRLSDSQLQSCEARKNELAGELnrnKDLMRNQDQLRRNIEDnlnyrttkAKVEE 1047
Cdd:COG4913 680 LDASSDDLAA---LE--EQLEELEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEA--------AEDLA 743
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18402837 1048 LTREIESLEEQILNIGGiAAVEAEIVKIL-RERERLLSELNRCRGTV 1093
Cdd:COG4913 744 RLELRALLEERFAAALG-DAVERELRENLeERIDALRARLNRAEEEL 789
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-56 |
4.37e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.83 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 18402837 4 VDKMLIKGIRSFdpenKNV-VTF--FRPLTLIVGANGAGKTTIIECLKVSCTGELP 56
Cdd:COG3950 3 IKSLTIENFRGF----EDLeIDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLS 54
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
530-970 |
4.93e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 530 VMAGDAEDRVKLSlkkteqenlKKKHKKIIDEckdrIRGVlkgrlppeKDMKREIVQALRSIEreyddlslksrEAEKEV 609
Cdd:TIGR02169 139 VLQGDVTDFISMS---------PVERRKIIDE----IAGV--------AEFDRKKEKALEELE-----------EVEENI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 610 NMLQMKIQEVNNSLFKHNKDTESRKRYiesklQALKQESVTIDAYPKLLESAKDKRDDRKREYNMAnGMRQMFEPFEKRa 689
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERY-----QALLKEKREYEGYELLKEKEALERQKEAIERQLA-SLEEELEKLTEE- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 690 RQEHSCPCCERSFTADEEASFIKK---------QRVKASSTGEHLKALAVESSNADSVFQQLDKLRAVFEEYSKLTTEII 760
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDlgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 761 PLAEKTlqehtEELGQKSEALddvlgiSAQIKADKDSIEALVQPLEN----ADRIFQEIVSYQKQIEDLEYKldfrglgv 836
Cdd:TIGR02169 340 ELEREI-----EEERKRRDKL------TEEYAELKEELEDLRAELEEvdkeFAETRDELKDYREKLEKLKRE-------- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 837 ktMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEkakaanllrdVTKAEEDLERLAEEksqld 916
Cdd:TIGR02169 401 --INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE----------IKKQEWKLEQLAAD----- 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 18402837 917 ldvkyltealgpLSKEKEQLLsdyndmkiRRNQEYEELAEKKRNYQQEVEALLK 970
Cdd:TIGR02169 464 ------------LSKYEQELY--------DLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-639 |
5.85e-04 |
|
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: 44.28 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 225 RESIAQDQERTESSKVQMLELETSVQKVDAEVHNKEMMLKDLRKLQDQVSIKTAERSTLFK---EQQRQYAALPEENEDT 301
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 302 IEELKEWKSKFEERLALLGTKIRKMEREMVDTETTISSLHNAKTNYMLEISKLQTEAEAHmllknerdstiqNIFFHynl 381
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL------------NEEAA--- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 382 gnvpstpfstevvlnltnRIKSRLGELEMDLLDKKKSNETalstawdcymdandrwksIEAQKRAKDEIKMGISKRIEEK 461
Cdd:TIGR02168 821 ------------------NLRERLESLERRIAATERRLED------------------LEEQIEELSEDIESLAAEIEEL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 462 EIERdsfefeistvdvkqtDEREKQVQVELERKTKQNSERG-FESKIEQKQHEIYSLEHKIKTLNRERDvmagdaEDRVK 540
Cdd:TIGR02168 865 EELI---------------EELESELEALLNERASLEEALAlLRSELEELSEELRELESKRSELRRELE------ELREK 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 541 LSLKKTEQENLKKKhkkiIDECKDRIRGvlKGRLPPEkdmkreivqalrSIEREYDDLSLKSREAEKEVNMLQMKIQE-- 618
Cdd:TIGR02168 924 LAQLELRLEGLEVR----IDNLQERLSE--EYSLTLE------------EAEALENKIEDDEEEARRRLKRLENKIKElg 985
|
410 420
....*....|....*....|..
gi 18402837 619 -VNNSLFKHNKDTESRKRYIES 639
Cdd:TIGR02168 986 pVNLAAIEEYEELKERYDFLTA 1007
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1237-1286 |
6.19e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 42.72 E-value: 6.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 18402837 1237 ILAlDEPTTNLDGPNSEslagALLRIMEDRKGQENFQLIVITHDERFAQM 1286
Cdd:COG1136 166 ILA-DEPTGNLDSKTGE----EVLELLRELNRELGTTIVMVTHDPELAAR 210
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-678 |
6.72e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 198 KDQAQE-IKTFKLKLENLQTLKDAAYKLRESIAQDQ-------ERTESSKVQMLELETSVQKVDAEVHNKEMMLKDLRKL 269
Cdd:PRK02224 236 RDEADEvLEEHEERREELETLEAEIEDLRETIAETErereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 270 QDQVSIKTAE-RSTLfkEQQRQYAalpEENEDTIEELKEWKSKFEERLALLGTKIRKMEREMVDTETTISSLHNaktnym 348
Cdd:PRK02224 316 REELEDRDEElRDRL--EECRVAA---QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE------ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 349 lEISKLQTEAEAhmLLKNERDSTIQniffhynLGNVPStpFSTEVVLNLtNRIKSRLGELEMDLLDKKKSNETA--LSTA 426
Cdd:PRK02224 385 -EIEELEEEIEE--LRERFGDAPVD-------LGNAED--FLEELREER-DELREREAELEATLRTARERVEEAeaLLEA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 427 WDCYMDANDRWKSIEAQKRAKDEikmgisKRIEEKEIERDSFEFEISTVDvKQTDEREKQVQVELERKTKQNSERGFESK 506
Cdd:PRK02224 452 GKCPECGQPVEGSPHVETIEEDR------ERVEELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 507 IEQKQHEIYSLEHKIKTLNRERDVMAGDAEDRVKLSLKKTEQenlkkkhkkiIDECKDRIrGVLKGRLppekdmkREIVQ 586
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----------AEEAREEV-AELNSKL-------AELKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 587 ALRSIEREYDDLSLKSrEAEKEVNMLQMK---IQEVNNSLFKHNKDTESRKRYIESK-----LQALKQESVTIDAYPKLL 658
Cdd:PRK02224 587 RIESLERIRTLLAAIA-DAEDEIERLREKreaLAELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQV 665
|
490 500
....*....|....*....|
gi 18402837 659 ESAKDKRDDRKREYNMANGM 678
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGA 685
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
765-1097 |
7.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 765 KTLQEHTEELgQKSEALDDVLGISAQIKADKDSIEALVQPLENADRifqEIVSYQKQIEDLEYKLDfrgLGVKTMEEIQS 844
Cdd:COG1196 216 RELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELE---ELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 845 ELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWhavREEKAKAANLLRDVTKAEEDLERLAEEKSQLDLDVKYLTE 924
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 925 ALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDDIQEKQRLSDSQLQSC 1004
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1005 EARKNELAGELNRNKDLMRNQDQLRRNIEDNLNYRTTKAKVEELTREIESLEEQILNIGGIAAVEAEiVKILRERERLLS 1084
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA-ALLLAGLRGLAG 524
|
330
....*....|...
gi 18402837 1085 ELNRCRGTVSVYE 1097
Cdd:COG1196 525 AVAVLIGVEAAYE 537
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1224-1290 |
7.51e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 7.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 1224 RLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRKGqenfQLIVITHDERFAQMIGQR 1290
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGT----TLILVTHDLQLAARCDRR 216
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
503-887 |
7.92e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 503 FESKIEQKQHEIYSLEHKIKTLnrerDVMagdaEDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGVLkgRLPPEKDMKR 582
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERL----DLI----IDEKRQQLERLRREREKAERYQALLKEKREYEGYE--LLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 583 EIVQALR---SIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSLfkhNKDTESRKRYIESKLQALKQEsvtidaypklLE 659
Cdd:TIGR02169 238 QKEAIERqlaSLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAE----------IA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 660 SAKDKRDDRKREY-NMANGMRQMFEPFEKRARQehscpccersftADEEASFIKKQRVKASSTGEHLKALAVESSNADSV 738
Cdd:TIGR02169 305 SLERSIAEKERELeDAEERLAKLEAEIDKLLAE------------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 739 FQQLDK-LRAVFEEYSKLTTEIIPLAEKtLQEHTEELGQKSEALDDVLGISAQIKADKDSIEALVQPLEnadrifQEIVS 817
Cdd:TIGR02169 373 LEEVDKeFAETRDELKDYREKLEKLKRE-INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE------EEKED 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 818 YQKQIEDLEYKLdfrglgvktmEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREE 887
Cdd:TIGR02169 446 KALEIKKQEWKL----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
9-128 |
1.01e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 9 IKGIRSFDPENknvVTFFRPLTLIVGANGAGKTTIIECLKVSCTGELPPNARsghsfIHD-PKVAGETETKAQIKLRFKT 87
Cdd:COG3593 8 IKNFRSIKDLS---IELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFD-----EEDfYLGDDPDLPEIEIELTFGS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18402837 88 AAGKdvvcirsfQLTQKASKMEYKAIESVLQTINPHTGEKV 128
Cdd:COG3593 80 LLSR--------LLRLLLKEEDKEELEEALEELNEELKEAL 112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
582-1097 |
1.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 582 REIVQALRSIEREYDDLSLKSREAEKEVNMLQMKIQEvnnslfkHNKDTESRKRYIESKLQALKQESVTIDAYPKLLESA 661
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRD-------LRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 662 KDKRDDRKREYNMANGMRQMFEPFEKRARqehscpccERSFTADEEAsfiKKQRVKASSTGEHLKALAVESSNADSvfqQ 741
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLR--------EDADDLEERA---EELREEAAELESELEEAREAVEDRRE---E 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 742 LDKLRAVFEEYSKlTTEIIPLAEKTLQEHTEELgqkSEALDDVLGISAQIKADKDSIEALV----------------QPL 805
Cdd:PRK02224 386 IEELEEEIEELRE-RFGDAPVDLGNAEDFLEEL---REERDELREREAELEATLRTARERVeeaealleagkcpecgQPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 806 ENADRIfQEIVSYQKQIEDLEYKLDfrglGVKTMEEIQSELSSLQSSKDKLHGELEKLRDDQiymeRDISCLQARWHAVR 885
Cdd:PRK02224 462 EGSPHV-ETIEEDRERVEELEAELE----DLEEEVEEVEERLERAEDLVEAEDRIERLEERR----EDLEELIAERRETI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 886 EEKAKAANLLRdvtKAEEDLERLAEEK----SQLDLDVKYLTEALGPLSKEKEQllsdyNDMKIRRNQEYEELAEKKRNY 961
Cdd:PRK02224 533 EEKRERAEELR---ERAAELEAEAEEKreaaAEAEEEAEEAREEVAELNSKLAE-----LKERIESLERIRTLLAAIADA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 962 QQEVEALlkasykineyhdlkkGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRNkdlmrNQDQLRrniEDNLNYRTT 1041
Cdd:PRK02224 605 EDEIERL---------------REKREALAELNDERRERLAEKRERKRELEAEFDEA-----RIEEAR---EDKERAEEY 661
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 18402837 1042 KAKVEELTREIESLEEQILNigGIAAVEAEIVKILRERERLLSELNRCRGTVSVYE 1097
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQA--EIGAVENELEELEELRERREALENRVEALEALYD 715
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1237-1286 |
1.14e-03 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 42.09 E-value: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 18402837 1237 ILAlDEPTTNLDGPNSEslagALLRIMEDRKGQENFQLIVITHDERFAQM 1286
Cdd:cd03255 162 ILA-DEPTGNLDSETGK----EVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1212-1279 |
1.16e-03 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 41.43 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRiMEDRKGqenfQLIVITH 1279
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGA----TRIVIAH 154
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
471-681 |
1.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 471 EISTVDVKQtDEREKQV------QVELERKTKQNSERgFESKIEQKQHEIYSLEHKIKTLNRERDVMAGDAEDRVKlSLK 544
Cdd:PHA02562 182 QIQTLDMKI-DHIQQQIktynknIEEQRKKNGENIAR-KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSA-ALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 545 KTEQENLKKKHKkiIDECKDRIRGVLKG--------RLPPEKDMKREIVQALRSIEREYDDLSLKSREAEK---EVNMLQ 613
Cdd:PHA02562 259 KLNTAAAKIKSK--IEQFQKVIKMYEKGgvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQS 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18402837 614 MKIQEVNNSLFKHNKD---TESRKRYIESKLQALKQESVTIDAYPKLLESAKDKRDDRKREYNMANGMRQM 681
Cdd:PHA02562 337 KKLLELKNKISTNKQSlitLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
874-1058 |
1.49e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 874 ISCLQARWHAVREEKAK---AANLLRDVTKAEEDLERLAEEKSQLdldvkylteaLGPLSKEKEQLLS-DYNDMKIRRNQ 949
Cdd:NF012221 1537 TSESSQQADAVSKHAKQddaAQNALADKERAEADRQRLEQEKQQQ----------LAAISGSQSQLEStDQNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 950 EYEELAEKKRNYQQEVEALLKASYKINEY--HDLKKGER---------LDDIQEK----QRLSDSQL----QSCEARKNE 1010
Cdd:NF012221 1607 QRDAILEESRAVTKELTTLAQGLDALDSQatYAGESGDQwrnpfagglLDRVQEQlddaKKISGKQLadakQRHVDNQQK 1686
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18402837 1011 LAGELNRNKDLMRNQDQLRRNIEDNLNYRTTKAKveelTREIESLEEQ 1058
Cdd:NF012221 1687 VKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAE----KRKDDALAKQ 1730
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
870-1157 |
1.58e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 870 MERDISCLQARWHAVREE----KAKAANLLRDVTKAEEDleRLAEEKSQLDLDVKYLTEALGPLSKEKEQLLS------- 938
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQlealKSESQNKIELLLQQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSqleiiqe 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 939 ---DYNDMKIRRNQEYE--------ELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDDIQEKQRLsDSQLQSCEA- 1006
Cdd:pfam15921 307 qarNQNSMYMRQLSDLEstvsqlrsELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL-DDQLQKLLAd 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1007 ---RKNELAGELNRNKDL----MRNQ---DQLRRNIED-NLNYRTTKAKVEELTREIE-SLEEQILNIGG-------IAA 1067
Cdd:pfam15921 386 lhkREKELSLEKEQNKRLwdrdTGNSitiDHLRRELDDrNMEVQRLEALLKAMKSECQgQMERQMAAIQGkneslekVSS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1068 VEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQAQykdidkrhfdqliqlKTTEMANKDLDRYYNALDKAL 1147
Cdd:pfam15921 466 LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE---------------RAIEATNAEITKLRSRVDLKL 530
|
330
....*....|
gi 18402837 1148 MRFHTMKMEE 1157
Cdd:pfam15921 531 QELQHLKNEG 540
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1224-1290 |
1.68e-03 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 41.72 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 1224 RLALAETFCLNCGILALDEPTTNLDgPNSeslAGALLRIMEDRKGQENFQLIVITHDERFAQMIGQR 1290
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLD-PIA---SGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADR 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
796-1062 |
1.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 796 DSIEALVQPLENADRIFQEIVSYQKQIEDLEykldfrglgvkTMEEIQSELSSLQSSKDKLHGELEKLRDDQIymERDIS 875
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLE-----------PIRELAERYAAARERLAELEYLRAALRLWFA--QRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 876 CLQARWHAVREEKAKAANLLRDVTK----AEEDLERLAEEKSQLDLDvkylteALGPLSKEKEQLlsdyndmkirrNQEY 951
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEArldaLREELDELEAQIRGNGGD------RLEQLEREIERL-----------EREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 952 EELAEKKRNYQQEVEALlkasykineyhDLKKGERLDDIQEKQRLSDSQLQSCEARKNELAgelnrnkdlmRNQDQLRRN 1031
Cdd:COG4913 355 EERERRRARLEALLAAL-----------GLPLPASAEEFAALRAEAAALLEALEEELEALE----------EALAEAEAA 413
|
250 260 270
....*....|....*....|....*....|.
gi 18402837 1032 IEDnlnyrtTKAKVEELTREIESLEEQILNI 1062
Cdd:COG4913 414 LRD------LRRELRELEAEIASLERRKSNI 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
187-994 |
2.15e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 187 TKALEVIKKLHKDQAQEIKtfklklENLQTLKDAAYKLRESIAQDQERTessKVQMLELETSVQKVDAEVHNKEMMLKDL 266
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLE------EIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 267 rklqdqvsiktAERSTLFKEQQRQYAALPEENEDTIEELKEWKSKFEERLALLGTKIRKMEREMVDTETTISSLHNaktn 346
Cdd:TIGR02169 321 -----------EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 347 ymlEISKLQTEAEAhmlLKNERDSTIQNIffhynlgnvpstpfstEVVLNLTNRIKSRLGELEMDLLDkKKSNETALSTa 426
Cdd:TIGR02169 386 ---ELKDYREKLEK---LKREINELKREL----------------DRLQEELQRLSEELADLNAAIAG-IEAKINELEE- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 427 wdcymDANDRWKSIEAQKRAKDEIKMGISKriEEKEIERDSFEFEIstVDVKQTDEREKQVQVELERKTKQNSERGFESK 506
Cdd:TIGR02169 442 -----EKEDKALEIKKQEWKLEQLAADLSK--YEQELYDLKEEYDR--VEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 507 IEQKQHEIYSLEHKIKTLNRER-------DVMAGDAEDRVKLSLKKTEQE--NLKKKHK----------KIIDECKDRIR 567
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGeryataiEVAAGNRLNNVVVEDDAVAKEaiELLKRRKagratflplnKMRDERRDLSI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 568 GVLKGRLPPEKDM---KREIVQALRSIEReyDDLSLKSREAEKEVnMLQMKIQEVNNSLF----------KHNKDTESRK 634
Cdd:TIGR02169 593 LSEDGVIGFAVDLvefDPKYEPAFKYVFG--DTLVVEDIEAARRL-MGKYRMVTLEGELFeksgamtggsRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 635 RYIESKLQALKQEsvtIDAYPKLLESAKDKRDDRKREYNMANGMRQmfepfekRARQEHSCPCCERSFTADEEASFikKQ 714
Cdd:TIGR02169 670 RSEPAELQRLRER---LEGLKRELSSLQSELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQEEEKL--KE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 715 RVKASStgEHLKALAVESSNADSvfqQLDKLRAVFEEY----SKLTTEIIPLAEKTLQEHTEELGQKSEALDDVLG-ISA 789
Cdd:TIGR02169 738 RLEELE--EDLSSLEQEIENVKS---ELKELEARIEELeedlHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrIEA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 790 QIKADKDSIEALVQPLENADRIFQEIvsyQKQIEDLEYKLDFRGlgvKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIY 869
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQEL---QEQRIDLKEQIKSIE---KEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 870 MERDISCLQARWHAVREEKAKAANllrDVTKAEEDLERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSdyndmkirrnq 949
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS----------- 952
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 18402837 950 eYEELAEKKRNYQQEVEALLKASYK-INEYHDLKKgeRLDDIQEKQ 994
Cdd:TIGR02169 953 -LEDVQAELQRVEEEIRALEPVNMLaIQEYEEVLK--RLDELKEKR 995
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1202-1280 |
2.40e-03 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 42.13 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1202 DTELEMRGRC-SAGQKvlasliIRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRkgqenfQLIVITHD 1280
Cdd:COG2274 602 DTVVGEGGSNlSGGQR------QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR------TVIIIAHR 669
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-59 |
3.78e-03 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 40.18 E-value: 3.78e-03
10 20
....*....|....*....|....*...
gi 18402837 32 IVGANGAGKTTIIECLkvscTGELPPNA 59
Cdd:cd03263 33 LLGHNGAGKTTTLKML----TGELRPTS 56
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
763-1109 |
3.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 763 AEKTLQEHTEELGQKSEALDDVLGISAQIKADKDSIEALVQPLENADRIFQEIVsyqkqiEDLEYKLDFRGLGVKTMEEI 842
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE------EERDDLLAEAGLDDADAEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 843 QSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEKA----KAANLLRDVTKAEEDLERLAEEKSQLDLD 918
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelreEAAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 919 VKYLTEA-------LGPLSKEKEQLLSDYNDMKIRRNqEYEELAEKKRNYQQEVEALLKASYKINEYHDLKKGERLDDIQ 991
Cdd:PRK02224 393 IEELRERfgdapvdLGNAEDFLEELREERDELREREA-ELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 992 EK-QRLSD--SQLQSCEARKNELAGELNRNKDLMRNQDQLRRNIE--DNLNYR--TTKAKVEELTREIESLEEQilnigg 1064
Cdd:PRK02224 472 EDrERVEEleAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELiaERRETIEEKRERAEELRER------ 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18402837 1065 IAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQ 1109
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
161-555 |
4.39e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 161 DESNWPLQDPSTLKKKFDdifsatRYTKALEVIKKLHKDQAQEIKTFKL--KLENLQTLKDAAYKLRESIAQDQERTESS 238
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQP------SVVSAVTGESKEPKEEKKQVKIPRQsgVSSEVAEEEKEATKDAAEAKAQLPKSEQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 239 KVQMLE--LETSVQKV-DAEVHNKEMMLKDLRKLQDQVSIKTAERSTLFKEQQRQYAALPEENEDTIEELKEW----KSK 311
Cdd:pfam09731 126 KEKALEevLKEAISKAeSATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVinlaKQS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 312 FEERLALLGTKIRKMEREMVDTETTISSLHNAKTNYMLEISKL-QTEAEAHMLLKNERDSTIQNIFFHYNLGNVPSTPFS 390
Cdd:pfam09731 206 EEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYkELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 391 TEVVLNLtnriKSRLGELEMDLLDKKKSNETALStawdcymdandrwKSIEAQKRAKDEIKMGISKRIEEKEIERDS-FE 469
Cdd:pfam09731 286 NSLIAHA----HREIDQLSKKLAELKKREEKHIE-------------RALEKQKEELDKLAEELSARLEEVRAADEAqLR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 470 FEISTVDVKQTDEREKQVQVELERKTKQNSERGFESKIEQKQHEIYSLEHKIKT-LNRERDVMAGDAE---------DRV 539
Cdd:pfam09731 349 LEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkVEEERAGRLLKLNellanlkglEKA 428
|
410
....*....|....*.
gi 18402837 540 KLSLKKTEQENLKKKH 555
Cdd:pfam09731 429 TSSHSEVEDENRKAQQ 444
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1202-1279 |
4.44e-03 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 40.29 E-value: 4.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1202 DTELEMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRKGqenfqlIVITH 1279
Cdd:cd03251 129 DTVIGERGvKLSGGQRQ------RIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTT------FVIAH 195
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
438-985 |
4.45e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 438 KSIEAQKRAKDEIKMGISKRIEE---KEIERDSFEFEISTVDVKQTDERE------KQVQVELERKTKQNSERGFESKIE 508
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKAEEakkDAEEAKKAEEERNNEEIRKFEEARmahfarRQAAIKAEEARKADELKKAEEKKK 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 509 QKQHEIYSLEHKIKTLNR--ERDVMAGDAEDRVKLSLKKTEQENLKKKHKKIIDECKDRIRGVLKGRLPPEKDmKREIVQ 586
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAE 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 587 ALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNSLFKHNKDTESRKRYIESKLQAlkQESVTIDAYPKLLESAKdKRD 666
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKKAEEAK-KAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 667 DRKREYNMANGMRQMFEPFEKRARQEHSCPCCERSFTADEeasfIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLR 746
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE----AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 747 AVFEEYSKLTTEIIPLAEKTLQEHTEELgQKSEAL---DDVLGISAQIKADKDSIEALvQPLENADRIFQEIVSYQKQIE 823
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELkkaEEKKKAEEAKKAEEDKNMAL-RKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 824 DLEYKLDFRGLG------VKTMEEIQSELSSLQSSKDKLHGELEKLRDDQIYMERDISCLQARWHAVREEKAKAAnlLRD 897
Cdd:PTZ00121 1602 EEEKKMKAEEAKkaeeakIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK--AEE 1679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 898 VTKAEEDlERLAEEKSQLDLDVKYLTEALGPLSKEKEQLLSDYNDMKIRRNQEYEELAEKKRNYQQEVEALLKASYKINE 977
Cdd:PTZ00121 1680 AKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
....*...
gi 18402837 978 YHDLKKGE 985
Cdd:PTZ00121 1759 IAHLKKEE 1766
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-68 |
4.57e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 41.26 E-value: 4.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18402837 8 LIKGIRSFDpeNKNVVTFFRPLTLIVGANGAGKTTIIECLKVSCTGELPPNARSGHSFIHD 68
Cdd:COG4694 7 KLKNVGAFK--DFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAG 65
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1202-1279 |
5.13e-03 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 39.88 E-value: 5.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1202 DTELEMRGR-CSAGQKVLasliirLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRkgqenfQLIVITH 1279
Cdd:cd03245 131 DLQIGERGRgLSGGQRQA------VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK------TLIIITH 197
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
553-1119 |
5.49e-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: 41.20 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 553 KKHKKIIDECKDRIRGVLKGRLPPEKDMKREIVQALRSIEREYDDLSLKSREAEKEVNMLQMKIQEVNNS-------LFK 625
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEieelqkeLYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 626 HNK---DTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKR----DDRKREYNMANGMRQMFEPFEKRARQEHscPCC 698
Cdd:TIGR02168 293 LANeisRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeelAELEEKLEELKEELESLEAELEELEAEL--EEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 699 ERSFTADEEAsfIKKQRVKASSTGEHLKALAVESSNADSVFQQLDKLRAVFEEysKLTTEIIPLAEKTLQEHTEELGQKS 778
Cdd:TIGR02168 371 ESRLEELEEQ--LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 779 EALDDVLG----ISAQIKADKDSIEALVQPLENADRIFQEIVSYQKQIEDLEYKLDFRGLGVKT-MEEIQSELSSLQSSK 853
Cdd:TIGR02168 447 EELEELQEelerLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAlLKNQSGLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 854 DKLHGE------LEKL---RDDQIYMERDISCLQARWHAVREEKAKAA----NLLRDVTKAEEDLERLAEEKSQLDL--- 917
Cdd:TIGR02168 527 ELISVDegyeaaIEAAlggRLQAVVVENLNAAKKAIAFLKQNELGRVTflplDSIKGTEIQGNDREILKNIEGFLGVakd 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 918 ----DVKY----------------LTEALGPLSK-------------------------EKEQLLSDYNDMKIRRN-QEY 951
Cdd:TIGR02168 607 lvkfDPKLrkalsyllggvlvvddLDNALELAKKlrpgyrivtldgdlvrpggvitggsAKTNSSILERRREIEELeEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 952 EELAEKKRNYQQEVEALLKASYKI-NEYHDLKKgeRLDDIQEKQRLSDSQLQSCEARKNELAGELNRNKDLMRNQDQLRR 1030
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELeEELEQLRK--ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1031 NIEDNLNYRTTKAKveELTREIESLEEQILNIGGIAAVEAEIVKILRERERLLS-ELNRCRGTVSVYESSISKNRVELKQ 1109
Cdd:TIGR02168 765 ELEERLEEAEEELA--EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRIAATERRLED 842
|
650
....*....|
gi 18402837 1110 AQYKDIDKRH 1119
Cdd:TIGR02168 843 LEEQIEELSE 852
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1202-1279 |
5.54e-03 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1202 DTELEMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRkgqenfQLIVITH 1279
Cdd:cd03253 128 DTIVGERGlKLSGGEKQ------RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR------TTIVIAH 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1212-1290 |
5.84e-03 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 39.82 E-value: 5.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18402837 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPnsesLAGALLRIMEDRKgQENFQLIVITHDERFAQMIGQR 1290
Cdd:cd03262 137 SGGQQQ------RVAIARALAMNPKVMLFDEPTSALDPE----LVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1202-1281 |
7.00e-03 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 40.42 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1202 DTEL-EMRGRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNSESLAGALLRIMEDRKgqenfqLIVITHD 1280
Cdd:TIGR02868 462 DTVLgEGGARLSGGERQ------RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRT------VVLITHH 529
|
.
gi 18402837 1281 E 1281
Cdd:TIGR02868 530 L 530
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
7-671 |
8.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 7 MLIKGIR--SFDPENKNVVTFFRPLTLIVGANGAGKTTIIECLKVSCTGElppnARSGHsfIHDPKVAGETETKAQIKLR 84
Cdd:PRK01156 1 MIIKRIRlkNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTD----KRTEK--IEDMIKKGKNNLEVELEFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 85 fktaAGKDVVCIRSfQLTQKASKMEYKAIESVLQTInphtgekvcLSYRCADMDREIPA-LMGVSKAILENVIFVHQDES 163
Cdd:PRK01156 75 ----IGGHVYQIRR-SIERRGKGSRREAYIKKDGSI---------IAEGFDDTTKYIEKnILGISKDVFLNSIFVGQGEM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 164 NWPLQ-DPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEIKTFKLKLENLQTLKDAAYKLRESIAQDQERTESSKVQM 242
Cdd:PRK01156 141 DSLISgDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 243 LELETSVQKVDAEVHNKEMMLKDLRKLQDQVS-----IKTAERSTLFKEQQRQYAALPEENEDTIEELKEWKSKFEERLA 317
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKSALNELSSLEDMKNryeseIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 318 LLGTKIRKMEREMVDT-ETTISSLHNAktnyMLEISKLQTEAEAHMLLKNERDSTIQNIF----FHYNLGNVPSTPFSTE 392
Cdd:PRK01156 301 FKYKNDIENKKQILSNiDAEINKYHAI----IKKLSVLQKDYNDYIKKKSRYDDLNNQILelegYEMDYNSYLKSIESLK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 393 VVLNLTNRIKSRLGELEMDLLDKKKSNETALSTAWD----CYMDANDRWKSIEAQKRAKDEIKMGISKRIEEKEIErdsf 468
Cdd:PRK01156 377 KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNeinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ---- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 469 efeiSTVDVKQTDEREKqvQVELERKTKQNSERGFESKIEQKQHEIYSLEHKIKTLNRERDVMAGD------AEDRVKLS 542
Cdd:PRK01156 453 ----SVCPVCGTTLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEeinksiNEYNKIES 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 543 LK------KTEQENLKKKHKKiIDECKDRIRGVLKGRLppekDMKREIVQALRSIEREYDDLSLKSR--EAEKEVNMLQM 614
Cdd:PRK01156 527 ARadlediKIKINELKDKHDK-YEEIKNRYKSLKLEDL----DSKRTSWLNALAVISLIDIETNRSRsnEIKKQLNDLES 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 18402837 615 KIQEVNNSLFKHNKDTESRKRYIESKLQALKQESVTIDAYPKLLESAKDKRDDRKRE 671
Cdd:PRK01156 602 RLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQ 658
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
952-1111 |
8.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 952 EELAEKKRNYQQEVEallkasyKINEYHDLKKGERLDDIQEKQRLSDSQLQSCEARKNELAGELNRnkdlmrnqdqlrrn 1031
Cdd:COG4913 255 EPIRELAERYAAARE-------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER-------------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18402837 1032 iednlnyrtTKAKVEELTREIESLEEQILNIGG--IAAVEAEIVKILRERERLLSELNRCRGTVSVYESSISKNRVELKQ 1109
Cdd:COG4913 314 ---------LEARLDALREELDELEAQIRGNGGdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
..
gi 18402837 1110 AQ 1111
Cdd:COG4913 385 LR 386
|
|
| |
