|
Name |
Accession |
Description |
Interval |
E-value |
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-1309 |
1.74e-162 |
|
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: 521.53 E-value: 1.74e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 2 STVDKMLIKGIRSFDPENKNV--ITFFKPLTLIVGPNGAGKTTIIECLKLSCTGELPPNSRsGHTFVHDPKVAGETETKG 79
Cdd:TIGR00606 1 AKFLKMSILGVRSFGIEDKDKqiIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTK-GNTFVHDPKVAQETDVRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 80 QIKLRFKTAAGKDVVCIRSFQLTQKASKMEFKAIESVLqTINPHtGEKVCLSYRCADMDREIPALMGVSKAILENVIFVH 159
Cdd:TIGR00606 80 QIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVI-TRYKH-GEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 160 QDESNWPLQDPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEIKTFRLKLENLQTLKDQAYRLRDNIAQDQEKSDALK 239
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 240 IQMEELRTNVQGVEDKIRRTEKSLADLRRLQQEINSSTSARTTYFTLQQQQYAALSEENEDTDDELKEWQTKFEERMALL 319
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 320 QNKISKLERDVDDENTTSSFLSKAINDLMRETGRLQAEADAHMSVKHERDSAIRKIFTKHNLGPIPDAPLTDAAAMHLTN 399
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 400 ITKAKLSN-------LNDDLQDKKKSneAQKQFlwgRYLEVNTRYSEVVGQIESKVASKKGISRRMKDKESERDAAEMDl 472
Cdd:TIGR00606 398 LVIERQEDeaktaaqLCADLQSKERL--KQEQA---DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 473 skynlpRIDEKERHLqieveRKALAlgernyDSIVNQKRTEIFSLDQKIKTLQWEKDSIISDSNDRVLLDVKKDELEESK 552
Cdd:TIGR00606 472 ------RILELDQEL-----RKAER------ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 553 KKLKKIFDEHKDKIRIVFKGRTPSEKEV---------KKELSQAFGSVDREYNDLNSKSQEAAQEL-KLVQMKildarSH 622
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELaSLEQNK-----NH 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 623 LSKLQKELDAKRSYVESKLQSITKMSAdinmFPKHLKDAMDEREKQKNNLSYAKGMRQMYEPF--ENLARELHMCPCCQR 700
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKLFDVCGSQD----EESDLERLKEEIEKSSKQRAMLAGATAVYSQFitQLTDENQSCCPVCQR 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 701 AF-TPDEEDEFVKKQRTTCESTADRMNKISLECSNAEDFFQQLNKLNATYEEFVKLGKEAIPLAEKNLKQLLADESEKAQ 779
Cdd:TIGR00606 686 VFqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 780 TFDDFVSVLAQVKMDKDAVQVLLQPVETIDRHVQEIQQLGPQVENLEYKLDvRGQGVKSLEQIQLELNSVQRTRDTLNNE 859
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ-GSDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 860 VDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQE 939
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 940 HEALKEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKKGEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNK 1019
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1020 ELLKSQDQLKRNIDDNLNYRRTKDEV-----ERLTHEIELLEDKILSIGSlstieaDLKQHSQEKDRLLSEYNRCQGTQS 1094
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLRKRENELkeveeELKQHLKEMGQMQVLQMKQ------EHQKLEENIDLIKRNHVLALGRQK 1078
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1095 VYQSNISKHKLELKQTQYKDIEKRYFNQLLQLKTTEMANKDLDRYYAALDKALMRFHTMKMEEINKIIKELWQQTYRGQD 1174
Cdd:TIGR00606 1079 GYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQD 1158
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1175 IDYISINSD-----SEGAGTRSYSYRVVMQTGDAELEMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDG 1249
Cdd:TIGR00606 1159 IEYIEIRSDadenvSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDR 1238
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1250 PNAESLAGALLRIMESRKGQENFQLIVITHDERFAQLIGQRQLAEKYYRVSKDEHQHSKI 1309
Cdd:TIGR00606 1239 ENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRLKKNEDQCSEI 1298
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1205-1308 |
6.26e-44 |
|
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: 158.54 E-value: 6.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1205 LEMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDGPNAEslaGALLRIMESRKGQENFQLIVITHDERFa 1284
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIE---ESLAEIIEERKSQKNFQLIVITHDEEL- 185
|
90 100
....*....|....*....|....
gi 1002245190 1285 qligqRQLAEKYYRVSKDEHQHSK 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 |
2.37e-41 |
|
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: 151.22 E-value: 2.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 4 VDKMLIKGIRSFDpeNKNVITFFKPLTLIVGPNGAGKTTIIECLKLSCTGELPPNSRSGHtfvHDPKVAGETETKGQIKL 83
Cdd:cd03240 1 IDKLSIRNIRSFH--ERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGA---HDPKLIREGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 84 RFKTAAGKDVVCIRSFqltqkaskmefkaiesvlqtinphtgekvclsyrcadmdreipalmgvskAILENVIFVHQDES 163
Cdd:cd03240 76 AFENANGKKYTITRSL--------------------------------------------------AILENVIFCHQGES 105
|
....*..
gi 1002245190 164 NWPLQDP 170
Cdd:cd03240 106 NWPLLDM 112
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-220 |
5.57e-25 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 103.73 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 9 IKGIRSFDPENknvITFFKPLTLIVGPNGAGKTTIIECLKLSCTGELP--PNSRSGHTFVHDPKVAGETETKGQIKLRFK 86
Cdd:pfam13476 3 IENFRSFRDQT---IDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSrlKRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 87 TAAGKDVVCI-RSFQLTQKASKMEFKAIESVLQTinphtgekvclsyrcADMDREIPALMGVSKAILENVIFVHQDEsnw 165
Cdd:pfam13476 80 NNDGRYTYAIeRSRELSKKKGKTKKKEILEILEI---------------DELQQFISELLKSDKIILPLLVFLGQER--- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1002245190 166 plQDPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEIKtfrlKLENLQTLKDQ 220
Cdd:pfam13476 142 --EEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKE----KKKELEELKEE 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-1111 |
2.93e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 457 RMKDKESERDAAEMDLSKYN--LPRIDEKERHLQIEVERKALALGERnyDSIVNQKRTEIFSLDQKIKTLQWEK----DS 530
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEeeLEELTAELQELEEKLEELRLEVSEL--EEEIEELQKELYALANEISRLEQQKqilrER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 531 IISDSNDRVLLDVKKDELEESKKKLKKIFDEHKDKIRIV------FKGRTPSEKEVKKELSQAFGSVDREYNDLNSKSQE 604
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 605 AAQELKLVQMKILDARSHLSKLQKELDAKRSYVESKLQSIT-----KMSADINMFPKHLKDAMDEREKQKNNLSYAKG-- 677
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREel 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 678 ------MRQMYEPFENLARELHMCPCCQRAF-TPDEEDEFVKKQR--------------------TTCESTADRMNKISL 730
Cdd:TIGR02168 471 eeaeqaLDAAERELAQLQARLDSLERLQENLeGFSEGVKALLKNQsglsgilgvlselisvdegyEAAIEAALGGRLQAV 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 731 ECSNAEDFFQQLNKLnatyeEFVKLGKEA-IPLAEKNLKQLLADESEKAQTFDDFVSVLAQVKMDKDAVQVLLQP----- 804
Cdd:TIGR02168 551 VVENLNAAKKAIAFL-----KQNELGRVTfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 805 --VETIDRHVQEIQQLGPQVEN--LEYKLdVRGQGV----------------KSLEQIQLELNSVQRTRDTLNNEVDDLR 864
Cdd:TIGR02168 626 lvVDDLDNALELAKKLRPGYRIvtLDGDL-VRPGGVitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 865 DQQRTLTDGLTNAQMRWHDIR----EEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLEESLGplskERESLLQEH 940
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 941 EALKEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKKgEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKE 1020
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR-ERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1021 LLKSQDQLKRNIDDNLNyrRTKDEVERLTHEIELLEDKilsigsLSTIEADLKQHSQEKDRLLSEYNRCQGTQSVYQSNI 1100
Cdd:TIGR02168 860 EIEELEELIEELESELE--ALLNERASLEEALALLRSE------LEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
730
....*....|.
gi 1002245190 1101 SKHKLELKQTQ 1111
Cdd:TIGR02168 932 EGLEVRIDNLQ 942
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1207-1301 |
1.79e-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: 63.92 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1207 MRGRCSAGQKVLASLIIRLALAEtfCLNCGILALDEPTTNLDGPNAESLAGAllrIMESRkgQENFQLIVITHDERFAql 1286
Cdd:cd03227 74 TRLQLSGGEKELSALALILALAS--LKPRPLYILDEIDRGLDPRDGQALAEA---ILEHL--VKGAQVIVITHLPELA-- 144
|
90
....*....|....*
gi 1002245190 1287 igqrQLAEKYYRVSK 1301
Cdd:cd03227 145 ----ELADKLIHIKK 155
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1212-1292 |
1.37e-10 |
|
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: 61.11 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMesrkgQENFQLIVITHDERFAQLIGQRQ 1291
Cdd:cd00267 82 SGGQRQ------RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-----EEGRTVIIVTHDPELAELAADRV 150
|
.
gi 1002245190 1292 L 1292
Cdd:cd00267 151 I 151
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1211-1292 |
9.47e-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: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1211 CSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMESRKGqenfqLIVITHDERFAQLIGQR 1290
Cdd:cd03226 127 LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA-----VIVITHDYEFLAKVCDR 195
|
..
gi 1002245190 1291 QL 1292
Cdd:cd03226 196 VL 197
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-120 |
2.74e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 58.48 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 9 IKGIRSFdpENKNVITFFKPLTLIVGPNGAGKTTIIECLKLSCTGELPPNSRSGHTFVHDPkvagetETKGQIKLRFkTA 88
Cdd:COG0419 7 LENFRSY--RDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVG------SEEASVELEF-EH 77
|
90 100 110
....*....|....*....|....*....|..
gi 1002245190 89 AGKDVVCIRSFQLTQKASKMEFKAIESVLQTI 120
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEAKPSERKEALKRL 109
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
771-1111 |
2.95e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 771 LADESEKAQTFDDFvsvlaQVKMDKDAVQVLLQPVETIDRhvqEIQQLGPQVENLEYKLDvrgQGVKSLEQIQLELNSVQ 850
Cdd:TIGR02169 203 LRREREKAERYQAL-----LKEKREYEGYELLKEKEALER---QKEAIERQLASLEEELE---KLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 851 RTRDTLNNEVDDL-RDQQRTLTdgltnAQMRWHDIREEKLKASGAVHK--FQKAEEDLGHLAEEKEKLTLEEKHLEESLG 927
Cdd:TIGR02169 272 QLLEELNKKIKDLgEEEQLRVK-----EKIGELEAEIASLERSIAEKEreLEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 928 PLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALethnerikgylnSKKGEKLNELQEKHTQLQSDLQKSKER 1007
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL------------KDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1008 KEEKSAELSKNKELLKSqdqlkrnIDDNLNyrRTKDEVERLTHEIELLEDKilsigsLSTIEADLKQHSQEKDRLLSEYN 1087
Cdd:TIGR02169 415 LQRLSEELADLNAAIAG-------IEAKIN--ELEEEKEDKALEIKKQEWK------LEQLAADLSKYEQELYDLKEEYD 479
|
330 340
....*....|....*....|....
gi 1002245190 1088 RCQGTQSVYQSNISKHKLELKQTQ 1111
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASE 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1084 |
5.68e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 839 LEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVHKFQK----AEEDLGHLAEEKEK 914
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrreLEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 915 LTLEEKHLEESLGPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKKgEKLNELQEKH 994
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 995 TQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLKRNIDDNLNyRRTKDEVERLTHEIELLEDKILSIGSLSTIEADLKQ 1074
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE-EEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250
....*....|
gi 1002245190 1075 HSQEKDRLLS 1084
Cdd:COG1196 486 LAEAAARLLL 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
285-1308 |
1.46e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 59.60 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 285 TLQQQQYAALSEENEDTDDELKEWQTKFEERMALLQNKISKLERDVDDENTTSSFLSKAINDLMRETGRLQAEADAHMSV 364
Cdd:pfam02463 193 EELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 365 KHERDSAIRKIFTKHNLgpipdaplTDAAAMHLTNITKAKLSNLNDDLQDKKKSNEAQKQFLwgrylevntrysevvgQI 444
Cdd:pfam02463 273 ENKEEEKEKKLQEEELK--------LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA----------------EK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 445 ESKVASKKGISRRMKDKESERDAAEMDLSKYNLPRIDEKERHLQIEVERKAlalgernydsivnQKRTEIFSLDQKIKTL 524
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-------------KLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 525 QWEKDSIISDSNDRVLLDVKKDELEESKKKLKKIFDEHKDKIRIVFKGRTPSEKEVKKELSQAFGSVDREYNDLNSKSQE 604
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 605 AAQELKLVQMKILDArshLSKLQKELDAKRSYVESKLQSITKMSADINmfPKHLKDAMDEREKQKNNLSYAKGMRQMYEP 684
Cdd:pfam02463 476 ETQLVKLQEQLELLL---SRQKLEERSQKESKARSGLKVLLALIKDGV--GGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 685 FEN--LARELHMCPCCQRAFTPdeEDEFVKKQRTTCESTADRMNKISLECSNAEDFFQQLNKLNATYEEFVKLGKEAIPL 762
Cdd:pfam02463 551 VEVsaTADEVEERQKLVRALTE--LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 763 AEKNLKQLLADESEKAQTFDDFVSVLAQVKMDKDAVQVLLQPVETIDRHVQEIQQLGPQVENLEYKLDVRGQGVKSLEQI 842
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 843 QLELNsvqrtRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHL 922
Cdd:pfam02463 709 KEELK-----KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 923 EESLGPLSKERESLLQEHEALKEKLDQEYhqLAERKREFQQEIDALEthNERIKGYLNSKKGEKLNELQEKHTQLQSDLQ 1002
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKE--EAELLEEEQLLIEQEE--KIKEEELEELALELKEEQKLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1003 KSKERKEEKSAELSKNKELLKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDKILSIGSLSTIEADLKQHSQEKDRL 1082
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1083 LSEYNRCQGTQSVYQSNISKHKLELKQTQYKDIEKRYFNQLLQLKTTEMANKDLDRYYAAL---DKALMRFHTMKMEEIN 1159
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLeeeKKKLIRAIIEETCQRL 1019
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1160 KIIKELWQQTYRGQDIDYISINSDSEGAGTRSYSY-------RVVMQTGDAELEMRGRCSAGQKVLASLIIRLALAE--- 1229
Cdd:pfam02463 1020 KEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDdpfsggiEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKykp 1099
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1230 -TFCLncgilaLDEPTTNLDGPNAESLAGALlrimesRKGQENFQLIVITHDErfaqliGQRQLAEKYYRVSKDEHQHSK 1308
Cdd:pfam02463 1100 aPFYL------LDEIDAALDDQNVSRVANLL------KELSKNAQFIVISLRE------EMLEKADKLVGVTMVENGVST 1161
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
806-1310 |
3.18e-08 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 58.21 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 806 ETIDRHVQEIQQ------LGPQVENLEYKLDvrgQGVKSLEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQM 879
Cdd:COG4694 79 DFVEENLRSGEEikgiftLGEENIELEEEIE---ELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 880 RWHDIREEKLKASGAVHKFQKAEEDLGH----LAEEKEKLTLEEKHLEESLGPLSKERESLLQE------HEALKEKLD- 948
Cdd:COG4694 156 ASSGRNYRKANLEKKLSALKSSSEDELKeklkLLKEEEPEPIAPITPLPDLKALLSEAETLLEKsavssaIEELAALIQn 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 949 ----------QEYHQLAERKR-EF-QQEIDAlethnERIKgYLNSKKGEKLNELQEKHTQLQSDLQKSKERKEEKSAEL- 1015
Cdd:COG4694 236 pgnsdwveqgLAYHKEEEDDTcPFcQQELAA-----ERIE-ALEAYFDDEYEKLLAALKDLLEELESAINALSALLLEIl 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1016 -----SKNKELLKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDKILSIGSLSTIEADLKQHSQEKDRLLSEYNRCQ 1090
Cdd:COG4694 310 rtllpSAKEDLKAALEALNALLETLLAALEEKIANPSTSIDLDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEAR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1091 gtQSVYQSNIskHKLELKQTQYKDIEKRYFNQLLQLKTTEMANKDLDRYYAALDKALMRFHTMKmEEINKIIKELwqqty 1170
Cdd:COG4694 390 --KKLEAHEL--AELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAA-DEINEELKAL----- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1171 rgqDIDYISINSDSEGagtrSYSYRVVMQTGDAElEMRGRCSAGQKVLASLIIRLALAE--TFCLNCGILALDEPTTNLD 1248
Cdd:COG4694 460 ---GFDEFSLEAVEDG----RSSYRLKRNGENDA-KPAKTLSEGEKTAIALAYFLAELEgdENDLKKKIVVIDDPVSSLD 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002245190 1249 GPNAESLAGaLLRimesRKGQENFQLIVITHDERFAQLI------GQRQLAEKYYRVSKDEHqHSKIE 1310
Cdd:COG4694 532 SNHRFAVAS-LLK----ELSKKAKQVIVLTHNLYFLKELrdladeDNKKKNCAFYEIRKDNR-GSKII 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1151 |
6.27e-08 |
|
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: 57.37 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 844 LELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASgavHKFQKAEEDLGHLAEEKEKLTLEEKHLE 923
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE---EEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 924 ESLGPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQ---EIDALETHNERIKGYLNSKKgEKLNELQEKHTQLQSD 1000
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAELEELE-SRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1001 LQKSKERKEEKSAELSKNKELLKsqdqlkrniddnlnyrRTKDEVERLTHEIELLEDKiLSIGSLSTIEADLKQHSQEKD 1080
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLE----------------RLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002245190 1081 RLLSEYNRCQgtQSVYQSNISKHKLELKQTQYKDIEKRYFNQLLQLKTTEMANKDLDRYYAALDKALMRFH 1151
Cdd:TIGR02168 451 ELQEELERLE--EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1212-1283 |
1.32e-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: 1.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALlrimesrkgqENFQ--LIVITHDERF 1283
Cdd:cd03221 72 SGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----------KEYPgtVILVSHDRYF 129
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
578-1279 |
1.36e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 578 KEVKKELSQAFGSVDREYNDLNSKSQEAAQELKlvqmKILDARSHLSKLQKELDAKRSYVESKLQSITKMSADINmfpkH 657
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIKK----QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----E 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 658 LKDAMDEREKQKNNLSYAKGMRQMYEPFENLAREL---HMCPCCQRAFTPDEEDEFVKKQRTTCESTADRMNKISLECSN 734
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELeerHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 735 AEDFFQQLNKLNATYEEFVKLGKEaiplaEKNLKQLLADESEKAQTFDDFVSVLAQVKMDKDAVQVLLQPVETIDRHVQE 814
Cdd:PRK01156 324 YHAIIKKLSVLQKDYNDYIKKKSR-----YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 815 IQQLGPQVENLEYKlDVRgqgvKSLEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLtDGLTNAQMRWHDIREEKLK--AS 892
Cdd:PRK01156 399 IQEIDPDAIKKELN-EIN----VKLQDISSKVSSLNQRIRALRENLDELSRNMEML-NGQSVCPVCGTTLGEEKSNhiIN 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 893 GAVHKFQKAEEDLGHLAEEKEKLTLEEKHLEESLGPLSKEReslLQEHEALKEKLDQEYHQLAERKREfQQEIDALETHN 972
Cdd:PRK01156 473 HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE---INKSINEYNKIESARADLEDIKIK-INELKDKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 973 ERIKGYLNSKKGEKLNELQEKHTQLQS-----DLQKSKERKEEKSAELsknKELLKSQDQLKRNIDDNLNY-----RRTK 1042
Cdd:PRK01156 549 EEIKNRYKSLKLEDLDSKRTSWLNALAvisliDIETNRSRSNEIKKQL---NDLESRLQEIEIGFPDDKSYidksiREIE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1043 DEVERLTHEIELLEDKILSIGSLSTIEADLKQHSQEKDRLL--------------SEYNRCQGTQSVYQSNIS--KHKLE 1106
Cdd:PRK01156 626 NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIpdlkeitsrindieDNLKKSRKALDDAKANRArlESTIE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1107 LKQTQYKDIEKRYFN---QLLQLKTTEMANKDLDRYYAALDKALMRfhTMKMEEINKIIKELWQQTYRGQDIDYISINSD 1183
Cdd:PRK01156 706 ILRTRINELSDRINDineTLESMKKIKKAIGDLKRLREAFDKSGVP--AMIRKSASQAMTSLTRKYLFEFNLDFDDIDVD 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1184 SEGAGTrsySYRVVMQTGDAELemrgrcSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIM 1263
Cdd:PRK01156 784 QDFNIT---VSRGGMVEGIDSL------SGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSL 854
|
730
....*....|....*.
gi 1002245190 1264 ESRKGQEnfQLIVITH 1279
Cdd:PRK01156 855 KDSSDIP--QVIMISH 868
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
880-1147 |
2.41e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 880 RWHDIREE--KLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLD---QEYHQL 954
Cdd:COG1196 214 RYRELKEElkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 955 AERKREFQQEIDALETHNERIKgylnskkgEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLKRNIDD 1034
Cdd:COG1196 294 LAELARLEQDIARLEERRRELE--------ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1035 NLNyRRTKDEVERLTHEIELLEDKILSIGSLSTIEADLKQHSQEKDRLLSEYNRCQGTQSVYQSNISKHKLELKQTQ--Y 1112
Cdd:COG1196 366 ALL-EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEeaL 444
|
250 260 270
....*....|....*....|....*....|....*
gi 1002245190 1113 KDIEKRYFNQLLQLKTTEMANKDLDRYYAALDKAL 1147
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-85 |
4.39e-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: 51.21 E-value: 4.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 20 KNVITFFKP-LTLIVGPNGAGKTTIIECLKLSCTGELPPNSRsghtfvhdPKVAGETETKGQIKLRF 85
Cdd:cd03227 13 PNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRR--------RSGVKAGCIVAAVSAEL 71
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1190-1259 |
1.39e-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: 47.61 E-value: 1.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002245190 1190 RSYSYRVVMQTGDAEL--EMRGRCSAGQK-VLASLIIRLALAETFCLN------CGILALDEPTTNLDGPNAESLAGAL 1259
Cdd:pfam13558 10 LSFEVEVRDEDGSEVEtyRRSGGLSGGEKqLLAYLPLAAALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
428-1085 |
2.98e-06 |
|
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: 51.99 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 428 GRYLEVNTRYSEVVGQIESKVASKKGISRRMKDKESERdaaemdlskynlpridekerhlqieverkalalgeRNYDSIV 507
Cdd:TIGR02169 287 EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL-----------------------------------AKLEAEI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 508 NQKRTEIFSLDQKIKTLQWEKDSIISD-SNDRVLLDVKKDELEESKKKLKKIFDEHKDkirivfkgrtpsEKEVKKELSQ 586
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKD------------YREKLEKLKR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 587 AFGSVDREYNDLNSKSQEAAQELKLVQMKILDARSHLSKLQKELDAKRSYVESKLQSITKMSADinmfpkhLKDAMDERE 666
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD-------LSKYEQELY 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 667 KQKNNLsyakgmRQMYEPFENLARELHMCPCCQRAFTPDEED----EFVKKQR-------------------TTCESTA- 722
Cdd:TIGR02169 473 DLKEEY------DRVEKELSKLQRELAEAEAQARASEERVRGgravEEVLKASiqgvhgtvaqlgsvgeryaTAIEVAAg 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 723 DRMNKISLEC-SNAEDFFQQLNKLNATYEEFVKLGK------EAIPLAEKNLKQLLAD--------ESEKAQTFDDFVSV 787
Cdd:TIGR02169 547 NRLNNVVVEDdAVAKEAIELLKRRKAGRATFLPLNKmrderrDLSILSEDGVIGFAVDlvefdpkyEPAFKYVFGDTLVV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 788 ---------LAQVKM------------------------------DKDAVQVLLQPVETIDRHVQEIQQLGPQVENLEYK 828
Cdd:TIGR02169 627 edieaarrlMGKYRMvtlegelfeksgamtggsraprggilfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 829 L-DVRGQGVKSLEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNA--------------QMRWHDIREE--KLKA 891
Cdd:TIGR02169 707 LsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelearieelEEDLHKLEEAlnDLEA 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 892 SGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLDqeyhQLAERKREFQQEIDALETH 971
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI----DLKEQIKSIEKEIENLNGK 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 972 NERIKGYLNSKKGEkLNELQEKHtqlqSDLQKSKERKEEKSAELSKNKELLKSQDQLKRNIDDNLNYRRtkdevERLTHE 1051
Cdd:TIGR02169 863 KEELEEELEELEAA-LRDLESRL----GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-----EALEEE 932
|
730 740 750
....*....|....*....|....*....|....
gi 1002245190 1052 IELLEDKILSIGSLSTIEADLKQHSQEKDRLLSE 1085
Cdd:TIGR02169 933 LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1202-1280 |
4.72e-06 |
|
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: 50.91 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1202 DAELEMRGRC-SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMESRkgqenfQLIVITHD 1280
Cdd:COG4988 464 DTPLGEGGRGlSGGQAQ------RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR------TVILITHR 531
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1212-1292 |
5.86e-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: 48.62 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAEslagALLRIMESRKgQENFQLIVITHDERFAQLIGQRQ 1291
Cdd:cd03225 136 SGGQKQ------RVAIAGVLAMDPDILLLDEPTAGLDPAGRR----ELLELLKKLK-AEGKTIIIVTHDLDLLLELADRV 204
|
.
gi 1002245190 1292 L 1292
Cdd:cd03225 205 I 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1212-1281 |
7.55e-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: 7.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMESRkgqenfQLIVITHDE 1281
Cdd:TIGR02857 460 SGGQAQ------RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR------TVLLVTHRL 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6-1008 |
8.64e-06 |
|
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: 50.35 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 6 KMLIKGIRSFDPENKNVITFFKPLTLIVGPNGAGKTTIIECLKLSCTGELPPNSRSGHT-FVHDPKVAGETETKGQIKLR 84
Cdd:TIGR00618 5 RLTLKNFGSYKGTHTIDFTALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSlNSLYAAPSEAAFAELEFSLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 85 FKT-AAGKDVVCIRSFQLTQKASKMEFKAIESVLQTINPHTGEKVCLsyrcadmdreIPALMGVSKAILENVIFVHQDE- 162
Cdd:TIGR00618 85 TKIyRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEV----------IHDLLKLDYKTFTRVVLLPQGEf 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 163 SNWPLQDPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEIKTFRLKLENLQTLKDQAYRLRDNIAQDQEKSDAlkiQM 242
Cdd:TIGR00618 155 AQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK---HL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 243 EELRTNVQGVEDKIRRTEKSLADLRRLQQEINSSTSARTTYftlqQQQYAALSEENEDTDdelkewQTKFEERMALLQNK 322
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL----RAQEAVLEETQERIN------RARKAAPLAAHIKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 323 ISKLERDVDDENTTssflskaINDLMRETGRLQAEADAHMSVKHERDSAIRKIFTKHnlgpipdapltdAAAMHLTNITK 402
Cdd:TIGR00618 302 VTQIEQQAQRIHTE-------LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH------------SQEIHIRDAHE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 403 AKLSNLNddlQDKKKSNEAQKQFLWGRYLEVNTrysevvgQIESKVASKKGISRRMKDKESERDAAEMDLskynlpRIDE 482
Cdd:TIGR00618 363 VATSIRE---ISCQQHTLTQHIHTLQQQKTTLT-------QKLQSLCKELDILQREQATIDTRTSAFRDL------QGQL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 483 KERHLQIEVERKALALGERnydSIVNQKRTEIFSLDQKIKTLQWEKDSIISDSNDRVLLDVKKDELEESKKKLKkifdEH 562
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAA---AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL----EL 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 563 KDKIRIvFKGRTpSEKEVKKELSQAFGSVDREYNDLNSKSQEAAQELKLVQMKILDARSHLSKLQKELDAKRSYVESKLQ 642
Cdd:TIGR00618 500 QEEPCP-LCGSC-IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 643 SITKMSADINMFPK------HLKDAMDEREKQKNNLSYAKgMRQMYEPFENLARELHmcpccQRAFTPDEEDEFVKKQRT 716
Cdd:TIGR00618 578 CDNRSKEDIPNLQNitvrlqDLTEKLSEAEDMLACEQHAL-LRKLQPEQDLQDVRLH-----LQQCSQELALKLTALHAL 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 717 TCESTADRMNKISLECSNAEDFFQQLNKLNATYEEfvklgkeaiplaekNLKQLLADESEKaqtfddfvsvLAQVKMdkd 796
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQLALQKMQ--------------SEKEQLTYWKEM----------LAQCQT--- 704
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 797 AVQVLLQPVETIDRHVQEIQQ-LGPQVENLEYKLDVRGQGVKSLEQiqlelnsvQRTRDTLNNEVDDLRDQQRTLTDGLT 875
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENaSSSLGSDLAAREDALNQSLKELMH--------QARTVLKARTEAHFNNNEEVTAALQT 776
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 876 NAQmrwhdirEEKLKASGAvHKFQKAEEDLGHLAeekEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKL-------- 947
Cdd:TIGR00618 777 GAE-------LSHLAAEIQ-FFNRLREEDTHLLK---TLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLeeksatlg 845
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 948 --DQEYHQLAERKREFQQ------EIDALETHNERIKGYLNSKKGEKLNEL-QEKHTQLQSDLQKSKERK 1008
Cdd:TIGR00618 846 eiTHQLLKYEECSKQLAQltqeqaKIIQLSDKLNGINQIKIQFDGDALIKFlHEITLYANVRLANQSEGR 915
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-1017 |
1.20e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 183 ATRYTKALEVIKKLHKD-QAQEIKTFRLKLENLQTLKDQAYRLRDNIaqdQEKSDALKIQMEELRTNVQGVEDKIRRTEK 261
Cdd:TIGR02168 212 AERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEEL---TAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 262 SLADLRRLQQEINSS---TSARTTYFTLQQQQYAALSEENEDTDDELKE----WQTKFEE---RMALLQNKISKLERDVD 331
Cdd:TIGR02168 289 ELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEelaeLEEKLEElkeELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 332 DENTTSS-------FLSKAINDLMRETGRLQAE---ADAHMSvkherDSAIRKIFTKHNLGPIPDAPltDAAAMHLTNIT 401
Cdd:TIGR02168 369 ELESRLEeleeqleTLRSKVAQLELQIASLNNEierLEARLE-----RLEDRRERLQQEIEELLKKL--EEAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 402 KAKLSNLNDDLQDKKKSNEAQKQFLWGRYLEVNTRYSEVVGQIESKVASKKGISRRMKDKESE-RDAAEMDLSKYNLP-- 478
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsEGVKALLKNQSGLSgi 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 479 --------RIDEK----------ERHLQIEVERKALALGERNYDSIVNQKRTEIFSLD----QKIKTLQWE----KDSII 532
Cdd:TIGR02168 522 lgvlseliSVDEGyeaaieaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDsikgTEIQGNDREilknIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 533 SDSNDRVLLDVKKDELEESKKKLKKIFDEHKDKIRIV----FKGR--TPSEKEVKKELSQAFGSVDREYNDLNSKSQ--E 604
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAkklrPGYRivTLDGDLVRPGGVITGGSAKTNSSILERRREieE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 605 AAQELKLVQMKILDARSHLSKLQKELDAKRSYVESKLQSITKMSADINMFPKHLKDAMDEREKqknnlsyakgmrqmyep 684
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----------------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 685 fenlarelhmcpCCQRAFTPDEEDEFVKKQRttcESTADRMNKISLECSNAEDffqQLNKLNATYEEFvklgKEAIPLAE 764
Cdd:TIGR02168 745 ------------LEERIAQLSKELTELEAEI---EELEERLEEAEEELAEAEA---EIEELEAQIEQL----KEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 765 KNLKQLLADESEKAQTFDDFVSVLAQVKMDKDAVQVLLQP-VETIDRHVQEIQQLGPQVENLEYkldvrgqgvkSLEQIQ 843
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEE----------LIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 844 LELNSVQRTRDTLNNEVDDLRDQQRTLTDgltnaqmrwhDIREEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLE 923
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSE----------ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 924 ESlgpLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNER-IKGYlnskkgEKLNELQEKHTQLQSDLQ 1002
Cdd:TIGR02168 943 ER---LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAaIEEY------EELKERYDFLTAQKEDLT 1013
|
890
....*....|....*
gi 1002245190 1003 KSKERKEEKSAELSK 1017
Cdd:TIGR02168 1014 EAKETLEEAIEEIDR 1028
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1212-1290 |
1.22e-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: 1.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDgpnaESLAGALLRIMESRKGQENFQLIVITHDERFAQLIGQR 1290
Cdd:cd03229 102 SGGQQQ------RVALARALAMDPDVLLLDEPTSALD----PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADR 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1209-1284 |
2.65e-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: 46.70 E-value: 2.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 1209 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDgpnAESLAgALLRIMESRKGQEnfQLIVI-THDERFA 1284
Cdd:COG4133 130 RQLSAGQKR------RVALARLLLSPAPLWLLDEPFTALD---AAGVA-LLAELIAAHLARG--GAVLLtTHQPLEL 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1224-1292 |
2.98e-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: 47.04 E-value: 2.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002245190 1224 RLALAETFCLNCGILALDEPTTNLDGPNAESLAGaLLRIMESRKGQenfQLIVITHDERFAQLIgQRQL 1292
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIID-LLFELNRERGT---TLVLVTHDPALAARC-DRVL 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
854-1130 |
4.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 854 DTLN---NEVDDLRDQQRTLTDGLTNAQmrwhdireeklkasgavhKFQKAEEDLGHLaeekekltleeKHLEESLGPLS 930
Cdd:COG4913 235 DDLErahEALEDAREQIELLEPIRELAE------------------RYAAARERLAEL-----------EYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 931 KERESLLQEHEAlkEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKKGEKLNELQEKhtqlQSDLQKSKERKEE 1010
Cdd:COG4913 286 AQRRLELLEAEL--EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLERE----IERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1011 KSAELSKNKELLK-----SQDQLKRNIddnlnyRRTKDEVERLTHEIELLEDKilsigsLSTIEADLKQHSQEKDRLLSE 1085
Cdd:COG4913 360 RRARLEALLAALGlplpaSAEEFAALR------AEAAALLEALEEELEALEEA------LAEAEAALRDLRRELRELEAE 427
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1086 YNRCQGTqsvyQSNISKHKLELK-----QTQYKDIEKRYFNQLLQLKTTE 1130
Cdd:COG4913 428 IASLERR----KSNIPARLLALRdalaeALGLDEAELPFVGELIEVRPEE 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
619-1281 |
4.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 619 ARSHLSKLQKELDAKRSYVESKLQSitkmSADINMFPKHLKDAMDEREKQKNNLSyaKGMRQMYEPFENLARELHMCPCC 698
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKR----TENIEELIKEKEKELEEVLREINEIS--SELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 699 QRAFTP-DEEDEFVKKQRTTCES----TADRMNKISLECSNAEDFFQQLNKLNATYEEFVKLGKEAIPLAEK--NLKQLL 771
Cdd:PRK03918 237 KEEIEElEKELESLEGSKRKLEEkireLEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElrEIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 772 ADESEKAQTF-------DDFVSVLAQVKMDKDAVQVLLQPVETIDRHVQEIQQLGPQVENLEYKLdvrgqGVKSLEQIQL 844
Cdd:PRK03918 317 SRLEEEINGIeerikelEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL-----TGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 845 ELNSVQRTRDTLNNEVDDLRDQQRTLTDglTNAQMRWHDIREEKLKASGAVHKFQKAEEDLGHL---------------A 909
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKK--EIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleeytaelkriekelK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 910 EEKEKLTLEEKHLEESLGPLSKERE-----SLLQEHEALKEKLD-----------QEYHQLAERKREFQQEIDALETHNE 973
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEKLKkynleelekkaEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 974 RIKGY------LNSKKGEKLNELQEKHTQLQSDLQKSKERKEEKSAEL--------------SKNKELLKSQDQLKRNID 1033
Cdd:PRK03918 550 KLEELkkklaeLEKKLDELEEELAELLKELEELGFESVEELEERLKELepfyneylelkdaeKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1034 DNLNY-RRTKDEVERLTHEIELLEdKILSIGSLSTIEADLKQHSQEKDRLLSEYNRCQGTQSVYQSNISKHKLELKQTQY 1112
Cdd:PRK03918 630 KAFEElAETEKRLEELRKELEELE-KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1113 KDIEKRYFNQLLQlKTTEMANKdLDRYyaaldKALMRFHTMKmeEINKIIKELWQQTYRGQdidYISINSDSEGAGTRSY 1192
Cdd:PRK03918 709 AKKELEKLEKALE-RVEELREK-VKKY-----KALLKERALS--KVGEIASEIFEELTEGK---YSGVRVKAEENKVKLF 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1193 syrVVMQTGDAELemrGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDgpnaESLAGALLRIMEsRKGQENF 1272
Cdd:PRK03918 777 ---VVYQGKERPL---TFLSGGERIALGLAFRLALSLYLAGNIPLLILDEPTPFLD----EERRRKLVDIME-RYLRKIP 845
|
....*....
gi 1002245190 1273 QLIVITHDE 1281
Cdd:PRK03918 846 QVIIVSHDE 854
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
4-56 |
4.41e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.91 E-value: 4.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002245190 4 VDKMLIKGIRSFdpenKNV-ITF--FKPLTLIVGPNGAGKTTIIECLKLSCTGELP 56
Cdd:COG3950 3 IKSLTIENFRGF----EDLeIDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLS 54
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
9-49 |
4.53e-05 |
|
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: 47.30 E-value: 4.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002245190 9 IKGIRSFDPENknvITFFKPLTLIVGPNGAGKTTIIECLKL 49
Cdd:COG3593 8 IKNFRSIKDLS---IELSDDLTVLVGENNSGKSSILEALRL 45
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
764-1295 |
4.74e-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: 48.04 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 764 EKNLKQLLADESEKAQTFDDFVSVLAQ---------VKMDKDAVQVLLQPVET--IDRHVQEIQQLGPQVENLEYKLDVR 832
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEepcplcgscIHPNPARQDIDNPGPLTrrMQRGEQTYAQLETSEEDVYHQLTSE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 833 GQGVKSL-EQIQLE----------LNSVQRTRDTLNNEVDDLRDqqrtLTDGLTNAQ-MRWHDIREEKLKASGAVHKFQK 900
Cdd:TIGR00618 555 RKQRASLkEQMQEIqqsfsiltqcDNRSKEDIPNLQNITVRLQD----LTEKLSEAEdMLACEQHALLRKLQPEQDLQDV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 901 AEEDlGHLAEEKEKLTLEEKHLEESLgPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNerikgYLN 980
Cdd:TIGR00618 631 RLHL-QQCSQELALKLTALHALQLTL-TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA-----QCQ 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 981 SKKGEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLKR-------NIDDNLNYRRTKDEV--ERLTHE 1051
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlkartEAHFNNNEEVTAALQtgAELSHL 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1052 IELLEDKI----LSIGSLSTIEADLKQH--SQEKDRLLSEYNRCQGTQSVYQSNISKHKL--ELKQTQYKDIEKRyfnql 1123
Cdd:TIGR00618 784 AAEIQFFNrlreEDTHLLKTLEAEIGQEipSDEDILNLQCETLVQEEEQFLSRLEEKSATlgEITHQLLKYEECS----- 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1124 lqlKTTEMANKDLDRYYAALDKALMRFHTMKMEEINKIIKELWQQTY----RGQDIDYISINSDSEGAGTRSYSYR---- 1195
Cdd:TIGR00618 859 ---KQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLyanvRLANQSEGRFHGRYADSHVNARKYQglal 935
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1196 VVMQTGDAELEMRGRCSAGQKVLASLIIRLALAETFCLNCGI----LALDEPTTNLDGPNAESLAGALLRIMESRKgqen 1271
Cdd:TIGR00618 936 LVADAYTGSVRPSATLSGGETFLASLSLALALADLLSTSGGTvldsLFIDEGFGSLDEDSLDRAIGILDAIREGSK---- 1011
|
570 580
....*....|....*....|....
gi 1002245190 1272 fQLIVITHDERFAQLIGQRQLAEK 1295
Cdd:TIGR00618 1012 -MIGIISHVPEFRERIPHRILVKK 1034
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1212-1279 |
6.68e-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: 44.68 E-value: 6.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMESRkgqenfQLIVITH 1279
Cdd:cd03228 98 SGGQRQ------RIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK------TVIVIAH 153
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-1058 |
7.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 407 NLNDDLQDKKKSNEAQKQFLwGRYLEVNTRYSEVVGQIESKVASKKGISRRMKDKESERDAAEMDLSKYNLPR--IDEKE 484
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKeeIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 485 RHL-QIEVERKALALGERNYDSIVNQKRTEIFSLDQKIK---TLQWEKDSIISDSNDRVLLDVKKDELEESKKKLKKIFD 560
Cdd:PRK03918 245 KELeSLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 561 EHKDKIRivfkgRTPSEKEVKKELSQAFGSVDREYNDLnSKSQEAAQELK--LVQMKILDAR------SHLSKLQKELDA 632
Cdd:PRK03918 325 GIEERIK-----ELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKakKEELERLKKRltgltpEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 633 KRSYVESKLQSITKMSADINMFPKHLKDAMDEREKqknnlsyAKGMrqmyepfenlarelhmCPCCQRAFTPDEEDEFVK 712
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGK----------------CPVCGRELTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 713 KQRTTCESTADRMNKISLECSNAEDFFQQLNKLNATYEEFVKLGK--EAIPLAEKNLKQLLADE-SEKAQTFDDFVSVLA 789
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 790 QVKMDkdavqvllqpVETIDRHVQEIQQLGPQVENLEYKLDVRGQGVKSLEQIQLELNSvqRTRDTLNNEVDDLRDqqrt 869
Cdd:PRK03918 536 KLKGE----------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF--ESVEELEERLKELEP---- 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 870 ltdgltnaqmrwhdIREEKLKASGAVHKFQKAEEDLGHLAEEKEKLtleekhlEESLGPLSKERESLLQEHEALKEKLDQ 949
Cdd:PRK03918 600 --------------FYNEYLELKDAEKELEREEKELKKLEEELDKA-------FEELAETEKRLEELRKELEELEKKYSE 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 950 E-YHQLAERKREFQQEIDALEthnerikgylnskkgEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQL 1028
Cdd:PRK03918 659 EeYEELREEYLELSRELAGLR---------------AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV 723
|
650 660 670
....*....|....*....|....*....|....*..
gi 1002245190 1029 KRNIDDNLNYR-----RTKDEVERLTHEI--ELLEDK 1058
Cdd:PRK03918 724 EELREKVKKYKallkeRALSKVGEIASEIfeELTEGK 760
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
831-1030 |
8.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 831 VRGQGVKSLEQIQLELNSVQRTRDTLN-NEVDDLRDQQRTLTDGLTnaqmRWHDIREEKLKASGAVHKFQKAEEDLGHLA 909
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 910 EEKEKLTLEEKHLEEsLGPLSKERESLLQEHEALKEKLdQEYHQLAERKREFQQEIDALETHNERIKGYLN-------SK 982
Cdd:COG4717 119 EKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSlateeelQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002245190 983 KGEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLKR 1030
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
9-49 |
1.25e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.08 E-value: 1.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1002245190 9 IKGIRSFdpenKNVITFFKPLTLIVGPNGAGKTTIIECLKL 49
Cdd:COG4637 7 IKNFKSL----RDLELPLGPLTVLIGANGSGKSNLLDALRF 43
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
922-1160 |
1.43e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 922 LEESLGPLSKER-ESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNERIK--GYLNSkkgeKLNELQEKHTQLQ 998
Cdd:PRK05771 72 LREEKKKVSVKSlEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDL----DLSLLLGFKYVSV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 999 SDLQKSKERKEEKSAELSKNKELLKSQDQLKRNIddNL-NYRRTKDEVERLTHEIELLEDKILSIGSLSTIeadLKQHSQ 1077
Cdd:PRK05771 148 FVGTVPEDKLEELKLESDVENVEYISTDKGYVYV--VVvVLKELSDEVEEELKKLGFERLELEEEGTPSEL---IREIKE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1078 EKDRLLSEYNRCQGTQSVYQSniSKHKLELKQTQYKDIEKRYFNQLLQLKTTEMA--------NKDLDRYYAALDKALMR 1149
Cdd:PRK05771 223 ELEEIEKERESLLEELKELAK--KYLEELLALYEYLEIELERAEALSKFLKTDKTfaiegwvpEDRVKKLKELIDKATGG 300
|
250
....*....|.
gi 1002245190 1150 FHTMKMEEINK 1160
Cdd:PRK05771 301 SAYVEFVEPDE 311
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
32-103 |
2.04e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 44.64 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 32 IVGPNGAGKTTIIECLklscTGELPPnsrsghtfvhdpkvageteTKGQIKLRfktaaGKDV-------VC----IRSFQ 100
Cdd:COG0411 35 LIGPNGAGKTTLFNLI----TGFYRP-------------------TSGRILFD-----GRDItglpphrIArlgiARTFQ 86
|
...
gi 1002245190 101 LTQ 103
Cdd:COG0411 87 NPR 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
837-1027 |
2.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 837 KSLEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVhkfQKAEEDLGHLAEEKEKLT 916
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 917 LEEKHLE---------------ESLGPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHneriKGYLNS 981
Cdd:COG3883 100 GSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1002245190 982 KKGEKLNELQekhtQLQSDLQKSKERKEEKSAELSKNKELLKSQDQ 1027
Cdd:COG3883 176 QQAEQEALLA----QLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-59 |
2.15e-04 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 44.72 E-value: 2.15e-04
10 20 30
....*....|....*....|....*....|.
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:COG4559 29 LTAIIGPNGAGKSTLLKLL----TGELTPSS 55
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
8-68 |
2.23e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.50 E-value: 2.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002245190 8 LIKGIRSFDpeNKNVITFFKPLTLIVGPNGAGKTTIIECLKLSCTGELPPNSRSGHTFVHD 68
Cdd:COG4694 7 KLKNVGAFK--DFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAG 65
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
29-120 |
2.42e-04 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 44.35 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPnsrsghtfvhdpkvageteTKGQIKLRfktaaGKDV-------VC----IR 97
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLI----SGFLRP-------------------TSGSVLFD-----GEDItglppheIArlgiGR 79
|
90 100
....*....|....*....|...
gi 1002245190 98 SFQLTQKASKMefkaieSVLQTI 120
Cdd:cd03219 80 TFQIPRLFPEL------TVLENV 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
985-1111 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 985 EKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDkilSIGS 1064
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDA---SSDD 686
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1002245190 1065 LSTIEADLKQHSQEKDRLLSEYNRCQGTQSVYQSNISKHKLELKQTQ 1111
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
770-1010 |
3.10e-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: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 770 LLADESEKaqtfDDFVSVLAQVKMDKDAVQVLLQPVETIDRHvQEIQQLGPQVENLEyklDVRGQGVKSLEQIQLELNSV 849
Cdd:TIGR02169 753 IENVKSEL----KELEARIEELEEDLHKLEEALNDLEARLSH-SRIPEIQAELSKLE---EEVSRIEARLREIEQKLNRL 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 850 QRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVHKFQKAEEDL----GHLAEEKEKLTLEEKHLEES 925
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlGDLKKERDELEAQLRELERK 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 926 LGPLSKERESLLQEHEALKEKL-----------------------DQEYHQLAERKREFQQEIDALETHNER-IKGYLNS 981
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLealeeelseiedpkgedeeipeeELSLEDVQAELQRVEEEIRALEPVNMLaIQEYEEV 984
|
250 260
....*....|....*....|....*....
gi 1002245190 982 KKgeKLNELQEKHTQLQSDLQKSKERKEE 1010
Cdd:TIGR02169 985 LK--RLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
922-1116 |
3.50e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 922 LEESLgplsKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKKgEKLNELQEKHTQLQSDL 1001
Cdd:pfam07888 36 LEECL----QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSR-EKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1002 QKSKERKEEKSAELSKNKELLK-----SQDQLKRNIDDNLNYRRTKDEVERLTHEI-ELLEDKILSIGSLSTIEADLKQH 1075
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIReleedIKTLTQRVLERETELERMKERAKKAGAQRkEEEAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002245190 1076 SQEKDRLLSEYNRCQGTQSVYQSNISKHKLELKQTQYKDIE 1116
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-357 |
3.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 188 KALEVIKKLH------KDQAQEIKTFRLKL------ENLQTLKDQAYRLRDNIAQDQEKSDALKIQMEELRTNVQGVEDK 255
Cdd:COG4913 252 ELLEPIRELAeryaaaRERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 256 IR----RTEKSL-ADLRRLQQEINSSTSARTTYftlqQQQYAALSEENEDTDDELKEWQTKFEERMALLQNKISKLERDV 330
Cdd:COG4913 332 IRgnggDRLEQLeREIERLERELEERERRRARL----EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL 407
|
170 180
....*....|....*....|....*..
gi 1002245190 331 DDenttssfLSKAINDLMRETGRLQAE 357
Cdd:COG4913 408 AE-------AEAALRDLRRELRELEAE 427
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
7-673 |
3.69e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 7 MLIKGIR--SFDPENKNVITFFKPLTLIVGPNGAGKTTIIECLKLSCTGElppnSRSGHTfvhdPKVAGETETKGQIKLR 84
Cdd:PRK01156 1 MIIKRIRlkNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTD----KRTEKI----EDMIKKGKNNLEVELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 85 FKTaaGKDVVCIRSfQLTQKASKMEFKAIESVLQTInphtgekvcLSYRCADMDREIPA-LMGVSKAILENVIFVHQDES 163
Cdd:PRK01156 73 FRI--GGHVYQIRR-SIERRGKGSRREAYIKKDGSI---------IAEGFDDTTKYIEKnILGISKDVFLNSIFVGQGEM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 164 NWPLQ-DPSTLKKKFDDIFSATRYTKALEVIKKLHKDQAQEIKTFRLKLENLQTLKDQAYRLRDNIAQDQEKSDALKIQM 242
Cdd:PRK01156 141 DSLISgDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 243 EELRTNVQGVEDKIRRTEKSLADLRRLQQEINSSTSARTTyftlQQQQYAALSEENEDTDDELKEWQTKFEERMALLQNK 322
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKT----AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 323 ISKLERDVDDENTTSSFLS------KAINDLMRETGRLQAEADAHMSVKHERDSairkifTKHNLGPIPDAPLTDAAAMH 396
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSnidaeiNKYHAIIKKLSVLQKDYNDYIKKKSRYDD------LNNQILELEGYEMDYNSYLK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 397 LTNITKAKLSNLNDDLQDKKKSNEAQKQFLWGRYLEVNTRYSEV---VGQIESKVASKKGISRRMKDKESE-RDAAEMdL 472
Cdd:PRK01156 371 SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEInvkLQDISSKVSSLNQRIRALRENLDElSRNMEM-L 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 473 SKYNLPRI------DEKERHLQIEVERKALALGERnydsiVNQKRTEIFSLDQKIKTLQWEKDSIISDSNDRV-----LL 541
Cdd:PRK01156 450 NGQSVCPVcgttlgEEKSNHIINHYNEKKSRLEEK-----IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSineynKI 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 542 DVKKDELEESKKKLKKIFDEH------KDKIRIVFKGRTPSEKEVKKELSQAFGSVDRE-----YNDLNSKSQEAAQELK 610
Cdd:PRK01156 525 ESARADLEDIKIKINELKDKHdkyeeiKNRYKSLKLEDLDSKRTSWLNALAVISLIDIEtnrsrSNEIKKQLNDLESRLQ 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002245190 611 LVQMKILDARSHLSKLQKELDAKRSYVESKLQSITKMSADINMFPKHLKD------AMDEREKQKNNLS 673
Cdd:PRK01156 605 EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNykkqiaEIDSIIPDLKEIT 673
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
9-54 |
3.95e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.84 E-value: 3.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1002245190 9 IKGIRSFdpENKNVITFFKPLTLIVGPNGAGKTTIIECLKLsCTGE 54
Cdd:cd03278 6 LKGFKSF--ADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRW-VLGE 48
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
593-1015 |
5.85e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 593 REYNDLNSKSQEAAQELKLVQMKILDARSHLSKLQKELDAKRSYVESKLQSITKMSADINMFPKHLKDAMDEREKQKNNL 672
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 673 SYAKGmrqmyepfENLARELHMcpccqraftpdEEDEFVKKQR-----TTCESTADRMNKISLECSNAEDFFQQL-NKLN 746
Cdd:pfam07888 121 LAQRA--------AHEARIREL-----------EEDIKTLTQRvlereTELERMKERAKKAGAQRKEEEAERKQLqAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 747 ATYEEFVKLGKEAiplaeKNLKQLLADESEKAQTFddfvsvlaqvkmdKDAVQVLLQPVETIDRHVQEIQQLGPQVENLE 826
Cdd:pfam07888 182 QTEEELRSLSKEF-----QELRNSLAQRDTQVLQL-------------QDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 827 YKLDVRGQGVKSLEQiqlELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWhdiREEKlkasgavhkfqkaeedlg 906
Cdd:pfam07888 244 ERLNASERKVEGLGE---ELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLAL---REGR------------------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 907 hlaeekekltleekhleeslGPLSKERESLLQEHEALKE---KLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKK 983
Cdd:pfam07888 300 --------------------ARWAQERETLQQSAEADKDrieKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQL 359
|
410 420 430
....*....|....*....|....*....|..
gi 1002245190 984 GEKLNELQEKHTQLQSdLQKSKERKEEKSAEL 1015
Cdd:pfam07888 360 SESRRELQELKASLRV-AQKEKEQLQAEKQEL 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
839-969 |
6.17e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 839 LEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAV----HKFQKAEEDLGH------- 907
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeveARIKKYEEQLGNvrnnkey 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002245190 908 --LAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALE 969
Cdd:COG1579 92 eaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
844-1108 |
7.46e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 844 LELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLE 923
Cdd:PRK01156 159 LEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 924 ESLGPLSkereSLLQEhealKEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLNSKKGEKLNELQEkHTQLQSDLQK 1003
Cdd:PRK01156 239 SALNELS----SLEDM----KNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIND-YFKYKNDIEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1004 SKERKEEKSAELSKNKELLKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDKILS-IGSLSTIEADLKQHSQEKDRL 1082
Cdd:PRK01156 310 KKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSyLKSIESLKKKIEEYSKNIERM 389
|
250 260
....*....|....*....|....*.
gi 1002245190 1083 LSEYNRCQGTQSVYQSNISKHKLELK 1108
Cdd:PRK01156 390 SAFISEILKIQEIDPDAIKKELNEIN 415
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1212-1279 |
8.79e-04 |
|
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: 8.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002245190 1212 SAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRiMESRKGqenfQLIVITH 1279
Cdd:cd03246 98 SGGQRQ------RLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA-LKAAGA----TRIVIAH 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-985 |
9.54e-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: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 188 KALEVIKKLHKDQAQEIKtfRLKLENLQTLKDQAYRLRDNIAQDQEKSDALKIQMEELRTNVQGVEDKIRRTEKSLADLR 267
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 268 RLQQEINSSTSARTTYFTLQQQQYAALSEENEDTDDELKEWQTKF---EERMALLQNKISKLERDVDDENTTSSFLSKAI 344
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 345 NDLMRETGRLQAEADAHMSVKHERDSAIRKIftkhnlgpipdapltdaaamhltnitKAKLSNLNDDLQDKKKSNEAQKQ 424
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQ--------------------------EWKLEQLAADLSKYEQELYDLKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 425 flwgRYLEVNTRYSEVVGQIESKVASKKGISRRmkdkESERDAAEMDLSKYN---------LPRIDEK----------ER 485
Cdd:TIGR02169 477 ----EYDRVEKELSKLQRELAEAEAQARASEER----VRGGRAVEEVLKASIqgvhgtvaqLGSVGERyataievaagNR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 486 HLQIEVERKALALGERNYDSIVNQKRTEIFSLDqKIKTLQWE-----KDSIISDSNDRVLLDVKKDELEESKKKLKKIFD 560
Cdd:TIGR02169 549 LNNVVVEDDAVAKEAIELLKRRKAGRATFLPLN-KMRDERRDlsilsEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 561 ------EHKDKIRIVfkgrTPSEKEVKKELSQAFGSVDREYNDLNSKSQEAaqELKLVQMKILDARSHLSKLQKELDAKR 634
Cdd:TIGR02169 628 dieaarRLMGKYRMV----TLEGELFEKSGAMTGGSRAPRGGILFSRSEPA--ELQRLRERLEGLKRELSSLQSELRRIE 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 635 SYVESKLQSITKMSADINMFPKHLKDAMDEREKQKnnlsyakgmrqmyEPFENLARELHMCpccqraftpDEEDEFVKKQ 714
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK-------------ERLEELEEDLSSL---------EQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 715 RTTCESTADRM----NKI-----SLECSNAEDFFQQLNKLNATYEEFVKLGKEAIPLAEKNLKQLLAD----ESEKAQTF 781
Cdd:TIGR02169 760 LKELEARIEELeedlHKLeealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkeylEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 782 DDFVSVLAQVKMDKDAVQVLLQPVETIDRHVQEIQ----QLGPQVENLEykldvrgqgvKSLEQIQLELNSVQRTRDTLN 857
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrDLESRLGDLK----------KERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 858 NEVDDLRDQQRTLTDGLTNAQMRWHDIR----------EEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHLEESLG 927
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002245190 928 PLSKERESLLQEHEALKEKLDqeyhQLAERKRE-FQQEIDALETHNERIKGYLNSKKGE 985
Cdd:TIGR02169 990 ELKEKRAKLEEERKAILERIE----EYEKKKREvFMEAFEAINENFNEIFAELSGGTGE 1044
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
766-993 |
9.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 766 NLKQLLADESEKAQTFDDfvsvLAQVKMDKDAVQVLLQPVETIDRHVQEIQQLGPQ---VENLEYKLDVRGQGVKSLEQI 842
Cdd:COG4913 608 NRAKLAALEAELAELEEE----LAEAEERLEALEAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 843 QLELNSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIREEKLKASGAVHKFQKAEEDLGHLAEEKEKLTLEEKHL 922
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 923 EESLgplskeRESLLQEHEALKEKLDQEYHQLAERKREFQQ--------------------------EIDALETHNERIK 976
Cdd:COG4913 764 EREL------RENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleslpeylalldrlEEDGLPEYEERFK 837
|
250
....*....|....*..
gi 1002245190 977 GYLNSKKGEKLNELQEK 993
Cdd:COG4913 838 ELLNENSIEFVADLLSK 854
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-59 |
1.01e-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: 42.11 E-value: 1.01e-03
10 20
....*....|....*....|....*...
gi 1002245190 32 IVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:cd03263 33 LLGHNGAGKTTTLKML----TGELRPTS 56
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
802-1130 |
1.06e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 802 LQPVETIDRHvQEIQQLGPQVENL--EYKLDVRGQGVKSLEQIQLELNSVQRTRDTlnNEvddlRDQQRTLTdgltnaQM 879
Cdd:pfam17380 230 LAPYEKMERR-KESFNLAEDVTTMtpEYTVRYNGQTMTENEFLNQLLHIVQHQKAV--SE----RQQQEKFE------KM 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 880 RWHDIREEKLKASGAVHKFQKAEEdlGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLD----QEYHQLA 955
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEE--AEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELErirqEEIAMEI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 956 ERKREFQQEIDALETHNERIKGYLNSKKGEKLNELQEKHTQLQSDLQKSKERKEEKSA--------ELSKNKEL------ 1021
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArqrevrrlEEERAREMervrle 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1022 -LKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDKILSIgslstIEADLKQHSQ-----EKDRLLSEYNRCQGTQSV 1095
Cdd:pfam17380 455 eQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-----LEKELEERKQamieeERKRKLLEKEMEERQKAI 529
|
330 340 350
....*....|....*....|....*....|....*
gi 1002245190 1096 YQSNISKHKLELKQTQYKDIEKRYFNQLLQLKTTE 1130
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
29-59 |
1.16e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 42.45 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|.
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:PRK13548 30 VVAILGPNGAGKSTLLRAL----SGELSPDS 56
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1237-1286 |
1.78e-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: 41.32 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1237 ILAlDEPTTNLDGPNAEslagALLRIMESRKGQENFQLIVITHDERFAQL 1286
Cdd:cd03255 162 ILA-DEPTGNLDSETGK----EVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1237-1285 |
2.09e-03 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 41.18 E-value: 2.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1002245190 1237 ILAlDEPTTNLDGPNAEslagALLRIMESRKGQENFQLIVITHDERFAQ 1285
Cdd:COG1136 166 ILA-DEPTGNLDSKTGE----EVLELLRELNRELGTTIVMVTHDPELAA 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1202-1279 |
2.41e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.07 E-value: 2.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002245190 1202 DAELEMRG-RCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMESRkgqenfQLIVITH 1279
Cdd:COG1132 467 DTVVGERGvNLSGGQRQ------RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR------TTIVIAH 533
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
794-1129 |
2.74e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 794 DKDAVQVL---LQPVETIDRHVQEIQQLGPQVENLEYKL--------------------DVRGQGVKSLE----QIQLEL 846
Cdd:PRK11281 58 DKLVQQDLeqtLALLDKIDRQKEETEQLKQQLAQAPAKLrqaqaelealkddndeetreTLSTLSLRQLEsrlaQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 847 NSVQRTRDTLNNEVDDLRDQQRTLTDGLTNAQMRWHDIReeKLKASGAVHKFQKAEEDLGHLAEEKEkltleekhleeSL 926
Cdd:PRK11281 138 QNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR--NLLKGGKVGGKALRPSQRVLLQAEQA-----------LL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 927 GPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALEThnerikgYLNSKkgeKLNELQEKHTQLQSdlQKSKE 1006
Cdd:PRK11281 205 NAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQE-------AINSK---RLTLSEKTVQEAQS--QDEAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1007 RKEEKS---AELSKNKE----LLKSQDQLKRNIDDNLnyrRTKDEVERLTHEIELLEDKI--------LS---------- 1061
Cdd:PRK11281 273 RIQANPlvaQELEINLQlsqrLLKATEKLNTLTQQNL---RVKNWLDRLTQSERNIKEQIsvlkgsllLSrilyqqqqal 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 1062 -----IGSLSTIEADLKQH----SQEKDRLlseynrcqgtqsvYQSNISKHKLELKQTQYKDIEKRyfNQLLQLKTT 1129
Cdd:PRK11281 350 psadlIEGLADRIADLRLEqfeiNQQRDAL-------------FQPDAYIDKLEAGHKSEVTDEVR--DALLQLLDE 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
897-1085 |
2.77e-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: 42.36 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 897 KFQKAEEDLGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLDQEYHQLAERKRefqqeidALETHNERIK 976
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE-------ALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 977 GYLNSKKGEklnelQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLkrniddnlnyrRTKDEVERLTHEIELLE 1056
Cdd:TIGR02169 244 RQLASLEEE-----LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL-----------RVKEKIGELEAEIASLE 307
|
170 180 190
....*....|....*....|....*....|
gi 1002245190 1057 DKI-LSIGSLSTIEADLKQHSQEKDRLLSE 1085
Cdd:TIGR02169 308 RSIaEKERELEDAEERLAKLEAEIDKLLAE 337
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
32-57 |
2.85e-03 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 40.84 E-value: 2.85e-03
10 20
....*....|....*....|....*.
gi 1002245190 32 IVGPNGAGKTTIiecLKLsCTGELPP 57
Cdd:COG1119 34 ILGPNGAGKSTL---LSL-ITGDLPP 55
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
963-1088 |
2.94e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 963 QEIDALETHNERIKGYLNskkgEKLNELQEKHTQLQSDLQKSKERKEEKSAELSKNKELLKSQDQLKRNIDDNLNYRRTK 1042
Cdd:COG1579 13 QELDSELDRLEHRLKELP----AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1002245190 1043 DEVERLTHEIE-------LLEDKILSI-GSLSTIEADLKQHSQEKDRLLSEYNR 1088
Cdd:COG1579 89 KEYEALQKEIEslkrrisDLEDEILELmERIEELEEELAELEAELAELEAELEE 142
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
6-78 |
3.05e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.72 E-value: 3.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 6 KMLIKGIRSFdpENKNVITF----FKPLTLIVGPNGAGKTTIIECLKLSCTGELPPNSRSGHTfvHDPKVAGETETK 78
Cdd:cd03279 5 KLELKNFGPF--REEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENL--RSVFAPGEDTAE 77
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
29-59 |
3.12e-03 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 40.84 E-value: 3.12e-03
10 20 30
....*....|....*....|....*....|.
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:COG1121 34 FVAIVGPNGAGKSTLLKAI----LGLLPPTS 60
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
188-332 |
3.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 188 KALEVIKKLHKDQAQEIKTFRLKLENLQTLKDQAYRLRDNIAQDQEKSDALKiQMEELRTNVQGVEDKIRRTEKSLADLR 267
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002245190 268 RLQQEINsstSARTTYFTLQQQQYAALSEENEDTDDELKEWQTKFEE---RMALLQNKISKLERDVDD 332
Cdd:COG4717 160 ELEEELE---ELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEE 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1224-1290 |
3.35e-03 |
|
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: 40.57 E-value: 3.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 1224 RLALAETFCLNCGILALDEPTTNLDgpnaESLAGALLRIMESRKGQENFQLIVITHDERFAQLIGQR 1290
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALD----VSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADR 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-68 |
3.36e-03 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 40.43 E-value: 3.36e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1002245190 32 IVGPNGAGKTTIIECLklscTGELPPNSRSGHTFVHD 68
Cdd:cd03265 31 LLGPNGAGKTTTIKML----TTLLKPTSGRATVAGHD 63
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1224-1290 |
3.48e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.53 E-value: 3.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 1224 RLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLrimeSRKGQENFQLIVITHDERFAQLIGQR 1290
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF----SLNREHGTTLILVTHDLQLAARCDRR 216
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-380 |
4.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 181 FSATRytkALEVIKKLHKDQAQEIKTFRLKLENLQTLKDQAYRLRDNIAQDQEKSDALkIQMEELRTNVQGVEDKIRRTE 260
Cdd:COG4913 606 FDNRA---KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 261 KSLADLRRLQQEINSstsarttyftlQQQQYAALSEENEDTDDELKEWQTKFEERMALLQNKISKLERDVDDENTTSSFL 340
Cdd:COG4913 682 ASSDDLAALEEQLEE-----------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002245190 341 ----------SKAINDLMRETGRLQAEADAHMSVKHERdsaIRKIFTKHN 380
Cdd:COG4913 751 leerfaaalgDAVERELRENLEERIDALRARLNRAEEE---LERAMRAFN 797
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
29-59 |
4.28e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.21 E-value: 4.28e-03
10 20 30
....*....|....*....|....*....|.
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:cd03235 27 FLAIVGPNGAGKSTLLKAI----LGLLKPTS 53
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-59 |
4.35e-03 |
|
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: 39.15 E-value: 4.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1002245190 20 KNVITFFKP--LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:cd00267 16 DNVSLTLKAgeIVALVGPNGSGKSTLLRAI----AGLLKPTS 53
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
779-1122 |
4.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 779 QTFDDFVSVLAQVKMDKD---AVQVLLQPVETIDRHVQEI----QQLGPQVENLEykldvrgQGVKSLEQIQLELNSVQR 851
Cdd:PRK04863 817 QAFSRFIGSHLAVAFEADpeaELRQLNRRRVELERALADHesqeQQQRSQLEQAK-------EGLSALNRLLPRLNLLAD 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 852 trDTLNNEVDDLRDQqrtltdgltnaqmrwhdiREEKLKASGAVHKFQKAEEDLGHLAeekekltleekhleeslgplsk 931
Cdd:PRK04863 890 --ETLADRVEEIREQ------------------LDEAEEAKRFVQQHGNALAQLEPIV---------------------- 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 932 ereSLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNERIK--GYLNSK----KGEKLNE-LQEKHTQLQSDLQKS 1004
Cdd:PRK04863 928 ---SVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAemlaKNSDLNEkLRQRLEQAEQERTRA 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1005 KERKEEKSAELSKNKELLKSQDQlkrniddnlNYRRTKDEVERLTHEIElledkilSIGSLSTIEADlKQHSQEKDRLLS 1084
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASLKS---------SYDAKRQMLQELKQELQ-------DLGVPADSGAE-ERARARRDELHA 1067
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1002245190 1085 EYNRCQGTQSVYQSNISKHKLELK--QTQYKDIEKRYFNQ 1122
Cdd:PRK04863 1068 RLSANRSRRNQLEKQLTFCEAEMDnlTKKLRKLERDYHEM 1107
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1224-1290 |
4.46e-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: 40.18 E-value: 4.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002245190 1224 RLALAETFCLNCGILALDEPTTNLDgPNAeslAGALLRIMESRKGQENFQLIVITHDERFAQLIGQR 1290
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLD-PIA---SGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADR 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1206-1281 |
4.68e-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: 41.19 E-value: 4.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002245190 1206 EMRGRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALLRIMESRKgqenfqLIVITHDE 1281
Cdd:TIGR02868 467 EGGARLSGGERQ------RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRT------VVLITHHL 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-64 |
4.82e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.20 E-value: 4.82e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1002245190 32 IVGPNGAGKTTIIECLklscTGELPPNS---RSGHT 64
Cdd:COG0488 346 LIGPNGAGKSTLLKLL----AGELEPDSgtvKLGET 377
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
29-59 |
5.08e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 40.41 E-value: 5.08e-03
10 20 30
....*....|....*....|....*....|.
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:COG1120 29 VTALLGPNGSGKSTLLRAL----AGLLKPSS 55
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1209-1293 |
5.11e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.20 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1209 GRCSAGQKVlasliiRLALAETFCLNCGILALDEPTTNLDGPNAESLAGALlrimesrkgqENFQ--LIVITHDERFAQL 1286
Cdd:COG0488 431 GVLSGGEKA------RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----------DDFPgtVLLVSHDRYFLDR 494
|
....*..
gi 1002245190 1287 IGQRQLA 1293
Cdd:COG0488 495 VATRILE 501
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
238-483 |
5.31e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 238 LKIQMEELRTNVQGVEDKIRRTEKSLADLRRLQQEINSSTSARTTyftlqqqqyaalseENEDTDDELKEWQTKFEERMA 317
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA--------------RKQNKYDELVEEAKTIKAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 318 LLQNKISKLERDVDDenttssfLSKAINDLMRETGRLQAeadahmsvKHERDSAIRKIFTKHNLGPIPDAPLTDAAAM-- 395
Cdd:PHA02562 238 ELTDELLNLVMDIED-------PSAALNKLNTAAAKIKS--------KIEQFQKVIKMYEKGGVCPTCTQQISEGPDRit 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 396 ----HLTNITKaKLSNLNDDLQD-KKKSNEAQKQFLwgRYLEVNTRYSEVVGQIESKVASKKGISRRMKDKESER--DAA 468
Cdd:PHA02562 303 kikdKLKELQH-SLEKLDTAIDElEEIMDEFNEQSK--KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdNAE 379
|
250
....*....|....*
gi 1002245190 469 EMDLSKYNLPRIDEK 483
Cdd:PHA02562 380 ELAKLQDELDKIVKT 394
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
941-1151 |
5.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 941 EALKEKLDQEYHQLAERKREFQQEIDALEthnerikgylnskkgEKLNELQEKHT---QLQSDLQKSKERKEEKSAELSK 1017
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELE---------------EELKEAEEKEEeyaELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1018 NKELLKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDKILSIGSLSTIEADLKQHSQEKDRLLSEYNRcqgtqsvYQ 1097
Cdd:COG4717 114 LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE-------QL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002245190 1098 SNISKHKLELKQTQYKDIEKRYFNQLLQLKTTEMANKDLDRYYAALDKALMRFH 1151
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
821-996 |
5.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 821 QVENLEYKLDVRGQGVKSLEQIQLELNSVQRTRDTLNNEVDDLRDQQRTLTDgLTNAQMRWHDIREEKLKASGAVHKFQK 900
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 901 AEEDLGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLDQEYHQLAERKREFQQEIDALETHNERIKGYLN 980
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|....*.
gi 1002245190 981 SKKGEKLNELQEKHTQ 996
Cdd:COG4717 231 QLENELEAAALEERLK 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-375 |
6.25e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 190 LEVIKKLHKDQAQEIKTFRLKLENLQTLKDQayrLRDNIAQDQEKSDALKIQMEELRTNVQGVEDKIRRTEKSLADLRRL 269
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEE---LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 270 QQEINSSTSARTTYFTLQQQQYAALSEENEDTDDELKEWQTKFEERMALLQNKISKLERDVDDENTTSSFLSKAINDLMR 349
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180
....*....|....*....|....*.
gi 1002245190 350 ETGRLQAEADAHMSVKHERDSAIRKI 375
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEEL 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
731-1291 |
6.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 731 ECSNAEDFFQQLNKLNATYEEFVKLGKEAIPLAEKnLKQLLADESEKAQTFDDFVSVLAQVKMDKDAVQVLLQPVETIDR 810
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQELEALEAELAELPER-LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 811 hvQEIQQLGPQVENLEYKLDvrgQGVKSLEQIQLELNSVQRTRDTLNNEVDDLRDQQRT--------LTDGLTNAQMRWH 882
Cdd:COG4717 192 --EELQDLAEELEELQQRLA---ELEEELEEAQEELEELEEELEQLENELEAAALEERLkearllllIAAALLALLGLGG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 883 DIREEKLKASGAV------------------HKFQKAEEDLGHLAEEKEKLTLEEKHLEESLGPLSKERESLLQEHEALK 944
Cdd:COG4717 267 SLLSLILTIAGVLflvlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 945 EKLDQEYHQLAERKREFQqeidaLETHNERIKGYLNSKKGEKLNELQEKHTQlqsdlqksKERKEEKSAELSKNKELLKS 1024
Cdd:COG4717 347 EELQELLREAEELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQ--------AEEYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1025 QDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDKILSI-GSLSTIEADLKQHsqEKDRLLSEynrcqgtqsvyqsniSKH 1103
Cdd:COG4717 414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELrEELAELEAELEQL--EEDGELAE---------------LLQ 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1104 KLELKQTQYKDIEKRYfnqllqlKTTEMAnkdldryYAALDKALMRFHTMK----MEEINKIIKELWQQTYRGQDIDyis 1179
Cdd:COG4717 477 ELEELKAELRELAEEW-------AALKLA-------LELLEEAREEYREERlppvLERASEYFSRLTDGRYRLIRID--- 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 1180 insdsegagtRSYSYRVVMQTGD----AELemrgrcSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDGPNAESL 1255
Cdd:COG4717 540 ----------EDLSLKVDTEDGRtrpvEEL------SRGTREQLYLALRLALAELLAGEPLPLILDDAFVNFDDERLRAA 603
|
570 580 590
....*....|....*....|....*....|....*.
gi 1002245190 1256 AGALLRIMESRkgqenfQLIVITHDERFAQLIGQRQ 1291
Cdd:COG4717 604 LELLAELAKGR------QVIYFTCHEELVELFQEEG 633
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
921-1059 |
7.78e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 921 HLEESLGPLSKERESLLQEHEALKEKLDqeyhQLAERKREFQQEIDALETHNERIKGYLNSKKGEK--------LNELQE 992
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeIESLKR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002245190 993 KHTQLQSDLQKSKERKEEKSAELSKNKELLKSQ----DQLKRNIDDNLNyrRTKDEVERLTHEIELLEDKI 1059
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELAELeaelEEKKAELDEELA--ELEAELEELEAEREELAAKI 172
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-49 |
8.67e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 8.67e-03
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
29-59 |
8.86e-03 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 38.57 E-value: 8.86e-03
10 20 30
....*....|....*....|....*....|.
gi 1002245190 29 LTLIVGPNGAGKTTIIECLklscTGELPPNS 59
Cdd:cd03214 27 IVGILGPNGAGKSTLLKTL----AGLLKPSS 53
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
794-1058 |
9.80e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 794 DKDAVQVLLQPVETIDRHVQEIQQ-LGPQVENLEYKLDVRGQGVKSLEQIQLELNSVQRTR----DTLNNEVDDLRDQQR 868
Cdd:PLN02939 94 DDDHNRASMQRDEAIAAIDNEQQTnSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQAledlEKILTEKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 869 TLTDGLTNAQMRWHDIREEKLKASGAVHKFQKAEEDLGHlaeEKEKLTLEEKHLEESLGPLSKERESLLQEHEALKEKLD 948
Cdd:PLN02939 174 ILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLI---RGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002245190 949 qEYHQLAERKREFQQEIDALETHNERIKGYLNSKKGE--KLNELQ-----EKHTQLQSDLQKSKERKEEKSAELSKNKEL 1021
Cdd:PLN02939 251 -EVAETEERVFKLEKERSLLDASLRELESKFIVAQEDvsKLSPLQydcwwEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
250 260 270
....*....|....*....|....*....|....*..
gi 1002245190 1022 LKSQDQLKRNIDDNLNYRRTKDEVERLTHEIELLEDK 1058
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEER 366
|
|
| |
