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Conserved domains on  [gi|487878312|ref|WP_001951778|]
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hypothetical protein [Helicobacter pylori]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
382-666 2.80e-07

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 382 KSSGKLKELERQITKGIEKFDEQIacwqekTKLEEQLKESEKIRKKYQ--RIINTFTDKnYLDKKDKLQKTREELIDLRQ 459
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEI------EELEEKVKELKELKEKAEeyIKLSEFYEE-YLDELREIEKRLSRLEEEIN 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 460 SKEGFLTFIKELKRVVNFESKENMEEKNSYD------KVYNQLKQdICKELEQIDINIKNGCFKSDEEKIEKLESEHQTL 533
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKA-KKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 534 LQEIGEFLKEKGVSDENIGDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNKINLAFK 613
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487878312 614 EISKNHKEEVRLITikyylNEDIFEGVFEDFDKLvdKGFNIQKHQSKIKEYLK 666
Cdd:PRK03918 484 ELEKVLKKESELIK-----LKELAEQLKELEEKL--KKYNLEELEKKAEEYEK 529
YbjD super family cl34639
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 660-840 9.78e-07

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG3593:

Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 51.93  E-value: 9.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 660 KIKEYLKGIELKDIIDVQCTEFIEKLDSLIENKKAAFyETMMDVFNR---EIHFQIYRLLILKHLRNVEKYKIFEVRYD- 735
Cdd:COG3593   76 TFGSLLSRLLRLLLKEEDKEELEEALEELNEELKEAL-KALNELLSEylkELLDGLDLELELSLDELEDLLKSLSLRIEd 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 736 --KRALNETSFGQRCTAVLVVLLSL------GNNPII-IDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLN 806
Cdd:COG3593  155 gkELPLDRLGSGFQRLILLALLSALaelkraPANPILlIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSE 234

                        170       180       190
                 ....*....|....*....|....*....|....
gi 487878312 807 ADAELIIQLKNENNKIIAQSFTIESDGYRDDLLK 840
Cdd:COG3593  235 VPLENIRRLRRDSGGTTSTKLIDLDDEDLRKLLR 268
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 294-400 3.25e-04

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd03277:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 213  Bit Score: 42.97  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 294 TLFFSPYFTCVIGGRGSGKSTLL-----------QLIASAIKNKSFVK-GLRLETIQKSLKIQS-DIDIADSVEYLAQNE 360
Cdd:cd03277   18 EFRPGPSLNMIIGPNGSGKSSIVcaiclglggkpKLLGRAKKVGEFVKrGCDEGTIEIELYGNPgNIQVDNLCQFLPQDR 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 487878312 361 VEEFATNVS-----KFteaifnridsKSSGKLKELERQITKGIEK 400
Cdd:cd03277   98 VGEFAKLSPiellvKF----------REGEQLQELDPHHQSGGER 132
 
Name Accession Description Interval E-value
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
382-666 2.80e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 382 KSSGKLKELERQITKGIEKFDEQIacwqekTKLEEQLKESEKIRKKYQ--RIINTFTDKnYLDKKDKLQKTREELIDLRQ 459
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEI------EELEEKVKELKELKEKAEeyIKLSEFYEE-YLDELREIEKRLSRLEEEIN 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 460 SKEGFLTFIKELKRVVNFESKENMEEKNSYD------KVYNQLKQdICKELEQIDINIKNGCFKSDEEKIEKLESEHQTL 533
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKA-KKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 534 LQEIGEFLKEKGVSDENIGDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNKINLAFK 613
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487878312 614 EISKNHKEEVRLITikyylNEDIFEGVFEDFDKLvdKGFNIQKHQSKIKEYLK 666
Cdd:PRK03918 484 ELEKVLKKESELIK-----LKELAEQLKELEEKL--KKYNLEELEKKAEEYEK 529
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 660-840 9.78e-07

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: 51.93  E-value: 9.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 660 KIKEYLKGIELKDIIDVQCTEFIEKLDSLIENKKAAFyETMMDVFNR---EIHFQIYRLLILKHLRNVEKYKIFEVRYD- 735
Cdd:COG3593   76 TFGSLLSRLLRLLLKEEDKEELEEALEELNEELKEAL-KALNELLSEylkELLDGLDLELELSLDELEDLLKSLSLRIEd 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 736 --KRALNETSFGQRCTAVLVVLLSL------GNNPII-IDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLN 806
Cdd:COG3593  155 gkELPLDRLGSGFQRLILLALLSALaelkraPANPILlIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSE 234

                        170       180       190
                 ....*....|....*....|....*....|....
gi 487878312 807 ADAELIIQLKNENNKIIAQSFTIESDGYRDDLLK 840
Cdd:COG3593  235 VPLENIRRLRRDSGGTTSTKLIDLDDEDLRKLLR 268
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 743-813 7.39e-06

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: 46.85  E-value: 7.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487878312 743 SFGQRCTAVLVVLLSLgnNP--IIIDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLNADAELII 813
Cdd:cd00267   82 SGGQRQRVALARALLL--NPdlLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 373-809 9.43e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.58  E-value: 9.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   373 EAIFNRIDSKSSGKLKELERQITKGIEKFDE--QIACWQEKTKLEEQLKESEKIRKKYQRIINTFTDKNYLDKKDKLQKT 450
Cdd:pfam02463  724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   451 REELIDLRQSKEGFLTFIKELKRVVNFESKENMEEKNSYDKVYNQLKQDICKELEQIDINIKNGCF-KSDEEKIEKLESE 529
Cdd:pfam02463  804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLqELLLKEEELEEQK 883

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   530 HQTLLQEIGEFLKEKGVSDENIGDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNKIN 609
Cdd:pfam02463  884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   610 LAFKEISKNHKEEVRLITIKYYLNEDiFEGVFEDFDKLVDKGFNIQKHQSKIKEYLKGIELKDIIDVQCTEFIEKLDSLI 689
Cdd:pfam02463  964 RLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLEL 1042

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   690 ENKKAAFYETMMDVFNREIHFqiyrllilkHLRNVEKykifevryDKRALNETSFGQRCTAVLVVLLSL-GNNPI---II 765
Cdd:pfam02463 1043 GGSAELRLEDPDDPFSGGIEI---------SARPPGK--------GVKNLDLLSGGEKTLVALALIFAIqKYKPApfyLL 1105

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 487878312   766 DEPEAHLDSALIAKyLVALIKERKQERQIIFATHNANFVLNADA 809
Cdd:pfam02463 1106 DEIDAALDDQNVSR-VANLLKELSKNAQFIVISLREEMLEKADK 1148
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 574-804 1.08e-05

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: 48.15  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  574 EIKEIANKIESFSY-EDMDKNIEKFKNQINE---ELNKINLAFKEISKNHKEEVRLITIKYYLNEDIFEGVFEDFDKLVD 649
Cdd:pfam13304  41 GIGGIPSLLNGIDPkEPIEFEISEFLEDGVRyryGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  650 KGFNIQKHQSKIKEYLKGIELKDIIDVQCT--EFIEKLDSLIENKKAAFY---ETMMDVFNREIHFQIYRLLILKHL--- 721
Cdd:pfam13304 121 GLDVEERIELSLSELSDLISGLLLLSIISPlsFLLLLDEGLLLEDWAVLDlaaDLALFPDLKELLQRLVRGLKLADLnls 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  722 --------------RNVEKYKIFEVRYDKRALNETSFG---QRCTAVLVVLLSLGNNP--IIIDEPEAHLDSALIAKYLV 782
Cdd:pfam13304 201 dlgegieksllvddRLRERGLILLENGGGGELPAFELSdgtKRLLALLAALLSALPKGglLLIDEPESGLHPKLLRRLLE 280

                         250       260
                  ....*....|....*....|..
gi 487878312  783 ALIKERKQERQIIFATHNANFV 804
Cdd:pfam13304 281 LLKELSRNGAQLILTTHSPLLL 302
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
287-842 3.24e-05

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 47.81  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 287 CYAGFNETLFFSPYfTCVIGGRGSGKSTLLQLIAS-AIKNKSFVKGLRLETIQKSLKIQSDIDIADSvEYLAQNeveeFA 365
Cdd:COG4694   13 AFKDFGWLAFFKKL-NLIYGENGSGKSTLSRILRSlELGDTSSEVIAEFEIEAGGSAPNPSVRVFNR-DFVEEN----LR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 366 TNVSKFTEAIFNRIDSKSSGKLKELERQITKGIEKFDEQIA-CWQEKTKLEEQLKESEKIRKKYQRIINTFTDKNYldKK 444
Cdd:COG4694   87 SGEEIKGIFTLGEENIELEEEIEELEKEIEDLKKELDKLEKeLKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNY--RK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 445 DKLQKTREEL-----IDLRQSKEGFltFIKELKRVVNFESKENMeeKNSYDKVYNQLKQDIC-KELEQIDINIKNgcfKS 518
Cdd:COG4694  165 ANLEKKLSALkssseDELKEKLKLL--KEEEPEPIAPITPLPDL--KALLSEAETLLEKSAVsSAIEELAALIQN---PG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 519 DEEKIEKLESEHQTLLQEIGEFLkEKGVSDENIGDIRNA-NYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKF 597
Cdd:COG4694  238 NSDWVEQGLAYHKEEEDDTCPFC-QQELAAERIEALEAYfDDEYEKLLAALKDLLEELESAINALSALLLEILRTLLPSA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 598 KNQINEELNKINLAFKE----ISKNHKEEVRLITIKYYLNEDIFEGVFEDFDKLVDKgFN--IQKHQSKIKEYLKGI--- 668
Cdd:COG4694  317 KEDLKAALEALNALLETllaaLEEKIANPSTSIDLDDQELLDELNDLIAALNALIEE-HNakIANLKAEKEEARKKLeah 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 669 ---ELKDIID----------------VQCTEFIEKLDSLIENKKAAFYET--MMDVFNREIH---FQIYRLLILKHlrNV 724
Cdd:COG4694  396 elaELKEDLSrykaeveelieelktiKALKKALEDLKTEISELEAELSSVdeAADEINEELKalgFDEFSLEAVED--GR 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 725 EKYKIFEVRYDKRALNET-SFG-QRCTAVLVVLLSL-------GNNPIIIDEPEAHLDSalIAKYLVA--LIKERKQERQ 793
Cdd:COG4694  474 SSYRLKRNGENDAKPAKTlSEGeKTAIALAYFLAELegdendlKKKIVVIDDPVSSLDS--NHRFAVAslLKELSKKAKQ 551

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 487878312 794 IIFATHNANFVLnadaELIIQLKNENNKIIAQSFTIESDGYRDDLLKLE 842
Cdd:COG4694  552 VIVLTHNLYFLK----ELRDLADEDNKKKNCAFYEIRKDNRGSKIIKLD 596
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 388-672 5.62e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.35  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   388 KELERQITKGIEKFDEQIACWQE-----KTKLEEQLKESEKIRK-------KYQRII--NTFTDKNYLDKKDKLQKTREE 453
Cdd:TIGR01612  536 AKLYKEIEAGLKESYELAKNWKKliheiKKELEEENEDSIHLEKeikdlfdKYLEIDdeIIYINKLKLELKEKIKNISDK 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   454 ------LIDLRQSKEGFLTFIKELKRVVNFESKENMEEKnsyDKVYNQLKQDICKeLEQIDINIKNGCFKSDEEKIEKLE 527
Cdd:TIGR01612  616 neyikkAIDLKKIIENNNAYIDELAKISPYQVPEHLKNK---DKIYSTIKSELSK-IYEDDIDALYNELSSIVKENAIDN 691

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   528 SEHQTLLQEIGEFLKEKGVSDENIgDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNK 607
Cdd:TIGR01612  692 TEDKAKLDDLKSKIDKEYDKIQNM-ETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNK 770

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487878312   608 INLAFKEISKNHKEEVRLITIKYYLNEDIfegvfeDFDKLVDKgfNIQKHQSKIKEYLKGIELKD 672
Cdd:TIGR01612  771 INDYAKEKDELNKYKSKISEIKNHYNDQI------NIDNIKDE--DAKQNYDKSKEYIKTISIKE 827
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 294-400 3.25e-04

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (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: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 42.97  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 294 TLFFSPYFTCVIGGRGSGKSTLL-----------QLIASAIKNKSFVK-GLRLETIQKSLKIQS-DIDIADSVEYLAQNE 360
Cdd:cd03277   18 EFRPGPSLNMIIGPNGSGKSSIVcaiclglggkpKLLGRAKKVGEFVKrGCDEGTIEIELYGNPgNIQVDNLCQFLPQDR 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 487878312 361 VEEFATNVS-----KFteaifnridsKSSGKLKELERQITKGIEK 400
Cdd:cd03277   98 VGEFAKLSPiellvKF----------REGEQLQELDPHHQSGGER 132
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
733-813 1.80e-03

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 40.29  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 733 RYDKRALNETSFGQRCTAVLVVLLSLGNNPIIIDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLNADAELI 812
Cdd:NF040873 111 DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190


                 .
gi 487878312 813 I 813
Cdd:NF040873 191 L 191
AAA_23 pfam13476
AAA domain;
292-459 5.61e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 39.02  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  292 NETLFFSPYFTCVIGGRGSGKSTLLQLIASAI--KNKSFVKGLRLETIQKSLKIQSDIDIADSVEYLAQNEVEEFATNVS 369
Cdd:pfam13476  11 DQTIDFSKGLTLITGPNGSGKTTILDAIKLALygKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRYTYAIE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  370 KFTEAIFNRIDSKSSGKLKELERQITKGI--------EKFDEQIACWQEKTKLEEQLKESEKIRKKYQRIINTFTD-KNY 440
Cdd:pfam13476  91 RSRELSKKKGKTKKKEILEILEIDELQQFisellksdKIILPLLVFLGQEREEEFERKEKKERLEELEKALEEKEDeKKL 170

                         170
                  ....*....|....*....
gi 487878312  441 LDKKDKLQKTREELIDLRQ 459
Cdd:pfam13476 171 LEKLLQLKEKKKELEELKE 189
cbiO PRK13645
energy-coupling factor transporter ATPase;
734-813 5.68e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 39.61  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 734 YDKRALNETSFGQRCTAVLVVLLSLGNNPIIIDEPEAHLDSALIAKYLVALIK-ERKQERQIIFATHNANFVLNADAELI 812
Cdd:PRK13645 143 YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVI 222


                 .
gi 487878312 813 I 813
Cdd:PRK13645 223 V 223
 
Name Accession Description Interval E-value
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
382-666 2.80e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 382 KSSGKLKELERQITKGIEKFDEQIacwqekTKLEEQLKESEKIRKKYQ--RIINTFTDKnYLDKKDKLQKTREELIDLRQ 459
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEI------EELEEKVKELKELKEKAEeyIKLSEFYEE-YLDELREIEKRLSRLEEEIN 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 460 SKEGFLTFIKELKRVVNFESKENMEEKNSYD------KVYNQLKQdICKELEQIDINIKNGCFKSDEEKIEKLESEHQTL 533
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKA-KKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 534 LQEIGEFLKEKGVSDENIGDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNKINLAFK 613
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487878312 614 EISKNHKEEVRLITikyylNEDIFEGVFEDFDKLvdKGFNIQKHQSKIKEYLK 666
Cdd:PRK03918 484 ELEKVLKKESELIK-----LKELAEQLKELEEKL--KKYNLEELEKKAEEYEK 529
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 660-840 9.78e-07

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: 51.93  E-value: 9.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 660 KIKEYLKGIELKDIIDVQCTEFIEKLDSLIENKKAAFyETMMDVFNR---EIHFQIYRLLILKHLRNVEKYKIFEVRYD- 735
Cdd:COG3593   76 TFGSLLSRLLRLLLKEEDKEELEEALEELNEELKEAL-KALNELLSEylkELLDGLDLELELSLDELEDLLKSLSLRIEd 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 736 --KRALNETSFGQRCTAVLVVLLSL------GNNPII-IDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLN 806
Cdd:COG3593  155 gkELPLDRLGSGFQRLILLALLSALaelkraPANPILlIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSE 234

                        170       180       190
                 ....*....|....*....|....*....|....
gi 487878312 807 ADAELIIQLKNENNKIIAQSFTIESDGYRDDLLK 840
Cdd:COG3593  235 VPLENIRRLRRDSGGTTSTKLIDLDDEDLRKLLR 268
COG4637 COG4637
Predicted ATPase [General function prediction only];
750-804 2.12e-06

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 50.70  E-value: 2.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 487878312 750 AVLVVLLSlgNNP---IIIDEPEAHLDSALIAKyLVALIKERKQERQIIFATHNANFV 804
Cdd:COG4637  268 ALLAALLS--PRPpplLCIEEPENGLHPDLLPA-LAELLREASERTQVIVTTHSPALL 322
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 743-813 7.39e-06

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: 46.85  E-value: 7.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487878312 743 SFGQRCTAVLVVLLSLgnNP--IIIDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLNADAELII 813
Cdd:cd00267   82 SGGQRQRVALARALLL--NPdlLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 373-809 9.43e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.58  E-value: 9.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   373 EAIFNRIDSKSSGKLKELERQITKGIEKFDE--QIACWQEKTKLEEQLKESEKIRKKYQRIINTFTDKNYLDKKDKLQKT 450
Cdd:pfam02463  724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   451 REELIDLRQSKEGFLTFIKELKRVVNFESKENMEEKNSYDKVYNQLKQDICKELEQIDINIKNGCF-KSDEEKIEKLESE 529
Cdd:pfam02463  804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLqELLLKEEELEEQK 883

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   530 HQTLLQEIGEFLKEKGVSDENIGDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNKIN 609
Cdd:pfam02463  884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   610 LAFKEISKNHKEEVRLITIKYYLNEDiFEGVFEDFDKLVDKGFNIQKHQSKIKEYLKGIELKDIIDVQCTEFIEKLDSLI 689
Cdd:pfam02463  964 RLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLEL 1042

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   690 ENKKAAFYETMMDVFNREIHFqiyrllilkHLRNVEKykifevryDKRALNETSFGQRCTAVLVVLLSL-GNNPI---II 765
Cdd:pfam02463 1043 GGSAELRLEDPDDPFSGGIEI---------SARPPGK--------GVKNLDLLSGGEKTLVALALIFAIqKYKPApfyLL 1105

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 487878312   766 DEPEAHLDSALIAKyLVALIKERKQERQIIFATHNANFVLNADA 809
Cdd:pfam02463 1106 DEIDAALDDQNVSR-VANLLKELSKNAQFIVISLREEMLEKADK 1148
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 574-804 1.08e-05

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: 48.15  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  574 EIKEIANKIESFSY-EDMDKNIEKFKNQINE---ELNKINLAFKEISKNHKEEVRLITIKYYLNEDIFEGVFEDFDKLVD 649
Cdd:pfam13304  41 GIGGIPSLLNGIDPkEPIEFEISEFLEDGVRyryGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  650 KGFNIQKHQSKIKEYLKGIELKDIIDVQCT--EFIEKLDSLIENKKAAFY---ETMMDVFNREIHFQIYRLLILKHL--- 721
Cdd:pfam13304 121 GLDVEERIELSLSELSDLISGLLLLSIISPlsFLLLLDEGLLLEDWAVLDlaaDLALFPDLKELLQRLVRGLKLADLnls 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  722 --------------RNVEKYKIFEVRYDKRALNETSFG---QRCTAVLVVLLSLGNNP--IIIDEPEAHLDSALIAKYLV 782
Cdd:pfam13304 201 dlgegieksllvddRLRERGLILLENGGGGELPAFELSdgtKRLLALLAALLSALPKGglLLIDEPESGLHPKLLRRLLE 280

                         250       260
                  ....*....|....*....|..
gi 487878312  783 ALIKERKQERQIIFATHNANFV 804
Cdd:pfam13304 281 LLKELSRNGAQLILTTHSPLLL 302
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
616-812 1.47e-05

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 48.12  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 616 SKNHKEEVRLITIKYYLNEDIFEGVFEDFDKLVDKGFNIQKHQSKIKEylkGIELKDIIDvqctEFIEKLDSLIENkkaa 695
Cdd:COG1106  103 ERIISEWLYFLSTAAQLNVPLLSPLYDWFDNNISLDTSSDGLTLLLKE---DESLKEELL----ELLKIADPGIED---- 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 696 fyetmMDVFNREIHFQIYRLLILKHlrnvekyKIFEVRYDkraLNETSFG-QR--CTAVLVVLLSLGNNPIIIDEPEAHL 772
Cdd:COG1106  172 -----IEVEEEEIEDLVERKLIFKH-------KGGNVPLP---LSEESDGtKRllALAGALLDALAKGGVLLIDEIEASL 236

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 487878312 773 DSALIaKYLVALIKERKQER--QIIFATHNANFvLNADAELI 812
Cdd:COG1106  237 HPSLL-RKLLKLFLDLANKNnaQLIFTTHSTEL-LDAFLELL 276
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 743-808 1.61e-05

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: 46.83  E-value: 1.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487878312 743 SFGQRCTAVLVVLLSL----GNN--PIIIDEPEAHLDSALIAKYLVALIKERKQE--RQIIFATHNANFVLNAD 808
Cdd:cd03240  117 SGGEKVLASLIIRLALaetfGSNcgILALDEPTTNLDEENIEESLAEIIEERKSQknFQLIVITHDEELVDAAD 190
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
287-842 3.24e-05

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 47.81  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 287 CYAGFNETLFFSPYfTCVIGGRGSGKSTLLQLIAS-AIKNKSFVKGLRLETIQKSLKIQSDIDIADSvEYLAQNeveeFA 365
Cdd:COG4694   13 AFKDFGWLAFFKKL-NLIYGENGSGKSTLSRILRSlELGDTSSEVIAEFEIEAGGSAPNPSVRVFNR-DFVEEN----LR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 366 TNVSKFTEAIFNRIDSKSSGKLKELERQITKGIEKFDEQIA-CWQEKTKLEEQLKESEKIRKKYQRIINTFTDKNYldKK 444
Cdd:COG4694   87 SGEEIKGIFTLGEENIELEEEIEELEKEIEDLKKELDKLEKeLKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNY--RK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 445 DKLQKTREEL-----IDLRQSKEGFltFIKELKRVVNFESKENMeeKNSYDKVYNQLKQDIC-KELEQIDINIKNgcfKS 518
Cdd:COG4694  165 ANLEKKLSALkssseDELKEKLKLL--KEEEPEPIAPITPLPDL--KALLSEAETLLEKSAVsSAIEELAALIQN---PG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 519 DEEKIEKLESEHQTLLQEIGEFLkEKGVSDENIGDIRNA-NYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKF 597
Cdd:COG4694  238 NSDWVEQGLAYHKEEEDDTCPFC-QQELAAERIEALEAYfDDEYEKLLAALKDLLEELESAINALSALLLEILRTLLPSA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 598 KNQINEELNKINLAFKE----ISKNHKEEVRLITIKYYLNEDIFEGVFEDFDKLVDKgFN--IQKHQSKIKEYLKGI--- 668
Cdd:COG4694  317 KEDLKAALEALNALLETllaaLEEKIANPSTSIDLDDQELLDELNDLIAALNALIEE-HNakIANLKAEKEEARKKLeah 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 669 ---ELKDIID----------------VQCTEFIEKLDSLIENKKAAFYET--MMDVFNREIH---FQIYRLLILKHlrNV 724
Cdd:COG4694  396 elaELKEDLSrykaeveelieelktiKALKKALEDLKTEISELEAELSSVdeAADEINEELKalgFDEFSLEAVED--GR 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 725 EKYKIFEVRYDKRALNET-SFG-QRCTAVLVVLLSL-------GNNPIIIDEPEAHLDSalIAKYLVA--LIKERKQERQ 793
Cdd:COG4694  474 SSYRLKRNGENDAKPAKTlSEGeKTAIALAYFLAELegdendlKKKIVVIDDPVSSLDS--NHRFAVAslLKELSKKAKQ 551

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 487878312 794 IIFATHNANFVLnadaELIIQLKNENNKIIAQSFTIESDGYRDDLLKLE 842
Cdd:COG4694  552 VIVLTHNLYFLK----ELRDLADEDNKKKNCAFYEIRKDNRGSKIIKLD 596
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 388-672 5.62e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 47.35  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   388 KELERQITKGIEKFDEQIACWQE-----KTKLEEQLKESEKIRK-------KYQRII--NTFTDKNYLDKKDKLQKTREE 453
Cdd:TIGR01612  536 AKLYKEIEAGLKESYELAKNWKKliheiKKELEEENEDSIHLEKeikdlfdKYLEIDdeIIYINKLKLELKEKIKNISDK 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   454 ------LIDLRQSKEGFLTFIKELKRVVNFESKENMEEKnsyDKVYNQLKQDICKeLEQIDINIKNGCFKSDEEKIEKLE 527
Cdd:TIGR01612  616 neyikkAIDLKKIIENNNAYIDELAKISPYQVPEHLKNK---DKIYSTIKSELSK-IYEDDIDALYNELSSIVKENAIDN 691

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   528 SEHQTLLQEIGEFLKEKGVSDENIgDIRNANYHLANEKMNIADLEREIKEIANKIESFSYEDMDKNIEKFKNQINEELNK 607
Cdd:TIGR01612  692 TEDKAKLDDLKSKIDKEYDKIQNM-ETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNK 770

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487878312   608 INLAFKEISKNHKEEVRLITIKYYLNEDIfegvfeDFDKLVDKgfNIQKHQSKIKEYLKGIELKD 672
Cdd:TIGR01612  771 INDYAKEKDELNKYKSKISEIKNHYNDQI------NIDNIKDE--DAKQNYDKSKEYIKTISIKE 827
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-621 1.35e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   333 RLETIQKSL-KIQSDI-DIADSVEYLAQnEVEEFATNVSKFTEAIFNRIDSKssgkLKELERQItkgiEKFDEQIAcwqe 410
Cdd:TIGR02169  245 QLASLEEELeKLTEEIsELEKRLEEIEQ-LLEELNKKIKDLGEEEQLRVKEK----IGELEAEI----ASLERSIA---- 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   411 ktKLEEQLKESEKIRKKYQRIINtftdkNYLDKKDKLqktREELIDLRQSKEGFLTFIKELKrvvnfeskenmeeknsyd 490
Cdd:TIGR02169  312 --EKERELEDAEERLAKLEAEID-----KLLAEIEEL---EREIEEERKRRDKLTEEYAELK------------------ 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   491 KVYNQLKQdickELEQIDINIKNGC--FKSDEEKIEKLESEHQTLLQEIGEFLKEKGVSDENIGDIRNAnyhLANEKMNI 568
Cdd:TIGR02169  364 EELEDLRA----ELEEVDKEFAETRdeLKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEAKI 436

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 487878312   569 ADLEREIKEIANKIE------SFSYEDMDKnIEKFKNQINEELNKINlafKEISKNHKE 621
Cdd:TIGR02169  437 NELEEEKEDKALEIKkqewklEQLAADLSK-YEQELYDLKEEYDRVE---KELSKLQRE 491
COG4938 COG4938
Predicted ATPase [General function prediction only];
739-807 1.76e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 44.19  E-value: 1.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487878312 739 LNETSFGQRCTAVLVVLLSLGNNP---IIIDEPEAHLD---SALIAKYLVALIKERKqerQIIFATHnANFVLNA 807
Cdd:COG4938  139 LSNVGSGVSELLPILLALLSAAKPgslLIIEEPEAHLHpkaQSALAELLAELANSGV---QVIIETH-SDYILNG 209
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 294-400 3.25e-04

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (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: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 42.97  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 294 TLFFSPYFTCVIGGRGSGKSTLL-----------QLIASAIKNKSFVK-GLRLETIQKSLKIQS-DIDIADSVEYLAQNE 360
Cdd:cd03277   18 EFRPGPSLNMIIGPNGSGKSSIVcaiclglggkpKLLGRAKKVGEFVKrGCDEGTIEIELYGNPgNIQVDNLCQFLPQDR 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 487878312 361 VEEFATNVS-----KFteaifnridsKSSGKLKELERQITKGIEK 400
Cdd:cd03277   98 VGEFAKLSPiellvKF----------REGEQLQELDPHHQSGGER 132
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
292-565 4.36e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 292 NETLFFSPYFTCVIGGRGSGKSTLLQliasaiknksFVKGLRLETIQKSLkiqsdidiadsveylaqneveefatnvskf 371
Cdd:COG4717   16 DRTIEFSPGLNVIYGPNEAGKSTLLA----------FIRAMLLERLEKEA------------------------------ 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 372 tEAIFN---RIDSKSSGKLKELERQITKGIEKFDEQIACWQEKTKLEEQLKESEKIRKKYQRIINTftdknyLDKKDKLQ 448
Cdd:COG4717   56 -DELFKpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK------LEKLLQLL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 449 KTREELIDLRQSKEGFLTFIKELKRVVNfESKENMEEKNSYDKVYNQLKQDICKELEQIDINIKNGcFKSDEEKIEKLES 528
Cdd:COG4717  129 PLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEELQQ 206

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 487878312 529 EHQTLLQEIGEFLKEKGVSDENIGDIRNANYHLANEK 565
Cdd:COG4717  207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 758-843 5.34e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 43.67  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 758 LGNNPIII-DEPEAHLDSALiAKYLVALIKERKQERQIIFATHNANFVLNADaeLIIQLknENNKIIAqsftiesDGYRD 836
Cdd:COG2274  627 LRNPRILIlDEATSALDAET-EAIILENLRRLLKGRTVIIIAHRLSTIRLAD--RIIVL--DKGRIVE-------DGTHE 694


                 ....*..
gi 487878312 837 DLLKLEG 843
Cdd:COG2274  695 ELLARKG 701
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 407-671 5.83e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   407 CWQEKTKLEEQLKESEKIRKKYqriintftdknyldkKDKLQKTREELIDLRQSKEGFLTFIKELK-RVVNFESKENMEE 485
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAEL---------------RKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   486 KNSYDKVYNQLKQDICKELEQIDINIKNGCFKSDEEKIEKLESEHQTLLQEIGEFLK-----EKGVSDENIgDIRNANYH 560
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldelRAELTLLNE-EAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   561 LANEKMNIADLEREIKEIANKIESFS--YEDMDKNIEKFKNQINEELNKINLAFKEISKnHKEEVRLITIKYYLNEDIFE 638
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSedIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELEELSEELR 904

                          250       260       270
                   ....*....|....*....|....*....|...
gi 487878312   639 GVFEDFDKLVDKGFNIQKHQSKIKEYLKGIELK 671
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVR 937
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 292-544 5.86e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 43.36  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  292 NETLFFSPYFTCVIGGRGSGKSTLLQLIASAIKNKSFVKGLRLETIQKSLKIQSDIDIADSVEYLAQNEVE----EFATN 367
Cdd:pfam13175  16 DTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNIFENISFSIDIeidvEFLLI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  368 VSKFTEAIFNRIDSKSSGKLKELErqITKGIEKFDEQIACWQEKtklEEQLKESEKIRKKYQRIINTFTD-KNYLDKKDK 446
Cdd:pfam13175  96 LFGYLEIKKKYLCLASKGKAKEYE--KTLHPKGANKADLLLELK---ISDLKKYLKQFKIYIYNNYYLDEkKNVFDKKSK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  447 LQKTREELIDLRQSKEGFLTFIKELKRVVN-----FESKENMEEKNSYDKVYNQLKQDICKELEQIDINIKNGCFKSDEE 521
Cdd:pfam13175 171 YELPSLKEEFLNSEKEEIKVDKEDLKKLINeleksINYHENVLENLQIKKLLISADRNASDEDSEKINSLLGALKQRIFE 250

                         250       260
                  ....*....|....*....|...
gi 487878312  522 KIEKLESEHQTLLQEIGEFLKEK 544
Cdd:pfam13175 251 EALQEELELTEKLKETQNKLKEI 273
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 381-633 9.70e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.12  E-value: 9.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   381 SKSSGKLKELERQITKGIEKFDEQIACWQEKtklEEQLKESEKIRKKYQRIINTftdknyldKKDKLQKTREELIDLRQS 460
Cdd:TIGR01612  775 AKEKDELNKYKSKISEIKNHYNDQINIDNIK---DEDAKQNYDKSKEYIKTISI--------KEDEIFKIINEMKFMKDD 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   461 kegfltFIKELKRVVNFES--KENME-EKNSYDKVYNQLKQDICKELEQIDINIKNGCFKSDEEKIEKLESEHQTL--LQ 535
Cdd:TIGR01612  844 ------FLNKVDKFINFENncKEKIDsEHEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNIntLK 917

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   536 EIGEFLKEKGVSDENIGDIRNANYHLaNEKMNiadleREIKEI--ANKIESfSYEDmdknieKFKNQINEELNKINLAFK 613
Cdd:TIGR01612  918 KVDEYIKICENTKESIEKFHNKQNIL-KEILN-----KNIDTIkeSNLIEK-SYKD------KFDNTLIDKINELDKAFK 984

                          250       260
                   ....*....|....*....|
gi 487878312   614 EISKNHKEEVRLITIKYYLN 633
Cdd:TIGR01612  985 DASLNDYEAKNNELIKYFND 1004
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 758-843 1.07e-03

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: 42.44  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 758 LGNNPIII-DEPEAHLDSALiAKYLVALIKERKQERQIIFATHNANFVLNADAelIIQLknENNKIIAQsftiesdGYRD 836
Cdd:COG4988  489 LRDAPLLLlDEPTAHLDAET-EAEILQALRRLAKGRTVILITHRLALLAQADR--ILVL--DDGRIVEQ-------GTHE 556


                 ....*..
gi 487878312 837 DLLKLEG 843
Cdd:COG4988  557 ELLAKNG 563
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 413-716 1.17e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  413 KLEEQLKESEKIRKKYqriINTFTDKNYLDKKDKLQKTREELIDLRQSKEGFLTFIKELKRVVNfeskenmeeknsydkv 492
Cdd:pfam06160 150 ELEKQLAEIEEEFSQF---EELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELP---------------- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  493 ynqlkqdickelEQIDiNIKNGCfksDEEKIEKLESEHQTLLQEIGEFLKEKGVSDENIgdirnanyhlanEKMNIADLE 572
Cdd:pfam06160 211 ------------DQLE-ELKEGY---REMEEEGYALEHLNVDKEIQQLEEQLEENLALL------------ENLELDEAE 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  573 REIKEIANKIESFsYEDMDKNIEKfKNQINEELNKINLAFKEISKNHKE---EVRLITIKYYLNEDI----------FEG 639
Cdd:pfam06160 263 EALEEIEERIDQL-YDLLEKEVDA-KKYVEKNLPEIEDYLEHAEEQNKElkeELERVQQSYTLNENElervrglekqLEE 340

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487878312  640 VFEDFDKLVDKGFNIQKHQSKIKEYLKGIE--LKDIIDVQcTEFIEKLDSLIENKKAAfyETMMDVFNREIHfQIYRLL 716
Cdd:pfam06160 341 LEKRYDEIVERLEEKEVAYSELQEELEEILeqLEEIEEEQ-EEFKESLQSLRKDELEA--REKLDEFKLELR-EIKRLV 415
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
733-813 1.80e-03

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 40.29  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 733 RYDKRALNETSFGQRCTAVLVVLLSLGNNPIIIDEPEAHLDSALIAKYLVALIKERKQERQIIFATHNANFVLNADAELI 812
Cdd:NF040873 111 DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190


                 .
gi 487878312 813 I 813
Cdd:NF040873 191 L 191
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 743-813 2.03e-03

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: 39.65  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487878312 743 SFGQRCTAVLVVLLSLGN-NP---IIIDEPEAHLDSALIAKyLVALIKE-RKQERQIIFATHNANFVLNADAELII 813
Cdd:cd03227   79 SGGEKELSALALILALASlKPrplYILDEIDRGLDPRDGQA-LAEAILEhLVKGAQVIVITHLPELAELADKLIHI 153
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 357-668 2.54e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.58  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   357 AQNEVEEFATNVSKFTEAIFNRIDSKSSGKLKELERQITKGIEKFDEQIAcwqekTKLEEQLKESEKIRKKYQRI-INTF 435
Cdd:TIGR01612 1027 ATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEIL-----EEAEINITNFNEIKEKLKHYnFDDF 1101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   436 TDKNYLDKKDKLQKTREElidlrqskegfltfIKELKRVVNFESKENMEEKNSYDKVYNQLKQDICKELEQIDINIKNGC 515
Cdd:TIGR01612 1102 GKEENIKYADEINKIKDD--------------IKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDD 1167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   516 FKSDEEKIEKLES----------EHQTLLQEIGEFLKEKgVSDENIGDIrNANYHLANEKMNIADLEREIKEIANKIESF 585
Cdd:TIGR01612 1168 PEEIEKKIENIVTkidkkkniydEIKKLLNEIAEIEKDK-TSLEEVKGI-NLSYGKNLGKLFLEKIDEEKKKSEHMIKAM 1245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   586 S--YEDMD---------KNIEKFKNQINEELNKINLAFKE------ISKNHKEEVRLITIKYY-LNEDIF-EGVFEDFDK 646
Cdd:TIGR01612 1246 EayIEDLDeikekspeiENEMGIEMDIKAEMETFNISHDDdkdhhiISKKHDENISDIREKSLkIIEDFSeESDINDIKK 1325

                          330       340
                   ....*....|....*....|...
gi 487878312   647 LVDKGF-NIQKHQSKIKEYLKGI 668
Cdd:TIGR01612 1326 ELQKNLlDAQKHNSDINLYLNEI 1348
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 754-843 3.44e-03

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 40.90  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 754 VLLSlgNNPIII-DEPEAHLDsALIAKYLVALIKERKQERQIIFATHNANFVLNADAelIIQLknENNKIIAQsftiesd 832
Cdd:COG4987  485 ALLR--DAPILLlDEPTEGLD-AATEQALLADLLEALAGRTVLLITHRLAGLERMDR--ILVL--EDGRIVEQ------- 550

                         90
                 ....*....|.
gi 487878312 833 GYRDDLLKLEG 843
Cdd:COG4987  551 GTHEELLAQNG 561
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 342-618 4.01e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.19  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   342 KIQSDIDIADSVEYLAQNEVEEFATNVSKFTEAIFNRIdskSSGKLKELERQITKGIEKFDEQIACWQEKTKLEEQLKES 421
Cdd:TIGR01612 1126 KIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI---SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEI 1202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   422 EKIRKKYQRI--INTFTDKN----YLDKKDKLQKTREELIDLRQSKEGFLTFIKELKRVVNFESKENMEEK--------- 486
Cdd:TIGR01612 1203 EKDKTSLEEVkgINLSYGKNlgklFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKaemetfnis 1282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   487 NSYDKVYNQLKQDICKELEQI-DINIKNGCFKSDEEKIEKLESEHQTLLQEigeflKEKGVSDENIGDIRNANYHlanek 565
Cdd:TIGR01612 1283 HDDDKDHHIISKKHDENISDIrEKSLKIIEDFSEESDINDIKKELQKNLLD-----AQKHNSDINLYLNEIANIY----- 1352

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 487878312   566 mNIADLEReIKEIANKIESFSyedmdKNIEKFKNQINEELNKINLAFKEISKN 618
Cdd:TIGR01612 1353 -NILKLNK-IKKIIDEVKEYT-----KEIEENNKNIKDELDKSEKLIKKIKDD 1398
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 358-706 5.00e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.81  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   358 QNEVEEFATNVSKFTEaifnrIDSKSSGKLKElerqiTKGIEKfdeQIACWQEKTKlEEQLKESEKIRKKYQRIINTFTD 437
Cdd:TIGR01612 1599 QLSLENFENKFLKISD-----IKKKINDCLKE-----TESIEK---KISSFSIDSQ-DTELKENGDNLNSLQEFLESLKD 1664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   438 --KNYLDKKDKLQKTREEL----IDLRQSKEGFLTFIKELKRVVNFESKENMEE-KNSYDKVYNQLKQDI-CKELEQIDI 509
Cdd:TIGR01612 1665 qkKNIEDKKKELDELDSEIekieIDVDQHKKNYEIGIIEKIKEIAIANKEEIESiKELIEPTIENLISSFnTNDLEGIDP 1744

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   510 NIKNGCFKSDeekIEKLESEHQTLLQEIGEFLKEkgVSDENI--GDIRNANYHLANEKMNIADLEREIKEIANKIESfsy 587
Cdd:TIGR01612 1745 NEKLEEYNTE---IGDIYEEFIELYNIIAGCLET--VSKEPItyDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEA--- 1816

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312   588 EDMDKNIEKFKNQIN-------EELNKINLAFKEIS------KNHKEEVRLITI--------------KYYLNEDIFEGV 640
Cdd:TIGR01612 1817 KEFDRIINHFKKKLDhvndkftKEYSKINEGFDDISksienvKNSTDENLLFDIlnktkdayagiigkKYYSYKDEAEKI 1896

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487878312   641 FEDFDKLVDKgFNIQKHQSkikeylKGIELKDIIDVQCTEFI--EKLDSLI-----ENKKAAF------YETMMDVFNR 706
Cdd:TIGR01612 1897 FINISKLANS-INIQIQNN------SGIDLFDNINIAILSSLdsEKEDTLKfipspEKEPEIYtkirdsYDTLLDIFKK 1968
AAA_23 pfam13476
AAA domain;
292-459 5.61e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 39.02  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  292 NETLFFSPYFTCVIGGRGSGKSTLLQLIASAI--KNKSFVKGLRLETIQKSLKIQSDIDIADSVEYLAQNEVEEFATNVS 369
Cdd:pfam13476  11 DQTIDFSKGLTLITGPNGSGKTTILDAIKLALygKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRYTYAIE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312  370 KFTEAIFNRIDSKSSGKLKELERQITKGI--------EKFDEQIACWQEKTKLEEQLKESEKIRKKYQRIINTFTD-KNY 440
Cdd:pfam13476  91 RSRELSKKKGKTKKKEILEILEIDELQQFisellksdKIILPLLVFLGQEREEEFERKEKKERLEELEKALEEKEDeKKL 170

                         170
                  ....*....|....*....
gi 487878312  441 LDKKDKLQKTREELIDLRQ 459
Cdd:pfam13476 171 LEKLLQLKEKKKELEELKE 189
cbiO PRK13645
energy-coupling factor transporter ATPase;
734-813 5.68e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 39.61  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 734 YDKRALNETSFGQRCTAVLVVLLSLGNNPIIIDEPEAHLDSALIAKYLVALIK-ERKQERQIIFATHNANFVLNADAELI 812
Cdd:PRK13645 143 YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVI 222


                 .
gi 487878312 813 I 813
Cdd:PRK13645 223 V 223
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 413-693 5.86e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 5.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 413 KLEEQLKESEKIRKKYQRIINtftDKNYLDKKDKLQKTREELIDLRQSKEGFLTFIKELKRVV--NFESKEN----MEEK 486
Cdd:PRK04778 169 ELEKQLENLEEEFSQFVELTE---SGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELpdQLQELKAgyreLVEE 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 487 NsYDKVYNQLK---QDICKELEQIDINIKNGCFKSDEEKIEKLESEHQTLLQEIGEFLKEKGVSDENIGDIRNANYHLAN 563
Cdd:PRK04778 246 G-YHLDHLDIEkeiQDLKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKE 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487878312 564 EKmniADLEREIKEIANkiesfSYEDMDKNIEKFKnQINEELNKINLAFKEISKNHKEEvrliTIKYYLNEDIFEGVFED 643
Cdd:PRK04778 325 QN---KELKEEIDRVKQ-----SYTLNESELESVR-QLEKQLESLEKQYDEITERIAEQ----EIAYSELQEELEEILKQ 391

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 487878312 644 FDklvdkgfNIQKHQSKIKEYLKGIElKDIIDVQctEFIEKLDSLIENKK 693
Cdd:PRK04778 392 LE-------EIEKEQEKLSEMLQGLR-KDELEAR--EKLERYRNKLHEIK 431
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 296-339 8.33e-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: 38.67  E-value: 8.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 487878312 296 FFSPYFTCVIGGRGSGKSTLLQLIASAIKNKS---FVKGLRLETIQK 339
Cdd:cd03235   22 VKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSgsiRVFGKPLEKERK 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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