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Conserved domains on  [gi|24762654|ref|NP_726454|]
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leucine zipper and EF-hand containing transmembrane protein 1, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LETM1_RBD pfam07766
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a ...
 219-450 1.14e-116

LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a role in potassium and hydrogen ion exchange. Deletion of LETM1 is thought to be involved in the development of Wolf-Hirschhorn syndrome in humans. This entry represents the ribosome-binding domain (RBD) of LETM1/MDM38 proteins.


:

Pssm-ID: 462258 [Multi-domain]  Cd Length: 229  Bit Score: 357.57  E-value: 1.14e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    219 LTRRENKQLQRTTSDLFRLIPFSVFIIVPFMELLLPLFIKFFPGMLPSTFQTSTDRQEKLRQSLSVRLEVAKFLQQTLDQ 298
Cdd:pfam07766    1 LTRREREQLRRTTRDLFRLVPFSVFIIVPFAELLLPVLLKLFPNLLPSTFWSKKQKEEKLKKRLKARLEVAKFLQETVEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    299 MpvqHKEHSSEEAKQFEAFFTKIRNPTEPVSNDEIIKFAKRFDDEITLDSLSREQLAALCRVLELNTIGTTTLLRFQLRL 378
Cdd:pfam07766   81 S---LSDETTELKEEFKEFFKKVRSGGEPPSNEEILKVAKLFKDDLTLDNLSRPQLVALCKYMNLTPFGTDNLLRYRLRH 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762654    379 KLRSLATDDRVIAREGVDSLDLLELQQACKARGMRAYGLTEERLRFQLKEWIDLSLNEQVPPTLLLLSRTML 450
Cdd:pfam07766  158 KLLEIKRDDRAIAREGVDSLSLEELQSACYSRGIRPLGLSEERLREWLQQWLDLSLNLKVPSSLLLLSRAVL 229
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
543-916 1.28e-06

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: 52.76  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   543 DHKEQSSVSETDKGISSTDVQLLSEALKTLSSDKQLVVE-KETIKELKEELADYKEDVEELREVRQVVKEPVR------- 614
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltg 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   615 ---ESRAAKLLY------------NRVNKMISQLDNVLNDLEARQHQIKQAESSDYAASSPTVEPQQMVHIDELVATIRR 679
Cdd:PRK03918  384 ltpEKLEKELEElekakeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKR 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   680 ----MKEASDEER-FKVVGDLLVKLDADKDGVISVNEITKAVQSIDREATNIDKKQLEEFTELLSKLASRrrheeivhID 754
Cdd:PRK03918  464 iekeLKEIEEKERkLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK--------LI 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   755 DLMNNIKVLKEtsDEARLKHIEAVLEKFDADKDGVVT-VNDIRKVLESIGRDNIKLSDKAIEEL-------ISLLDKEQV 826
Cdd:PRK03918  536 KLKGEIKSLKK--ELEKLEELKKKLAELEKKLDELEEeLAELLKELEELGFESVEELEERLKELepfyneyLELKDAEKE 613

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   827 LQAEQKiekaiaksmkEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDI-----ANEMRDKEETVPDKAKELKAEPAFKD 901
Cdd:PRK03918  614 LEREEK----------ELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELE 683

                         410
                  ....*....|....*.
gi 24762654   902 TAKTLKDN-AKDLDDL 916
Cdd:PRK03918  684 ELEKRREEiKKTLEKL 699
 
Name Accession Description Interval E-value
LETM1_RBD pfam07766
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a ...
 219-450 1.14e-116

LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a role in potassium and hydrogen ion exchange. Deletion of LETM1 is thought to be involved in the development of Wolf-Hirschhorn syndrome in humans. This entry represents the ribosome-binding domain (RBD) of LETM1/MDM38 proteins.


Pssm-ID: 462258 [Multi-domain]  Cd Length: 229  Bit Score: 357.57  E-value: 1.14e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    219 LTRRENKQLQRTTSDLFRLIPFSVFIIVPFMELLLPLFIKFFPGMLPSTFQTSTDRQEKLRQSLSVRLEVAKFLQQTLDQ 298
Cdd:pfam07766    1 LTRREREQLRRTTRDLFRLVPFSVFIIVPFAELLLPVLLKLFPNLLPSTFWSKKQKEEKLKKRLKARLEVAKFLQETVEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    299 MpvqHKEHSSEEAKQFEAFFTKIRNPTEPVSNDEIIKFAKRFDDEITLDSLSREQLAALCRVLELNTIGTTTLLRFQLRL 378
Cdd:pfam07766   81 S---LSDETTELKEEFKEFFKKVRSGGEPPSNEEILKVAKLFKDDLTLDNLSRPQLVALCKYMNLTPFGTDNLLRYRLRH 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762654    379 KLRSLATDDRVIAREGVDSLDLLELQQACKARGMRAYGLTEERLRFQLKEWIDLSLNEQVPPTLLLLSRTML 450
Cdd:pfam07766  158 KLLEIKRDDRAIAREGVDSLSLEELQSACYSRGIRPLGLSEERLREWLQQWLDLSLNLKVPSSLLLLSRAVL 229
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
543-916 1.28e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   543 DHKEQSSVSETDKGISSTDVQLLSEALKTLSSDKQLVVE-KETIKELKEELADYKEDVEELREVRQVVKEPVR------- 614
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltg 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   615 ---ESRAAKLLY------------NRVNKMISQLDNVLNDLEARQHQIKQAESSDYAASSPTVEPQQMVHIDELVATIRR 679
Cdd:PRK03918  384 ltpEKLEKELEElekakeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKR 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   680 ----MKEASDEER-FKVVGDLLVKLDADKDGVISVNEITKAVQSIDREATNIDKKQLEEFTELLSKLASRrrheeivhID 754
Cdd:PRK03918  464 iekeLKEIEEKERkLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK--------LI 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   755 DLMNNIKVLKEtsDEARLKHIEAVLEKFDADKDGVVT-VNDIRKVLESIGRDNIKLSDKAIEEL-------ISLLDKEQV 826
Cdd:PRK03918  536 KLKGEIKSLKK--ELEKLEELKKKLAELEKKLDELEEeLAELLKELEELGFESVEELEERLKELepfyneyLELKDAEKE 613

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   827 LQAEQKiekaiaksmkEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDI-----ANEMRDKEETVPDKAKELKAEPAFKD 901
Cdd:PRK03918  614 LEREEK----------ELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELE 683

                         410
                  ....*....|....*.
gi 24762654   902 TAKTLKDN-AKDLDDL 916
Cdd:PRK03918  684 ELEKRREEiKKTLEKL 699
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 625-924 7.56e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 7.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    625 RVNKMISQLDNVLNDLEARQHQIKQAESSdyaASSPTVEPQQMvhIDELVATIRRMKEasDEERFK-VVGDLLVKLDADK 703
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASRK--IGEIEKEIEQLEQ--EEEKLKeRLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    704 DgvisvnEITKAVQSIDREATNIDKKQ--LEEFTELLSKLASRRRHEEIVHIDDLMNNIKvlKETSD-EARLKHIEAVLE 780
Cdd:TIGR02169  751 Q------EIENVKSELKELEARIEELEedLHKLEEALNDLEARLSHSRIPEIQAELSKLE--EEVSRiEARLREIEQKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    781 KFDADKDgvvtvndirkvlesigrdnikLSDKAIEELISLLDKEQVLQAEqkIEKAIAKSMKEAEKLKSEVDKADKDLSK 860
Cdd:TIGR02169  823 RLTLEKE---------------------YLEKEIQELQEQRIDLKEQIKS--IEKEIENLNGKKEELEEELEELEAALRD 879

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    861 LVNDIHDSAKEIQDIANEMR------DKEETVPDKAKELKAEpaFKDTAKTLKDNAKDLDDLAKDPKSDP 924
Cdd:TIGR02169  880 LESRLGDLKKERDELEAQLRelerkiEELEAQIEKKRKRLSE--LKAKLEALEEELSEIEDPKGEDEEIP 947
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 774-823 4.32e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.45  E-value: 4.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24762654  774 HIEAVLEKFDADKDGVVTVNDIRKVLESIGRDnikLSDKAIEELISLLDK 823
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEG---LSEEEIDEMIREVDK 47
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
698-823 6.83e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654  698 KLDADKDGVISVNEITKAVQSIDREA-----TNIDKK-QLEEFTELLSKLASRRRHEEIvhiddlmnnikvlketsdear 771
Cdd:COG5126   13 LLDADGDGVLERDDFEALFRRLWATLfseadTDGDGRiSREEFVAGMESLFEATVEPFA--------------------- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24762654  772 lkhiEAVLEKFDADKDGVVTVNDIRKVLESIGrdnikLSDKAIEELISLLDK 823
Cdd:COG5126   72 ----RAAFDLLDTDGDGKISADEFRRLLTALG-----VSEEEADELFARLDT 114
LETM1_rel_film NF040639
LETM1-related biofilm-associated protein; This bacterial protein family is related to the ...
 219-268 8.62e-04

LETM1-related biofilm-associated protein; This bacterial protein family is related to the mitochondrial protein LETM1. The founding member, WP_060382447 from the fish pathogen Flavobacterium columnare, called a calcium-binding EF hand protein, was found highly up-regulated in expression during biofilm formation.


Pssm-ID: 468607  Cd Length: 396  Bit Score: 42.95  E-value: 8.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24762654   219 LTRRENKQLQRTTSDLFRLIPfSVFI-IVPFMELLLPLFIKFFPGMLPSTF 268
Cdd:NF040639  341 LNDEEKKKVKKQLLDIFKSIP-SLAIfLLPGGALLLPILIKFIPKLLPSAF 390
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 575-907 1.85e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    575 DKQLVVEKETIKELKEELADYKEDVEELREVRQVV--------KEPVRESRAAKLLYNRVNKMISQLDNVLNDLEARQHQ 646
Cdd:pfam15921  348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkreKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    647 IKQAESSDYAASSPTV--EPQQMVHID------ELVATIRRMKEASDEERFKVVGDLLVKLDADKDGVISVNEITKAVQS 718
Cdd:pfam15921  428 VQRLEALLKAMKSECQgqMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    719 IDR--EATNIDKKQLEEFTEL-LSKLASRRRHEEivHIDDLMNNIKVL------KETSDEARLKHIEAV----------- 778
Cdd:pfam15921  508 KERaiEATNAEITKLRSRVDLkLQELQHLKNEGD--HLRNVQTECEALklqmaeKDKVIEILRQQIENMtqlvgqhgrta 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    779 ----LEKFDADKDgvvtVNDIRKVLES--IGRDNIKLSDKAIEELISLLDKEQV--LQAEQKIEKAIAKSMKEAEKLKSE 850
Cdd:pfam15921  586 gamqVEKAQLEKE----INDRRLELQEfkILKDKKDAKIRELEARVSDLELEKVklVNAGSERLRAVKDIKQERDQLLNE 661

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24762654    851 VDKADKDLSKLVNDIHDSAKEIQDIANEMrdkeETVPDKAK-ELK-AEPAFKDTAKTLK 907
Cdd:pfam15921  662 VKTSRNELNSLSEDYEVLKRNFRNKSEEM----ETTTNKLKmQLKsAQSELEQTRNTLK 716
 
Name Accession Description Interval E-value
LETM1_RBD pfam07766
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a ...
 219-450 1.14e-116

LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a role in potassium and hydrogen ion exchange. Deletion of LETM1 is thought to be involved in the development of Wolf-Hirschhorn syndrome in humans. This entry represents the ribosome-binding domain (RBD) of LETM1/MDM38 proteins.


Pssm-ID: 462258 [Multi-domain]  Cd Length: 229  Bit Score: 357.57  E-value: 1.14e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    219 LTRRENKQLQRTTSDLFRLIPFSVFIIVPFMELLLPLFIKFFPGMLPSTFQTSTDRQEKLRQSLSVRLEVAKFLQQTLDQ 298
Cdd:pfam07766    1 LTRREREQLRRTTRDLFRLVPFSVFIIVPFAELLLPVLLKLFPNLLPSTFWSKKQKEEKLKKRLKARLEVAKFLQETVEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    299 MpvqHKEHSSEEAKQFEAFFTKIRNPTEPVSNDEIIKFAKRFDDEITLDSLSREQLAALCRVLELNTIGTTTLLRFQLRL 378
Cdd:pfam07766   81 S---LSDETTELKEEFKEFFKKVRSGGEPPSNEEILKVAKLFKDDLTLDNLSRPQLVALCKYMNLTPFGTDNLLRYRLRH 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24762654    379 KLRSLATDDRVIAREGVDSLDLLELQQACKARGMRAYGLTEERLRFQLKEWIDLSLNEQVPPTLLLLSRTML 450
Cdd:pfam07766  158 KLLEIKRDDRAIAREGVDSLSLEELQSACYSRGIRPLGLSEERLREWLQQWLDLSLNLKVPSSLLLLSRAVL 229
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
543-916 1.28e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   543 DHKEQSSVSETDKGISSTDVQLLSEALKTLSSDKQLVVE-KETIKELKEELADYKEDVEELREVRQVVKEPVR------- 614
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltg 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   615 ---ESRAAKLLY------------NRVNKMISQLDNVLNDLEARQHQIKQAESSDYAASSPTVEPQQMVHIDELVATIRR 679
Cdd:PRK03918  384 ltpEKLEKELEElekakeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKR 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   680 ----MKEASDEER-FKVVGDLLVKLDADKDGVISVNEITKAVQSIDREATNIDKKQLEEFTELLSKLASRrrheeivhID 754
Cdd:PRK03918  464 iekeLKEIEEKERkLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEK--------LI 535

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   755 DLMNNIKVLKEtsDEARLKHIEAVLEKFDADKDGVVT-VNDIRKVLESIGRDNIKLSDKAIEEL-------ISLLDKEQV 826
Cdd:PRK03918  536 KLKGEIKSLKK--ELEKLEELKKKLAELEKKLDELEEeLAELLKELEELGFESVEELEERLKELepfyneyLELKDAEKE 613

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   827 LQAEQKiekaiaksmkEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDI-----ANEMRDKEETVPDKAKELKAEPAFKD 901
Cdd:PRK03918  614 LEREEK----------ELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELE 683

                         410
                  ....*....|....*.
gi 24762654   902 TAKTLKDN-AKDLDDL 916
Cdd:PRK03918  684 ELEKRREEiKKTLEKL 699
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 666-892 1.37e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 49.16  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   666 QMVHIDELVATIRRMKEASDEERFKVVGDLLVKLDADKD---------GVISVNEITKAVQSIDREATNIDKKqLEEFTE 736
Cdd:PRK05771   29 GVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPklnplreekKKVSVKSLEELIKDVEEELEKIEKE-IKELEE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   737 LLSKLASRrrheeivhIDDLMNNIKVLK-------ETSDEARLKHIEAVLEKFDADKDGVVTVNDIRKVLESIGRDNIK- 808
Cdd:PRK05771  108 EISELENE--------IKELEQEIERLEpwgnfdlDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYv 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   809 ---------LSDKAIEELISLLDKEQVLQAEQKIEKAIAKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDIANEM 879
Cdd:PRK05771  180 yvvvvvlkeLSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIE 259

                         250
                  ....*....|...
gi 24762654   880 RDKEEtVPDKAKE 892
Cdd:PRK05771  260 LERAE-ALSKFLK 271
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 625-924 7.56e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 7.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    625 RVNKMISQLDNVLNDLEARQHQIKQAESSdyaASSPTVEPQQMvhIDELVATIRRMKEasDEERFK-VVGDLLVKLDADK 703
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASRK--IGEIEKEIEQLEQ--EEEKLKeRLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    704 DgvisvnEITKAVQSIDREATNIDKKQ--LEEFTELLSKLASRRRHEEIVHIDDLMNNIKvlKETSD-EARLKHIEAVLE 780
Cdd:TIGR02169  751 Q------EIENVKSELKELEARIEELEedLHKLEEALNDLEARLSHSRIPEIQAELSKLE--EEVSRiEARLREIEQKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    781 KFDADKDgvvtvndirkvlesigrdnikLSDKAIEELISLLDKEQVLQAEqkIEKAIAKSMKEAEKLKSEVDKADKDLSK 860
Cdd:TIGR02169  823 RLTLEKE---------------------YLEKEIQELQEQRIDLKEQIKS--IEKEIENLNGKKEELEEELEELEAALRD 879

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    861 LVNDIHDSAKEIQDIANEMR------DKEETVPDKAKELKAEpaFKDTAKTLKDNAKDLDDLAKDPKSDP 924
Cdd:TIGR02169  880 LESRLGDLKKERDELEAQLRelerkiEELEAQIEKKRKRLSE--LKAKLEALEEELSEIEDPKGEDEEIP 947
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
545-894 1.48e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   545 KEQSSVSETDKGISSTDVQLLSEALKTLSSDKQLVVEKETIKELKEELADYKEDVEELREVRQVVKEPVRESRaaklLYN 624
Cdd:PRK03918  228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   625 RVNKMISQLDNVLNDLEAR----QHQIKQAESSDYAASSPTVEpqqmvhIDELVATIRRMKEASDE-ERFKVVGDLLVKL 699
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEingiEERIKELEEKEERLEELKKK------LKELEKRLEELEERHELyEEAKAKKEELERL 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   700 DADKDGvISVNEITKAVQSIDREATNIDKKqLEEFTELLSKLASRrrheeivhIDDLMNNIKVLKETSDEARL------- 772
Cdd:PRK03918  378 KKRLTG-LTPEKLEKELEELEKAKEEIEEE-ISKITARIGELKKE--------IKELKKAIEELKKAKGKCPVcgrelte 447

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   773 KHIEAVLEKFDADkdgvvtVNDIRKVLESIGRDNIKLSDKAIE---------ELISLLD-KEQVLQAEQKIEK----AIA 838
Cdd:PRK03918  448 EHRKELLEEYTAE------LKRIEKELKEIEEKERKLRKELRElekvlkkesELIKLKElAEQLKELEEKLKKynleELE 521

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24762654   839 KSMKEAEKLKSEVDKADKDLSKLVNDIhdsaKEIQDIANEMRDKEETVPDKAKELK 894
Cdd:PRK03918  522 KKAEEYEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELA 573
PRK11281 PRK11281
mechanosensitive channel MscK;
545-882 3.03e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   545 KEQSSVSETDKGIsstdVQLLSEALKTLS----SDKQLVVEKETIKELKEELADYKEDVEELREVRQVVKEPVRESRAAK 620
Cdd:PRK11281   49 NKQKLLEAEDKLV----QQDLEQTLALLDkidrQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   621 LLYNRVNKMISQLDNVLNDLEA-------RQHQIKQAESSDYAASSPTvepQQmvhidelvatIRRMKEASDEERFKVVG 693
Cdd:PRK11281  125 QLESRLAQTLDQLQNAQNDLAEynsqlvsLQTQPERAQAALYANSQRL---QQ----------IRNLLKGGKVGGKALRP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   694 DLLVKLDADKDGVisvneitkavqsidrEATNIDKKQLEEFTELLSKLASRRRHEEIVHIDDLMNNIKVLKETSDEARLK 773
Cdd:PRK11281  192 SQRVLLQAEQALL---------------NAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLT 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   774 HIEAVLEKFDADKDGVVTVND--IRKVLESigrdNIKLSD---KAIEELISL----------LDKeqVLQAEQKIEKAIA 838
Cdd:PRK11281  257 LSEKTVQEAQSQDEAARIQANplVAQELEI----NLQLSQrllKATEKLNTLtqqnlrvknwLDR--LTQSERNIKEQIS 330

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24762654   839 ---KSM-------KEAEKLKSevDKADKDLSKlvnDIHDSAKEIQDIaNEMRDK 882
Cdd:PRK11281  331 vlkGSLllsrilyQQQQALPS--ADLIEGLAD---RIADLRLEQFEI-NQQRDA 378
PTZ00121 PTZ00121
MAEBL; Provisional
 566-912 3.98e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   566 SEALKTLSSDKQLVVEKETIKELKEELADYKEDVEELREVRQVvKEPVRESRAAKLLYNRVNKMISQLDNVLNDLEARQH 645
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKA-EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA 1172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   646 QikQAESSDYAASSPTVEPQQMVHIDElvaTIRRMKEASDEERFKVVGDLLVKLDADK-DGVISVNEITKAVQSIDREAT 724
Cdd:PTZ00121 1173 E--DAKKAEAARKAEEVRKAEELRKAE---DARKAEAARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEE 1247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   725 NIDKKQLEEFTELLSKLASRR----RHEEIVHIDDLMNNIKVLKetSDEARLKHIEAVLEKFDADKDGVVTVNDIRKVLE 800
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRqaaiKAEEARKADELKKAEEKKK--ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   801 SIGRDNIKLSDKAIEelislldKEQVLQAEQKIEKAIAKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDiANEMR 880
Cdd:PTZ00121 1326 EAKKKADAAKKKAEE-------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAK 1397

                         330       340       350
                  ....*....|....*....|....*....|..
gi 24762654   881 DKEETVPDKAKELKAEPAFKDTAKTLKDNAKD 912
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 774-823 4.32e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.45  E-value: 4.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24762654  774 HIEAVLEKFDADKDGVVTVNDIRKVLESIGRDnikLSDKAIEELISLLDK 823
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEG---LSEEEIDEMIREVDK 47
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
698-823 6.83e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654  698 KLDADKDGVISVNEITKAVQSIDREA-----TNIDKK-QLEEFTELLSKLASRRRHEEIvhiddlmnnikvlketsdear 771
Cdd:COG5126   13 LLDADGDGVLERDDFEALFRRLWATLfseadTDGDGRiSREEFVAGMESLFEATVEPFA--------------------- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24762654  772 lkhiEAVLEKFDADKDGVVTVNDIRKVLESIGrdnikLSDKAIEELISLLDK 823
Cdd:COG5126   72 ----RAAFDLLDTDGDGKISADEFRRLLTALG-----VSEEEADELFARLDT 114
LETM1_rel_film NF040639
LETM1-related biofilm-associated protein; This bacterial protein family is related to the ...
 219-268 8.62e-04

LETM1-related biofilm-associated protein; This bacterial protein family is related to the mitochondrial protein LETM1. The founding member, WP_060382447 from the fish pathogen Flavobacterium columnare, called a calcium-binding EF hand protein, was found highly up-regulated in expression during biofilm formation.


Pssm-ID: 468607  Cd Length: 396  Bit Score: 42.95  E-value: 8.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24762654   219 LTRRENKQLQRTTSDLFRLIPfSVFI-IVPFMELLLPLFIKFFPGMLPSTF 268
Cdd:NF040639  341 LNDEEKKKVKKQLLDIFKSIP-SLAIfLLPGGALLLPILIKFIPKLLPSAF 390
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
582-917 1.49e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   582 KETIKELKEELADYKEDVEELREVRQVVKEPVRESRAAKL-LYNRVNKMISQLDnvLNDLEARQHQIKQAESSDYAASSP 660
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEeLEEERDDLLAEAG--LDDADAEAVEARREELEDRDEELR 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   661 TVEPQQMVHIDELVATIRRMKEASD--EERFKVV----GDLLVKLDADKDGV----ISVNEITKAVQSIdREATNIDKKQ 730
Cdd:PRK02224  328 DRLEECRVAAQAHNEEAESLREDADdlEERAEELreeaAELESELEEAREAVedrrEEIEELEEEIEEL-RERFGDAPVD 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   731 LEEFTELLSKLASRRrheeivhiDDLMNnikvlKETSDEARLKHIEAVLEKFDADKDGVVTVNDIRKVLESIGRDNIKLS 810
Cdd:PRK02224  407 LGNAEDFLEELREER--------DELRE-----REAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEED 473

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   811 DKAIEELISLLD--KEQVLQAEQKIEKAiaKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDIANEMRDKEETVPD 888
Cdd:PRK02224  474 RERVEELEAELEdlEEEVEEVEERLERA--EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551

                         330       340       350
                  ....*....|....*....|....*....|....
gi 24762654   889 KAKE-----LKAEPAFKDTAKTLKDNAKDLDDLA 917
Cdd:PRK02224  552 EAEEkreaaAEAEEEAEEAREEVAELNSKLAELK 585
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 575-907 1.85e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.41  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    575 DKQLVVEKETIKELKEELADYKEDVEELREVRQVV--------KEPVRESRAAKLLYNRVNKMISQLDNVLNDLEARQHQ 646
Cdd:pfam15921  348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkreKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    647 IKQAESSDYAASSPTV--EPQQMVHID------ELVATIRRMKEASDEERFKVVGDLLVKLDADKDGVISVNEITKAVQS 718
Cdd:pfam15921  428 VQRLEALLKAMKSECQgqMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    719 IDR--EATNIDKKQLEEFTEL-LSKLASRRRHEEivHIDDLMNNIKVL------KETSDEARLKHIEAV----------- 778
Cdd:pfam15921  508 KERaiEATNAEITKLRSRVDLkLQELQHLKNEGD--HLRNVQTECEALklqmaeKDKVIEILRQQIENMtqlvgqhgrta 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    779 ----LEKFDADKDgvvtVNDIRKVLES--IGRDNIKLSDKAIEELISLLDKEQV--LQAEQKIEKAIAKSMKEAEKLKSE 850
Cdd:pfam15921  586 gamqVEKAQLEKE----INDRRLELQEfkILKDKKDAKIRELEARVSDLELEKVklVNAGSERLRAVKDIKQERDQLLNE 661

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24762654    851 VDKADKDLSKLVNDIHDSAKEIQDIANEMrdkeETVPDKAK-ELK-AEPAFKDTAKTLK 907
Cdd:pfam15921  662 VKTSRNELNSLSEDYEVLKRNFRNKSEEM----ETTTNKLKmQLKsAQSELEQTRNTLK 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 582-898 1.98e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    582 KETIKELKEELADYKEDVEELR-EVRQVVKEPVRESRAAKLLYNRVNKMISQLDNVLNDLEARQHQIKQAEssdyaassp 660
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE--------- 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    661 tvepQQMVHIDELVATIRRMKEASDEERfkvvgdllVKLDADKDGV-ISVNEITKAVQSIDREATNIDkkqlEEFTELLS 739
Cdd:TIGR02168  761 ----AEIEELEERLEEAEEELAEAEAEI--------EELEAQIEQLkEELKALREALDELRAELTLLN----EEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    740 KLAS--RRRHEEIVHIDDLMNNIKVLKEtsdeaRLKHIEAVLEKFDADKDgvvtvnDIRKVLESIGrdniKLSDKAIEEL 817
Cdd:TIGR02168  825 RLESleRRIAATERRLEDLEEQIEELSE-----DIESLAAEIEELEELIE------ELESELEALL----NERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654    818 ISLLDKEQVLQAE-QKIEKAIAKSMKEAEKLKSEVDKADKDLSKLVNDIhdsaKEIQD-IANEMRDKEETVPDKAKELKA 895
Cdd:TIGR02168  890 ALLRSELEELSEElRELESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQErLSEEYSLTLEEAEALENKIED 965


                   ...
gi 24762654    896 EPA 898
Cdd:TIGR02168  966 DEE 968
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
537-919 2.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   537 GSQDLLDHKeQSSVSETDKGISSTDVQLLSEALKTLSSD--------KQLVVEKETIKELKEELADYKEDVEELREVRQV 608
Cdd:PRK02224  177 GVERVLSDQ-RGSLDQLKAQIEEKEEKDLHERLNGLESElaeldeeiERYEEQREQARETRDEADEVLEEHEERREELET 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   609 VKEPVRESRAAKLLYNR----VNKMISQLDNVLNDLEARQHQIKqAESSDYAASSPTVEpqqmVHIDELVATIRRMKEAS 684
Cdd:PRK02224  256 LEAEIEDLRETIAETERereeLAEEVRDLRERLEELEEERDDLL-AEAGLDDADAEAVE----ARREELEDRDEELRDRL 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   685 DEERfkvvgdllvkLDADKDGvisvNEITKAVQSIDREATNIDKKQlEEFTELLSKLAS-----RRRHEEIVHIDDlmnN 759
Cdd:PRK02224  331 EECR----------VAAQAHN----EEAESLREDADDLEERAEELR-EEAAELESELEEareavEDRREEIEELEE---E 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   760 IKVLKETSDEA--RLKHIEAVLEKFDADKDGVVT-VNDIRKVLESIgrdniklsDKAIEELISLLDKEQVLQAEQKIEKA 836
Cdd:PRK02224  393 IEELRERFGDApvDLGNAEDFLEELREERDELRErEAELEATLRTA--------RERVEEAEALLEAGKCPECGQPVEGS 464

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   837 ------------IAKSMKEAEKLKSEVDKADKDLSKLVnDIHDSAKEIQDIANEMRDKEETVPDKAKELKAEpafKDTAK 904
Cdd:PRK02224  465 phvetieedrerVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEK---RERAE 540

                         410
                  ....*....|....*
gi 24762654   905 TLKDNAKDLDDLAKD 919
Cdd:PRK02224  541 ELRERAAELEAEAEE 555
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 723-896 2.32e-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: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654  723 ATNIDKKQLEEFTELLSKLAS-RRRHEEI-VHIDDLMNNIKVLKETSDEARLKHIEAVLEKFDADkdgvvtvNDIRKVLE 800
Cdd:COG1579    1 AMPEDLRALLDLQELDSELDRlEHRLKELpAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-------LEIEEVEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654  801 SIGRDNIKLSD-KAIEELISLLDKEQVLQAEQ-KIEKAIAKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDIANE 878
Cdd:COG1579   74 RIKKYEEQLGNvRNNKEYEALQKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153

                        170
                 ....*....|....*...
gi 24762654  879 MRDKEETVPDKAKELKAE 896
Cdd:COG1579  154 LEAELEELEAEREELAAK 171
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 697-879 3.43e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.82  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654  697 VKLDADKDGVISVNEITKAVQSIDREATNIDKKQLEEFTELLSKLasrrrheeivhIDDLMNNIKVLKETSDEARlKHIE 776
Cdd:cd22656   78 IYNYAQNAGGTIDSYYAEILELIDDLADATDDEELEEAKKTIKAL-----------LDDLLKEAKKYQDKAAKVV-DKLT 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654  777 AVLEKFDADKDGVVTVNDirKVLESIGRDNIKLSDKAIEELISLLDKEQvlqaeqkieKAIAKSMKEA-EKLKSEVDKAD 855
Cdd:cd22656  146 DFENQTEKDQTALETLEK--ALKDLLTDEGGAIARKEIKDLQKELEKLN---------EEYAAKLKAKiDELKALIADDE 214

                        170       180
                 ....*....|....*....|....*..
gi 24762654  856 KDLS---KLVNDIHDSAKEIQDIANEM 879
Cdd:cd22656  215 AKLAaalRLIADLTAADTDLDNLLALI 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
582-896 5.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   582 KETIKELKEELADYKEDVEELREVRQ---VVKEPVRESRAAKLL------YNRVNKMISQLDNVLNDLEARQHQIKQAES 652
Cdd:PRK03918  411 TARIGELKKEIKELKKAIEELKKAKGkcpVCGRELTEEHRKELLeeytaeLKRIEKELKEIEEKERKLRKELRELEKVLK 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   653 SDYAASSPTVEPQQMVHIDELVATIRRMKEASDEERFKVVGDLLVKLDADkdgVISVNEITKAVQSIDREATNIDKKqLE 732
Cdd:PRK03918  491 KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE---IKSLKKELEKLEELKKKLAELEKK-LD 566

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   733 EFTELLSKLASRRRHEEIVHIDDLMNNIKVLKETSDE-ARLKHIEAVLE-KFDADKDGVVTVNDIRKVLESIGRDNIKLS 810
Cdd:PRK03918  567 ELEEELAELLKELEELGFESVEELEERLKELEPFYNEyLELKDAEKELErEEKELKKLEEELDKAFEELAETEKRLEELR 646

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   811 dKAIEELISLLDKEQVLQAEQKIEK------AIAKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDIaNEMRDKEE 884
Cdd:PRK03918  647 -KELEELEKKYSEEEYEELREEYLElsrelaGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVE 724

                         330
                  ....*....|..
gi 24762654   885 TVPDKAKELKAE 896
Cdd:PRK03918  725 ELREKVKKYKAL 736
PRK01156 PRK01156
chromosome segregation protein; Provisional
 552-908 5.49e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   552 ETDKGISSTDVQ---LLSEALKTLSSDKQLVVEKETIKEL----------KEELADYKEDVEELR----EVRQVVKEPVR 614
Cdd:PRK01156  139 EMDSLISGDPAQrkkILDEILEINSLERNYDKLKDVIDMLraeisnidylEEKLKSSNLELENIKkqiaDDEKSHSITLK 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   615 ESRAAKLLYNRVNKMISQLDNVLNDLEARQHQIKQAES----SDYAASSPTVEPQQMVHIDELVATIRRMKEASDEER-- 688
Cdd:PRK01156  219 EIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESeiktAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYin 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   689 --FKVVGDL------LVKLDADkdgVISVNEITK--AVQSIDREATNIDKKQLEEFTELLSKLasRRRHEEIVhidDLMN 758
Cdd:PRK01156  299 dyFKYKNDIenkkqiLSNIDAE---INKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILEL--EGYEMDYN---SYLK 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   759 NIKVLKETSDEARLKHIEAVLEKFDADKDGVVTVNDIRKVLESIGRDNIKLSDK----------------AIEELISLLD 822
Cdd:PRK01156  371 SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKvsslnqriralrenldELSRNMEMLN 450

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   823 KEQVLQ------AEQKIEKAIAKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDIANEMRDKEETVPDKAKELKAE 896
Cdd:PRK01156  451 GQSVCPvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD 530

                         410
                  ....*....|...
gi 24762654   897 -PAFKDTAKTLKD 908
Cdd:PRK01156  531 lEDIKIKINELKD 543
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 669-878 6.54e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.59  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   669 HIDELVATIRRMKEASDEERFKVVGDL---LVKLDADKDG----VISVNEITKAVQSIDREATNIDKKQLEEFTELLSKL 741
Cdd:PTZ00440  953 KINNLKMQIEKTLEYYDKSKENINGNDgthLEKLDKEKDEwehfKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELIDKL 1032

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24762654   742 ASRRRHEEIVHIDdlmNNIKVLKETSDEARLKHIEavlekfdadkdgvvtvNDIRKVLESIGRDNIKLSDKAIEELISLL 821
Cdd:PTZ00440 1033 IKEKGKEIEEKVD---QYISLLEKMKTKLSSFHFN----------------IDIKKYKNPKIKEEIKLLEEKVEALLKKI 1093

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24762654   822 D--KEQVLQAEQKIEKAIAKSMKEAEKLKSEVDKADKDLSKLVNDIHDSAKEIQDIANE 878
Cdd:PTZ00440 1094 DenKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLE 1152
 
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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