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Conserved domains on  [gi|305855043|ref|NP_001182240|]
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cortactin-binding protein 2 [Ovis aries]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
36-180 1.84e-48

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


:

Pssm-ID: 430779 [Multi-domain]  Cd Length: 188  Bit Score: 171.25  E-value: 1.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGR-FNLNDPFLALQRDYEAGA----SDKEKKPVCTNPLS 109
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKtKQLLLEARYGFkYPLSDPLQALQRDSELLRgtsqDEEVYEAMYEKPLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   110 ILEAVMAHCRKMQERMSTQLAAAESRQKK------------------------------------LEMEKLQLQALEQEH 153
Cdd:pfam09727   82 ELEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKEL 161
                          170       180
                   ....*....|....*....|....*..
gi 305855043   154 KKLAARLEEERGKNKHVVLMLVKECKQ 180
Cdd:pfam09727  162 KKLLEKLEEELSRQKQIALLLVKERKR 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
741-828 2.69e-24

Ankyrin repeats (3 copies);


:

Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 98.27  E-value: 2.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   741 LYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYdANINhAADGGQTPLYLACKNGNKECIK 820
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 305855043   821 LLLEAGTD 828
Cdd:pfam12796   79 LLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
632-826 4.46e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 88.34  E-value: 4.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  632 WPAETPGLNQPACSESSLVIpTTTAFRSSINPVSASSRRAGASDSLLVTASGWSPSLTPLLMSGGP--APLAGRPTLLQQ 709
Cdd:COG0666     1 SKPSLSALLLINKCFLDLLL-VALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVDRHlaARDLDGRLPLHS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  710 AAAQGNVTLLSmLLNEEGLDINYSCEDGHSALYSAAKNGHT-----DCVRLLLNAEAQ---VNAADKNGFTPLCAAAAQG 781
Cdd:COG0666    80 AASKGDDKIVK-LLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADldvNNLRDEDGNTPLHWAALNG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 305855043  782 HFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAG 826
Cdd:COG0666   159 DADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKG 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
807-935 1.32e-14

Ankyrin repeats (3 copies);


:

Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 70.54  E-value: 1.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   807 LYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHgapahgnklqeepglaiFDLDqeehheg 886
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----------------ADVN------- 56
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 305855043   887 tskpvvpadlinhADSEGWTAAHIAASKGFKNCLEVLCRHgGLEPERRD 935
Cdd:pfam12796   57 -------------LKDNGRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
128-271 2.69e-10

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 63.78  E-value: 2.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkhVVLMLVKECKQLSG--------KVLEEAQKLEEVMAKL 199
Cdd:pfam13868   90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR-----QLREEIDEFNEEQAkwkelekeEEKEEDLRILEYLKEK 164
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   200 EEEKKKTSALEEELATEK-RRSAEMEAQMEKQLSEFDtEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam13868  165 AEREEEREAERREIKEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKWRQKEREEAEKKARQRQE 236
PHA03247 super family cl33720
large tegument protein UL36; Provisional
271-706 4.24e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  271 RGNDSKPSLSLPRKTKDR-RLVSISVATEGPMTRS----VACQTDLVTETAEPLKKLPLTVPVKPAAGSPLVSASAKGNA 345
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAarptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  346 CASAASvrpgierqvshgdligsslPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTVSPASG---HTPTPPPHSLHS 422
Cdd:PHA03247 2733 PALPAA-------------------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprRLTRPAVASLSE 2793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  423 PCANAPLHPGLNPRIQAArfrfQGSNANDPDQNGNTTQSPPSRDVSPTsrdtlvAKQLARNTVTQALSrftsppagapPR 502
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAV----LAPAAALPPAASPAGPLPPPTSAQPT------APPPPPGPPPPSLP----------LG 2853
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  503 PGAPPTGDVGTYPPVGRTSLK--TPGGARVDRGNPPPIPPKKPGLSQTPSPPHPQlkvimdssrasstgikadnKTVASS 580
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQPERP-------------------PQPQAP 2914
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  581 PSSLPQgnrviNEENLSKSSSPQLPPKPSIDLTVAPagcavsalatsQVGAWPAETPGLNQPACSESSLVIPTTTAFRSS 660
Cdd:PHA03247 2915 PPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAP-----------TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 305855043  661 InPVSASSRRAGAS------DSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 706
Cdd:PHA03247 2979 V-PQPAPSREAPASstppltGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
PRK11331 super family cl32675
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
1070-1359 3.21e-06

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


The actual alignment was detected with superfamily member PRK11331:

Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 51.62  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1070 NKAEQVTVLLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCLKHRQMaagfPCEIV 1149
Cdd:PRK11331  153 NSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA----PQRVN 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1150 RAEVDADFSKEQLV-------------DLFISSACLiPVKQSPaNKKIIIILENLEKSSLSELLGDFLGPLEN----HST 1212
Cdd:PRK11331  229 MVQFHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENW 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1213 ESPCTFQKGNgmSECYYFHENCFLMGTI--AKACLQGSDLLVQQHFRWVqlrwDSEPmqGLLQRFLRRKVVNKfrGQVPS 1290
Cdd:PRK11331  307 SVPLTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPS 376
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 1291 PCDPVCKTVDwalavwrQLNSCLARLGTpeaLLGPKY-----FLSCPVIPGHAQATvKWMSKLWNAVIAPRVQE 1359
Cdd:PRK11331  377 FVESLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
36-180 1.84e-48

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 430779 [Multi-domain]  Cd Length: 188  Bit Score: 171.25  E-value: 1.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGR-FNLNDPFLALQRDYEAGA----SDKEKKPVCTNPLS 109
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKtKQLLLEARYGFkYPLSDPLQALQRDSELLRgtsqDEEVYEAMYEKPLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   110 ILEAVMAHCRKMQERMSTQLAAAESRQKK------------------------------------LEMEKLQLQALEQEH 153
Cdd:pfam09727   82 ELEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKEL 161
                          170       180
                   ....*....|....*....|....*..
gi 305855043   154 KKLAARLEEERGKNKHVVLMLVKECKQ 180
Cdd:pfam09727  162 KKLLEKLEEELSRQKQIALLLVKERKR 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
741-828 2.69e-24

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 98.27  E-value: 2.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   741 LYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYdANINhAADGGQTPLYLACKNGNKECIK 820
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 305855043   821 LLLEAGTD 828
Cdd:pfam12796   79 LLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
632-826 4.46e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 88.34  E-value: 4.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  632 WPAETPGLNQPACSESSLVIpTTTAFRSSINPVSASSRRAGASDSLLVTASGWSPSLTPLLMSGGP--APLAGRPTLLQQ 709
Cdd:COG0666     1 SKPSLSALLLINKCFLDLLL-VALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVDRHlaARDLDGRLPLHS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  710 AAAQGNVTLLSmLLNEEGLDINYSCEDGHSALYSAAKNGHT-----DCVRLLLNAEAQ---VNAADKNGFTPLCAAAAQG 781
Cdd:COG0666    80 AASKGDDKIVK-LLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADldvNNLRDEDGNTPLHWAALNG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 305855043  782 HFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAG 826
Cdd:COG0666   159 DADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKG 203
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-863 1.08e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 84.11  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  701 AGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQ 780
Cdd:COG0666    37 KKLNLYLELALLPAASLSELLLKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  781 GHFK-----CVELLI---AYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSL 852
Cdd:COG0666   117 GNPPegnieVAKLLLeagADLDVNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELV 196
                         170
                  ....*....|.
gi 305855043  853 KLLMYHGAPAH 863
Cdd:COG0666   197 KLLLDKGLHLS 207
PHA03095 PHA03095
ankyrin-like protein; Provisional
706-866 1.69e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  706 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLNAEAQVNAADKNGFTPL-CAAAAQ 780
Cdd:PHA03095   15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  781 GHFKCVELLIAYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVD--SLKLLM 856
Cdd:PHA03095   95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLI 174
                         170
                  ....*....|
gi 305855043  857 YHGAPAHGNK 866
Cdd:PHA03095  175 DAGADVYAVD 184
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
710-941 1.36e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.61  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  710 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELL 789
Cdd:PLN03192  532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  790 IAYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGAPA-HGNKLQ 868
Cdd:PLN03192  611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDD 688
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  869 EEPGLAIFDLDQEEH--HEGTSKPVVPADLINHADSEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTA 941
Cdd:PLN03192  689 DFSPTELRELLQKRElgHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEA 763
Ank_2 pfam12796
Ankyrin repeats (3 copies);
807-935 1.32e-14

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 70.54  E-value: 1.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   807 LYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHgapahgnklqeepglaiFDLDqeehheg 886
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----------------ADVN------- 56
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 305855043   887 tskpvvpadlinhADSEGWTAAHIAASKGFKNCLEVLCRHgGLEPERRD 935
Cdd:pfam12796   57 -------------LKDNGRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
39-270 3.02e-12

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 72.05  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   39 SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRfnLNDPFLALQRDYEagasDKEKKpvctnpLSILEAVMAHC 118
Cdd:COG1196   249 SRLEEELEELQEELEEAEKEIEELKSELEE--LREELEE--LQEELLELKEEIE----ELEGE------ISLLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEE 194
Cdd:COG1196   315 ENELEELEERLEELKEKiealKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAE 394
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196   395 IRNELEELKREIESLEERLERLSERLEDLKEElkeLEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQ 473
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
30-271 2.60e-10

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: 65.47  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGASDKEKkpvct 105
Cdd:TIGR02169  167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEK----- 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   106 nplsilEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARL----EEERGKNKHVVLMLVKECKQL 181
Cdd:TIGR02169  233 ------EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGELEAEIASL 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   182 SGKV---LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEE 258
Cdd:TIGR02169  307 ERSIaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
                          250
                   ....*....|...
gi 305855043   259 IDKMKKMIEQLKR 271
Cdd:TIGR02169  387 LKDYREKLEKLKR 399
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
128-271 2.69e-10

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 63.78  E-value: 2.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkhVVLMLVKECKQLSG--------KVLEEAQKLEEVMAKL 199
Cdd:pfam13868   90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR-----QLREEIDEFNEEQAkwkelekeEEKEEDLRILEYLKEK 164
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   200 EEEKKKTSALEEELATEK-RRSAEMEAQMEKQLSEFDtEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam13868  165 AEREEEREAERREIKEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKWRQKEREEAEKKARQRQE 236
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
108-322 3.33e-10

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.12  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  108 LSILEAVMAHCRKMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLaaRLEEERGKNKHVVLMLVKECKQLSGKVLE 187
Cdd:COG1196   188 LERLEDLLEELEKQLEKLERQAEKAE-RYQELKAELRELELALLLAKLK--ELRKELEELEEELSRLEEELEELQEELEE 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAhttdLKEEIDKMKKMIE 267
Cdd:COG1196   265 AEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEE----LKEKIEALKEELE 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  268 ----QLKRGNDSKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKKL 322
Cdd:COG1196   341 eretLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNEL 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-271 5.96e-10

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: 64.31  E-value: 5.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   115 MAHCRKMQERMSTQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKHVVLMLVKECKQLSGKVLEEAQK 191
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   192 LEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAK-----LHREEAHTT-----DLKEEIDK 261
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLrerleSLERRIAA 835
                          170
                   ....*....|
gi 305855043   262 MKKMIEQLKR 271
Cdd:TIGR02168  836 TERRLEDLEE 845
PTZ00121 PTZ00121
MAEBL; Provisional
51-298 1.15e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   51 ELEARDLVIEALRARRKEvfiqerygrfnlNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMA-HCRKMQERM--ST 127
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAE------------EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeEAKKAEEAKikAE 1623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  128 QLAAAESRQKKLEmeklQLQALEQEHKKLAARLEEERGKNKhvvlmlVKEcKQLSGKVLEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PTZ00121 1624 ELKKAEEEKKKVE----QLKKKEAEEKKKAEELKKAEEENK------IKA-AEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  208 ALEEElaTEKRRSAEmeaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1693 ALKKE--AEEAKKAE---ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
                         250
                  ....*....|.
gi 305855043  288 RRLVSISVATE 298
Cdd:PTZ00121 1768 KKAEEIRKEKE 1778
Ank_2 pfam12796
Ankyrin repeats (3 copies);
705-767 1.24e-09

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 56.67  E-value: 1.24e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   705 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAAD 767
Cdd:pfam12796   32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00121 PTZ00121
MAEBL; Provisional
89-287 3.42e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.08  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   89 RDYEAGASDKEKKPVCTNPLSILEAVMAHCRKMQERMStqlaaAESRQKKLEMEKlqlqaLEQEHKKLAARLEEERGKnk 168
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK-----AEEARKADELKK-----AEEKKKADEAKKAEEKKK-- 1303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  169 hvvlmlVKECKqlsgKVLEEAQKLEEVMAKLEEEKKKTSALEEElATEKRRSAEM-EAQMEKQLSEFDTEREQLRA-KLH 246
Cdd:PTZ00121 1304 ------ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAaKAEAEAAADEAEAAEEKAEAaEKK 1372
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 305855043  247 REEAhttdlKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1373 KEEA-----KKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
PHA03247 PHA03247
large tegument protein UL36; Provisional
271-706 4.24e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  271 RGNDSKPSLSLPRKTKDR-RLVSISVATEGPMTRS----VACQTDLVTETAEPLKKLPLTVPVKPAAGSPLVSASAKGNA 345
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAarptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  346 CASAASvrpgierqvshgdligsslPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTVSPASG---HTPTPPPHSLHS 422
Cdd:PHA03247 2733 PALPAA-------------------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprRLTRPAVASLSE 2793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  423 PCANAPLHPGLNPRIQAArfrfQGSNANDPDQNGNTTQSPPSRDVSPTsrdtlvAKQLARNTVTQALSrftsppagapPR 502
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAV----LAPAAALPPAASPAGPLPPPTSAQPT------APPPPPGPPPPSLP----------LG 2853
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  503 PGAPPTGDVGTYPPVGRTSLK--TPGGARVDRGNPPPIPPKKPGLSQTPSPPHPQlkvimdssrasstgikadnKTVASS 580
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQPERP-------------------PQPQAP 2914
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  581 PSSLPQgnrviNEENLSKSSSPQLPPKPSIDLTVAPagcavsalatsQVGAWPAETPGLNQPACSESSLVIPTTTAFRSS 660
Cdd:PHA03247 2915 PPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAP-----------TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 305855043  661 InPVSASSRRAGAS------DSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 706
Cdd:PHA03247 2979 V-PQPAPSREAPASstppltGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
705-841 5.01e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQ-VNAADKN----GFTPLCAAAA 779
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  780 QGHFKCVELLIAYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTDrsVKTRDGW--TPIH 841
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
1070-1359 3.21e-06

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 51.62  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1070 NKAEQVTVLLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCLKHRQMaagfPCEIV 1149
Cdd:PRK11331  153 NSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA----PQRVN 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1150 RAEVDADFSKEQLV-------------DLFISSACLiPVKQSPaNKKIIIILENLEKSSLSELLGDFLGPLEN----HST 1212
Cdd:PRK11331  229 MVQFHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENW 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1213 ESPCTFQKGNgmSECYYFHENCFLMGTI--AKACLQGSDLLVQQHFRWVqlrwDSEPmqGLLQRFLRRKVVNKfrGQVPS 1290
Cdd:PRK11331  307 SVPLTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPS 376
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 1291 PCDPVCKTVDwalavwrQLNSCLARLGTpeaLLGPKY-----FLSCPVIPGHAQATvKWMSKLWNAVIAPRVQE 1359
Cdd:PRK11331  377 FVESLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
803-828 1.79e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.79e-05
                            10        20
                    ....*....|....*....|....*.
gi 305855043    803 GQTPLYLACKNGNKECIKLLLEAGTD 828
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
707-844 2.95e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   707 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGHtDCVRLLLNAEAQ----------VNAADKNGF----T 772
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAafrksgplelANDQYTSEFtpgiT 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   773 PLCAAAAQGHFKCVELLIAYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTDrsVKTRD--G 836
Cdd:TIGR00870  131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208

                   ....*...
gi 305855043   837 WTPIHAAV 844
Cdd:TIGR00870  209 NTLLHLLV 216
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
319-723 6.87e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 6.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   319 LKKLPLTVPVKPAAGSPLVSASAKGNACASAASVRPGIERQVSHGDLIGSSLPTVPPPStdrieenGPSTGSTPdLTSSP 398
Cdd:pfam05109  421 FSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPA-------GTTSGASP-VTPSP 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   399 T--------ALPSTVSPASG-HTPTP----PPHSLHSPCANAPlHPGLNPRIQAARFRFQGSNANDPDQnGNTTQSPPSR 465
Cdd:pfam05109  493 SprdngtesKAPDMTSPTSAvTTPTPnatsPTPAVTTPTPNAT-SPTLGKTSPTSAVTTPTPNATSPTP-AVTTPTPNAT 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   466 -----DVSPTSRDTLVAKQLARNTVTQAlsrfTSPPAGAPPRPGAPPTGDVGTYPPVGRTSLKTPGGARVDRGNPPPIPP 540
Cdd:pfam05109  571 iptlgKTSPTSAVTTPTPNATSPTVGET----SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSL 646
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   541 KKPGLSQTPSP---------------PHPQ-LKVIMDSSRASSTGIKADNKTVASSPSSLPQ----GNRVIN----EENL 596
Cdd:pfam05109  647 RPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEVNV 726
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   597 SKSSSPQ---LPPKPSIDLTVAPAGCAVSALATSQVGAwpAETPGLNQPACSEsslviPTTTAFRSSINPVSassrRAGA 673
Cdd:pfam05109  727 TKGTPPKnatSPQAPSGQKTAVPTVTSTGGKANSTTGG--KHTTGHGARTSTE-----PTTDYGGDSTTPRT----RYNA 795
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   674 SDSLLVTASG-----WSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 723
Cdd:pfam05109  796 TTYLPPSTSSklrprWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
735-915 3.40e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  735 EDGHSALYSAA---KNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGH-----------FKCVELLIAYDANINHAA 800
Cdd:cd21882    24 ATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADVSARA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  801 DG-------------GQTPLYLACKNGNKECIKLLLEAGTD-RSVKTRD--GWTPIHAAVDTGN--VDSLKLL--MYHGA 860
Cdd:cd21882   104 TGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYNLL 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  861 PAHGNKLQeepglaifdldqeehhegtskPVVPADLI-NHadsEGWTAAHIAASKG 915
Cdd:cd21882   184 LSYGAHLD---------------------PTQQLEEIpNH---QGLTPLKLAAVEG 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
835-860 6.88e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 6.88e-04
                            10        20
                    ....*....|....*....|....*.
gi 305855043    835 DGWTPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
NOPS_NONA_like cd12945
NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from ...
199-242 6.93e-04

NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from invertebrate species; The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension , found in Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA), Chironomus tentans hrp65 gene encoding protein Hrp65 and similar proteins. D. melanogaster NONA is involved in eye development and behavior, and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies.


Pssm-ID: 240580 [Multi-domain]  Cd Length: 100  Bit Score: 40.42  E-value: 6.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 305855043  199 LEEEKKKTSALEEELATEKRRsaeMEAQMEKQLSEFDTE--REQLR 242
Cdd:cd12945    58 HELYKQKEEALKRELKMEEEK---LEAQMEYARYEHETEllREQLR 100
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
119-168 1.78e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 37.91  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 305855043  119 RKMQERMstqlAAAESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 168
Cdd:cd14686     4 RRERNRE----AARRSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
36-180 1.84e-48

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 430779 [Multi-domain]  Cd Length: 188  Bit Score: 171.25  E-value: 1.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGR-FNLNDPFLALQRDYEAGA----SDKEKKPVCTNPLS 109
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKtKQLLLEARYGFkYPLSDPLQALQRDSELLRgtsqDEEVYEAMYEKPLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   110 ILEAVMAHCRKMQERMSTQLAAAESRQKK------------------------------------LEMEKLQLQALEQEH 153
Cdd:pfam09727   82 ELEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKEL 161
                          170       180
                   ....*....|....*....|....*..
gi 305855043   154 KKLAARLEEERGKNKHVVLMLVKECKQ 180
Cdd:pfam09727  162 KKLLEKLEEELSRQKQIALLLVKERKR 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
741-828 2.69e-24

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 98.27  E-value: 2.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   741 LYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYdANINhAADGGQTPLYLACKNGNKECIK 820
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 305855043   821 LLLEAGTD 828
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
707-797 2.71e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.80  E-value: 2.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   707 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNaEAQVNAADkNGFTPLCAAAAQGHFKCV 786
Cdd:pfam12796    1 LMLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|.
gi 305855043   787 ELLIAYDANIN 797
Cdd:pfam12796   78 KLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
774-860 1.72e-20

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 87.49  E-value: 1.72e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   774 LCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGtdRSVKTRDGWTPIHAAVDTGNVDSLK 853
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78

                   ....*..
gi 305855043   854 LLMYHGA 860
Cdd:pfam12796   79 LLLEKGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
632-826 4.46e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 88.34  E-value: 4.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  632 WPAETPGLNQPACSESSLVIpTTTAFRSSINPVSASSRRAGASDSLLVTASGWSPSLTPLLMSGGP--APLAGRPTLLQQ 709
Cdd:COG0666     1 SKPSLSALLLINKCFLDLLL-VALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVDRHlaARDLDGRLPLHS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  710 AAAQGNVTLLSmLLNEEGLDINYSCEDGHSALYSAAKNGHT-----DCVRLLLNAEAQ---VNAADKNGFTPLCAAAAQG 781
Cdd:COG0666    80 AASKGDDKIVK-LLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADldvNNLRDEDGNTPLHWAALNG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 305855043  782 HFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAG 826
Cdd:COG0666   159 DADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKG 203
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
701-863 1.08e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 84.11  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  701 AGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQ 780
Cdd:COG0666    37 KKLNLYLELALLPAASLSELLLKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  781 GHFK-----CVELLI---AYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSL 852
Cdd:COG0666   117 GNPPegnieVAKLLLeagADLDVNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELV 196
                         170
                  ....*....|.
gi 305855043  853 KLLMYHGAPAH 863
Cdd:COG0666   197 KLLLDKGLHLS 207
PHA03095 PHA03095
ankyrin-like protein; Provisional
706-866 1.69e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  706 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLNAEAQVNAADKNGFTPL-CAAAAQ 780
Cdd:PHA03095   15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  781 GHFKCVELLIAYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVD--SLKLLM 856
Cdd:PHA03095   95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLI 174
                         170
                  ....*....|
gi 305855043  857 YHGAPAHGNK 866
Cdd:PHA03095  175 DAGADVYAVD 184
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
710-941 1.36e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.61  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  710 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELL 789
Cdd:PLN03192  532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  790 IAYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGAPA-HGNKLQ 868
Cdd:PLN03192  611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDD 688
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  869 EEPGLAIFDLDQEEH--HEGTSKPVVPADLINHADSEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRTA 941
Cdd:PLN03192  689 DFSPTELRELLQKRElgHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEA 763
PHA03100 PHA03100
ankyrin repeat protein; Provisional
714-860 1.62e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  714 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEAQVNAADKngftplcaaaaqghfkcVELLIA 791
Cdd:PHA03100  119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  792 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02878 PHA02878
ankyrin repeat protein; Provisional
722-860 8.05e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 8.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  722 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAA 800
Cdd:PHA02878  152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043  801 DGGQTPLYLA---CKngNKECIKLLLEAGTDRSVK-TRDGWTPIHAAVDTGnvDSLKLLMYHGA 860
Cdd:PHA02878  232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGA 291
PHA02874 PHA02874
ankyrin repeat protein; Provisional
725-844 1.25e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.08  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  725 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQ 804
Cdd:PHA02874  112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 305855043  805 TPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAV 844
Cdd:PHA02874  192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
807-935 1.32e-14

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 70.54  E-value: 1.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   807 LYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHgapahgnklqeepglaiFDLDqeehheg 886
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----------------ADVN------- 56
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 305855043   887 tskpvvpadlinhADSEGWTAAHIAASKGFKNCLEVLCRHgGLEPERRD 935
Cdd:pfam12796   57 -------------LKDNGRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
705-860 1.70e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  705 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFK 784
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  785 CVELLIAYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTDRSVKTRD--GWTPIHAAVDTG-NVDSLKLLMYHGA 860
Cdd:PHA02874  205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHKA 279
PHA02875 PHA02875
ankyrin repeat protein; Provisional
710-860 4.06e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 4.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  710 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELL 789
Cdd:PHA02875    9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305855043  790 IAYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:PHA02875   88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
PHA03100 PHA03100
ankyrin repeat protein; Provisional
715-860 4.31e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  715 NVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHT-----DCVRLLLNAEAQVNAADKNGFTPLCAAAAQ--GHFKCVE 787
Cdd:PHA03100   47 NIDVVKILLDN-GADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  788 LLIAYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTR--------------D--GWTPIHAAVDTGNV 849
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyllsygvpinikDvyGFTPLHYAVYNNNP 205
                         170
                  ....*....|.
gi 305855043  850 DSLKLLMYHGA 860
Cdd:PHA03100  206 EFVKYLLDLGA 216
PHA02878 PHA02878
ankyrin repeat protein; Provisional
715-860 8.44e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  715 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLNAEAQVNAADKN-GFTPLCAAAAQGHFKCVEL 788
Cdd:PHA02878  113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043  789 LIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDT-GNVDSLKLLMYHGA 860
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGV 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
716-928 1.02e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 69.47  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  716 VTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDcvrLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDAN 795
Cdd:COG0666    22 ALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELL---LKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGAD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  796 INHAADGGQTPLYLACKNGNK-----ECIKLLLEAGTDRSVKTR---DGWTPIHAAVDTGNVDSLKLLMYHGAPahgnkl 867
Cdd:COG0666    99 VNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLDVNNLrdeDGNTPLHWAALNGDADIVELLLEAGAD------ 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043  868 qeepglaifdldqeehhegtskpvvpadlINHADSEGWTAAHIAASKGFKNCLEVLCRHGG 928
Cdd:COG0666   173 -----------------------------PNSRNSYGVTALDPAAKNGRIELVKLLLDKGL 204
PHA02875 PHA02875
ankyrin repeat protein; Provisional
691-860 1.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.56  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  691 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLNAEAQVNA 765
Cdd:PHA02875   53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  766 ADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDG-WTPIHAAV 844
Cdd:PHA02875  131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
                         170
                  ....*....|....*.
gi 305855043  845 DTGNVDSLKLLMYHGA 860
Cdd:PHA02875  211 ENNKIDIVRLFIKRGA 226
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
39-270 3.02e-12

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 72.05  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   39 SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRfnLNDPFLALQRDYEagasDKEKKpvctnpLSILEAVMAHC 118
Cdd:COG1196   249 SRLEEELEELQEELEEAEKEIEELKSELEE--LREELEE--LQEELLELKEEIE----ELEGE------ISLLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEE 194
Cdd:COG1196   315 ENELEELEERLEELKEKiealKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAE 394
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196   395 IRNELEELKREIESLEERLERLSERLEDLKEElkeLEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQ 473
Ank_4 pfam13637
Ankyrin repeats (many copies);
737-790 3.48e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 3.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 305855043   737 GHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLI 790
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
705-859 4.35e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 4.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  705 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LNAEA 761
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  762 QVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIH 841
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                         170
                  ....*....|....*...
gi 305855043  842 AAVDTGNVDSLKLLMYHG 859
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHG 213
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
38-271 4.82e-12

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 71.28  E-value: 4.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   38 KSELRMLlsvmEGELEARDLViealRARRKEVFIQERYGRfnlndpflaLQRDYEAGASDKEKkpvctnplsILEAVMAH 117
Cdd:COG1196   219 KAELREL----ELALLLAKLK----ELRKELEELEEELSR---------LEEELEELQEELEE---------AEKEIEEL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  118 CRKMQE-RMSTQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKHvvlmLVKECKQLSGKVLEEAQKLEE 194
Cdd:COG1196   273 KSELEElREELEELQEELLELKEEIEELegEISLLRERLEELENELEELEERLEE----LKEKIEALKEELEERETLLEE 348
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG1196   349 LEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKE 425
Ank_4 pfam13637
Ankyrin repeats (many copies);
772-823 8.14e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 8.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 305855043   772 TPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLL 823
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
714-865 9.75e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 9.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  714 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLI--- 790
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdng 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  791 ----------------------AYDANINHAADggQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGN 848
Cdd:PHA02874   92 vdtsilpipciekdmiktildcGIDVNIKDAEL--KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169
                         170
                  ....*....|....*..
gi 305855043  849 VDSLKLLMYHGAPAHGN 865
Cdd:PHA02874  170 FDIIKLLLEKGAYANVK 186
PHA03100 PHA03100
ankyrin repeat protein; Provisional
723-860 1.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  723 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGH-----FKCVELLIAYDANIN 797
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  798 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDS--LKLLMYHGA 860
Cdd:PHA03100  101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
37-286 4.64e-11

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 68.20  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   37 SKSELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRF-NLNDPFLALQRDYEAGASDKEKKpvctnpLSILEAVM 115
Cdd:COG1196   703 LLEELRRQLEELERQLEELKRELAALEEELEQ--LQSRLEELeEELEELEEELEELQERLEELEEE------LESLEEAL 774
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  116 AHCRKMQERMSTQLAAAESRQKKLEME----KLQLQALEQE---HKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEE 188
Cdd:COG1196   775 AKLKEEIEELEEKRQALQEELEELEEEleeaERRLDALERElesLEQRRERLEQEIEELEEEIEELEEKLDELEEELEEL 854
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  189 AQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFD---TEREQLRAKLHREEAHTTDLKEEIdkmKKM 265
Cdd:COG1196   855 EKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAelkEEIEKLRERLEELEAKLERLEVEL---PEL 931
                         250       260
                  ....*....|....*....|.
gi 305855043  266 IEQLKRGNDSKPSLSLPRKTK 286
Cdd:COG1196   932 EEELEEEYEDTLETELEREIE 952
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
51-270 2.09e-10

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.89  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   51 ELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagASDKEKKpvCTNPLSILEAVMAHCRKMQERMSTQLA 130
Cdd:COG1196   661 SSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRS-----LEDLLEE--LRRQLEELERQLEELKRELAALEEELE 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALE 210
Cdd:COG1196   734 QLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALE 813
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043  211 EELATEKRRSAEME---AQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196   814 RELESLEQRRERLEqeiEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELE 876
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
30-271 2.60e-10

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: 65.47  E-value: 2.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGASDKEKkpvct 105
Cdd:TIGR02169  167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEK----- 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   106 nplsilEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARL----EEERGKNKHVVLMLVKECKQL 181
Cdd:TIGR02169  233 ------EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGELEAEIASL 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   182 SGKV---LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEE 258
Cdd:TIGR02169  307 ERSIaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
                          250
                   ....*....|...
gi 305855043   259 IDKMKKMIEQLKR 271
Cdd:TIGR02169  387 LKDYREKLEKLKR 399
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
128-271 2.69e-10

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 63.78  E-value: 2.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkhVVLMLVKECKQLSG--------KVLEEAQKLEEVMAKL 199
Cdd:pfam13868   90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR-----QLREEIDEFNEEQAkwkelekeEEKEEDLRILEYLKEK 164
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   200 EEEKKKTSALEEELATEK-RRSAEMEAQMEKQLSEFDtEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam13868  165 AEREEEREAERREIKEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKWRQKEREEAEKKARQRQE 236
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
108-322 3.33e-10

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.12  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  108 LSILEAVMAHCRKMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLaaRLEEERGKNKHVVLMLVKECKQLSGKVLE 187
Cdd:COG1196   188 LERLEDLLEELEKQLEKLERQAEKAE-RYQELKAELRELELALLLAKLK--ELRKELEELEEELSRLEEELEELQEELEE 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAhttdLKEEIDKMKKMIE 267
Cdd:COG1196   265 AEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEE----LKEKIEALKEELE 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  268 ----QLKRGNDSKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKKL 322
Cdd:COG1196   341 eretLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNEL 399
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
51-271 5.86e-10

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 64.40  E-value: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   51 ELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKkpvctnpLSILEAVMAHCRKMQERMSTQLA 130
Cdd:COG0419   243 ELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIER-------LEELEREIEELEEELEGLRALLE 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvkeckqlsgkvlEEAQKLEEVMAKLEEEkkktsalE 210
Cdd:COG0419   316 ELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKN------------------ELAKLLEERLKELEER-------L 370
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  211 EELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKL----HREEAHT---TDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419   371 EELEKELEKALERLKQLEEAIQELKEELAELSAALeeiqEELEELEkelEELERELEELEEEIKKLEE 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
115-271 5.96e-10

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: 64.31  E-value: 5.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   115 MAHCRKMQERMSTQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKHVVLMLVKECKQLSGKVLEEAQK 191
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   192 LEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAK-----LHREEAHTT-----DLKEEIDK 261
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLrerleSLERRIAA 835
                          170
                   ....*....|
gi 305855043   262 MKKMIEQLKR 271
Cdd:TIGR02168  836 TERRLEDLEE 845
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
122-298 9.87e-10

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: 63.55  E-value: 9.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKHVVLML-----------VKECKQLSGKVLEEAQ 190
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKLEEALndlearlshsrIPEIQAELSKLEEEVS 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   191 KLEEVMAKLEEEKKKTSA----LEEELATEKRRSAEMEAQ----------MEKQLSEFDTEREQLRAKLHREEAHTTDLK 256
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLekeyLEKEIQELQEQRIDLKEQiksiekeienLNGKKEELEEELEELEAALRDLESRLGDLK 888
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 305855043   257 EEIDKMKKMIEQLKRG-NDSKPSLSLPRKTKDRRLVSISVATE 298
Cdd:TIGR02169  889 KERDELEAQLRELERKiEELEAQIEKKRKRLSELKAKLEALEE 931
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
37-271 1.12e-09

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.58  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   37 SKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMA 116
Cdd:COG1196   773 ALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE 852
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  117 HCRKMQERMSTQLAAA-------ESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEA 189
Cdd:COG1196   853 ELEKELEELKEELEELeaekeelEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELE 932
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  190 QKLEEvmaklEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEahttDLKEEIDKMKKMIEQL 269
Cdd:COG1196   933 EELEE-----EYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQRE----DLEEAKEKLLEVIEEL 1003

                  ..
gi 305855043  270 KR 271
Cdd:COG1196  1004 DK 1005
PTZ00121 PTZ00121
MAEBL; Provisional
51-298 1.15e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   51 ELEARDLVIEALRARRKEvfiqerygrfnlNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMA-HCRKMQERM--ST 127
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAE------------EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeEAKKAEEAKikAE 1623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  128 QLAAAESRQKKLEmeklQLQALEQEHKKLAARLEEERGKNKhvvlmlVKEcKQLSGKVLEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PTZ00121 1624 ELKKAEEEKKKVE----QLKKKEAEEKKKAEELKKAEEENK------IKA-AEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  208 ALEEElaTEKRRSAEmeaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1693 ALKKE--AEEAKKAE---ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
                         250
                  ....*....|.
gi 305855043  288 RRLVSISVATE 298
Cdd:PTZ00121 1768 KKAEEIRKEKE 1778
Ank_2 pfam12796
Ankyrin repeats (3 copies);
705-767 1.24e-09

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 56.67  E-value: 1.24e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   705 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAAD 767
Cdd:pfam12796   32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
115-271 1.93e-09

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 62.45  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   115 MAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSG----KVLEeaQ 190
Cdd:pfam17380  422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEeqrrKILE--K 499
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   191 KLEEVMAKLEEEKKKTSALEEEL--------ATEKRRSAEMEAQMEKQLSEFDTEREQLRaKLHREEAHTTDLKEEIDKM 262
Cdd:pfam17380  500 ELEERKQAMIEEERKRKLLEKEMeerqkaiyEEERRREAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMEREREMM 578

                   ....*....
gi 305855043   263 KKMIEQLKR 271
Cdd:pfam17380  579 RQIVESEKA 587
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
774-863 2.59e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  774 LCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLK 853
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
                          90
                  ....*....|
gi 305855043  854 LLMYHGAPAH 863
Cdd:PTZ00322  166 LLSRHSQCHF 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
127-321 2.80e-09

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: 62.00  E-value: 2.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   127 TQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKT 206
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   207 S-------ALEEELATEKRRSAEMEAQMEKQlsefDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGND----S 275
Cdd:TIGR02168  347 EelkeeleSLEAELEELEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqqE 422
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 305855043   276 KPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKK 321
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
51-270 3.20e-09

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: 62.00  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    51 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGASDKEKKpvcTNPLSILEAVMAHCRKMQERMSTQLA 130
Cdd:TIGR02168  221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   131 AAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKHV---VLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEK 203
Cdd:TIGR02168  292 ALANEISRLEQQKQILRErlanLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELE 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   204 KKTSALEEELATEKRRSAEMEAQ----------MEKQLSEFDTEREQLRAKL--HREEAHTTDLKE---EIDKMKKMIEQ 268
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQiaslnneierLEARLERLEDRRERLQQEIeeLLKKLEEAELKElqaELEELEEELEE 451

                   ..
gi 305855043   269 LK 270
Cdd:TIGR02168  452 LQ 453
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
119-271 3.34e-09

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 60.31  E-value: 3.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAESRQKKLEMEK----------LQLQALEQEHKKLAARLEEERGK---NKHVVLMLVKECKQLSGKV 185
Cdd:pfam13868   43 RRLDEMMEEERERALEEEEEKEEERkeerkqyrqeLEEQIEEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEEKL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQKLEEVMAKLEE--EKKKTSALEEELATEK---------RRSAEMEAQMEKQLSEFDTEREQLRAKLHREEahttD 254
Cdd:pfam13868  123 EKQRQLREEIDEFNEEqaKWKELEKEEEKEEDLRileylkekaEREEEREAERREIKEEKEREIARLRAQQEKAQ----D 198
                          170
                   ....*....|....*....
gi 305855043   255 LKEEIDKM--KKMIEQLKR 271
Cdd:pfam13868  199 EKAERDELraKLYQEEQER 217
PTZ00121 PTZ00121
MAEBL; Provisional
89-287 3.42e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.08  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   89 RDYEAGASDKEKKPVCTNPLSILEAVMAHCRKMQERMStqlaaAESRQKKLEMEKlqlqaLEQEHKKLAARLEEERGKnk 168
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK-----AEEARKADELKK-----AEEKKKADEAKKAEEKKK-- 1303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  169 hvvlmlVKECKqlsgKVLEEAQKLEEVMAKLEEEKKKTSALEEElATEKRRSAEM-EAQMEKQLSEFDTEREQLRA-KLH 246
Cdd:PTZ00121 1304 ------ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAaKAEAEAAADEAEAAEEKAEAaEKK 1372
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 305855043  247 REEAhttdlKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1373 KEEA-----KKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
Ank_4 pfam13637
Ankyrin repeats (many copies);
805-855 4.79e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 4.79e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 305855043   805 TPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLL 855
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00121 PTZ00121
MAEBL; Provisional
119-289 1.08e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvLMLVKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  199 LEEEKKKTSALEEELATEKRRSAEME--AQMEKQLSEFDTEREQLR----AKLHREEAHTTD-LKEEIDKMKKMIEQLKR 271
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
                         170
                  ....*....|....*...
gi 305855043  272 GNDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
Ank_4 pfam13637
Ankyrin repeats (many copies);
705-757 1.13e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.13e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 305855043   705 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 757
Cdd:pfam13637    3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
722-841 1.14e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  722 LLNEEGLDINYSCEDGHSALYSAAKNGHT-DCVRLLLNAEAQVNAADKNGFTPL--CAAAAQGHFKCVELLIAYDANINH 798
Cdd:PHA03095   68 LLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNA 147
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 305855043  799 AADGGQTPL--YLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIH 841
Cdd:PHA03095  148 LDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
40-271 1.26e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 58.77  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGASDKEKKpvctnplsILEAVMAHCR 119
Cdd:pfam13868   99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAKWKELEKEEEKE--------EDLRILEYLK 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   120 KMQERMstqlAAAESRQKKLEMEKlqlqalEQEHKKLAARLEEERGKNKHVVLMLVKeckqlsgKVLEEAQK------LE 193
Cdd:pfam13868  163 EKAERE----EEREAERREIKEEK------EREIARLRAQQEKAQDEKAERDELRAK-------LYQEEQERkwrqkeRE 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   194 EVMAKLEEEKKKTSALEEELAtEKRRSAEMEAQMEKQLSE-------FDTEREQLRA--KLHREEAHTTDLKEEIDKMKK 264
Cdd:pfam13868  226 EAEKKARQRQELQQAREEQIE-LKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAekRREKRLEHRRELEKQIEERER 304

                   ....*..
gi 305855043   265 MIEQLKR 271
Cdd:pfam13868  305 QRAAERE 311
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
134-270 1.69e-08

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 59.73  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  134 SRQKK-LEMEKLQLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEE 212
Cdd:COG1196   656 SRNKRsSLAQKRELKELEEELAELEAQLEK-----------LEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRE 724
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  213 LATEKRRsaemEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196   725 LAALEEE----LEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLK 778
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
133-298 2.06e-08

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 57.38  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  133 ESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERgknkhvvlMLVKECKQLSG------KVLEEAQKLEEVMAKLEEEKK 204
Cdd:COG1340   101 EFNLGGRSIKSLEreIERLEKKQQTSVLTPEEER--------ELVQKIKELRKeledakKALEENEKLKELKAEIDELKK 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  205 KTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQlRAKLHREeahTTDLKEEIDKMKKMIEQLK---RGNDSKPSLSL 281
Cdd:COG1340   173 KAREIHEKIQELANEAQEYHEEMIKLFEEADELRKE-ADELHEE---FVELSKKIDELHEEFRNLQnelRELEKKIKALR 248
                         170
                  ....*....|....*..
gi 305855043  282 PRKTKDRRLVSISVATE 298
Cdd:COG1340   249 AKEKAAKRREKREELKE 265
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
131-270 2.57e-08

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 56.49  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   131 AAEsrQKKLEMEKlQLQALEQEHKKLAARLEEERGKnkhvVLMLVKECKQLSgkvlEEAQKLEEVMAKLEEEKkktsale 210
Cdd:pfam00769    3 EAE--REKQELEE-RLKQYEEETRKAQEELEESEET----AELLEEKLRVAE----EEAELLEQKAQEAEEEK------- 64
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043   211 EELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEI----DKMKKMIEQLK 270
Cdd:pfam00769   65 ERLEESAEMEAEEKEQLERELREAQEEVARLEEESERKEEEAERLQEELeearEEEEEAKEKLL 128
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
28-270 2.74e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 2.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    28 KKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARrkevfIQERYGRFNLNDPFLALQRDYEAGASDKEKKPvcTNP 107
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-----VEQLEERIAQLSKELTELEAEIEELEERLEEA--EEE 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   108 LSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKV-- 185
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIes 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 ----LEEAQKLEEVM-AKLEEEKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHreeahttDLKE 257
Cdd:TIGR02168  857 laaeIEELEELIEELeSELEALLNERASLEEALALLRSELEELSEElreLESKRSELRRELEELREKLA-------QLEL 929
                          250
                   ....*....|...
gi 305855043   258 EIDKMKKMIEQLK 270
Cdd:TIGR02168  930 RLEGLEVRIDNLQ 942
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
117-321 2.89e-08

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 58.58  E-value: 2.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   117 HCRKMQERMSTQLAAAESRQKKL--EMEKLQLQALEQEHK---KL------AARLEEERGKNKHVVLMLVKECKQLSGKV 185
Cdd:pfam05483  524 NCKKQEERMLKQIENLEEKEMNLrdELESVREEFIQKGDEvkcKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQI 603
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQKLEEVMAKLEEEKKKTSA--------------LEEELATEKRRSAEMEAQMEKQLSEFDTEREQL-----RAKLH 246
Cdd:pfam05483  604 ENKNKNIEELHQENKALKKKGSAenkqlnayeikvnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLleeveKAKAI 683
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   247 REEAhtTDLKEEIDK--------MKKMIEQLKRGNDS-----KPSLSLpRKTKDRRLVSISVATEGPMTR------SVAC 307
Cdd:pfam05483  684 ADEA--VKLQKEIDKrcqhkiaeMVALMEKHKHQYDKiieerDSELGL-YKNKEQEQSSAKAALEIELSNikaellSLKK 760
                          250
                   ....*....|....
gi 305855043   308 QTDLVTETAEPLKK 321
Cdd:pfam05483  761 QLEIEKEEKEKLKM 774
PTZ00121 PTZ00121
MAEBL; Provisional
34-321 3.58e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   34 DTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDK-EKKPVCTNPLSIL 111
Cdd:PTZ00121 1549 DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAEELKKA 1628
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  112 EAVMAHCRKMQERMSTQLAAAESRQKKLEMEKL---QLQALEQEHKKLA--ARLEEERGKNKHVVLML----VKECKQLS 182
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKeaeeAKKAEELK 1708
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  183 GKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEM--EAQMEKQLSEFDTEREQLRAKLHREEAHTtdLKEEID 260
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELD 1786
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  261 KmkkmieqlkrgNDSKPSLSLPRKTKDRR---------------LVSISVATEGPMTRSVACQTDLVTETAEPLKK 321
Cdd:PTZ00121 1787 E-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
115-271 4.03e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 57.23  E-value: 4.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   115 MAHCRK-----MQER-MSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLE-------------EERGKNKHVVLMLV 175
Cdd:pfam13868   17 AAKCNKerdaqIEEKkRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkqyrqeleeqiEEREQKRQEEYEEK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   176 KECKQLSGKVLEEAQkLEEVMAKLEEEKKKTSALEE------ELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREE 249
Cdd:pfam13868   97 LQEREQMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidefneEQAKWKELEKEEEKEEDLRILEYLKEKAEREEEREAER 175
                          170       180
                   ....*....|....*....|...
gi 305855043   250 AHTTDLKE-EIDKMKKMIEQLKR 271
Cdd:pfam13868  176 REIKEEKErEIARLRAQQEKAQD 198
PTZ00121 PTZ00121
MAEBL; Provisional
112-289 5.46e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  112 EAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQ--EHKKLAARLEEERGKNKHVVLMLVKecKQLSGKVLEEA 189
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEA 1423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  190 QKLEEVMAKLEEEKKKtsALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTD-LKEEIDKMKKMIEQ 268
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeAKKKAEEAKKKADE 1501
                         170       180
                  ....*....|....*....|.
gi 305855043  269 LKRGNDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAK 1522
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
86-296 5.72e-08

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 5.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   86 ALQRDYEAGASDKEKkpvCTNPLSILEAVMAHCRKMQERMSTQLaaaESRQKKLEMEKLQLQALEQEHKKLAARLEEERG 165
Cdd:COG1196   671 ELEEELAELEAQLEK---LEEELKSLKNELRSLEDLLEELRRQL---EELERQLEELKRELAALEEELEQLQSRLEELEE 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  166 KNKHVVLMLVKECKQLSgKVLEEAQKLEEVMAKLEEEKKKTS----ALEEELA---TEKRRSAEMEAQMEKQLSEFDTER 238
Cdd:COG1196   745 ELEELEEELEELQERLE-ELEEELESLEEALAKLKEEIEELEekrqALQEELEeleEELEEAERRLDALERELESLEQRR 823
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  239 EQLRAKLHREEAHTTDLKEEIDKMKkmiEQLKRGNDSKPSLSLPRKTKDRRLVSISVA 296
Cdd:COG1196   824 ERLEQEIEELEEEIEELEEKLDELE---EELEELEKELEELKEELEELEAEKEELEDE 878
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
48-271 6.48e-08

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 57.86  E-value: 6.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGASDKEKKpvctnpLSILEAVMAH 117
Cdd:pfam01576  775 LELDLKELEAQIEAANKGRDEAVKQLKKLQAQMKD----LQRELDearasrdeifAQSKESEKK------LKSLEAELLQ 844
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   118 crkMQErmstQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKHVVLML-------VK 176
Cdd:pfam01576  845 ---LQE----DLAAAERARRQAQQERDELAeeiasgnsgksALLDEKRRLEARiaqLEEELEEEQSNTELLndrlrklTL 917
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   177 ECKQLSGKVLEE---AQKLEEVMAKLEEEKKKTSA-LEEELATEKRRS----AEMEA---QMEKQLSEFDTEReQLRAKL 245
Cdd:pfam01576  918 QVEQLTTELAAErstSQKSESARQQLERQNKELKAkLQEMEGTVKSKYkssiAALEAkiaQLEEQLEQESRER-QAANKL 996
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 305855043   246 HR---------------EEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam01576  997 VRrtekklkevllqvedERRNADQYKDQAEKGNSRLKQLKR 1037
DHR10 pfam18595
Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies ...
136-271 7.54e-08

Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies of a modular structure unit1 are widespread in nature and have critical roles in molecular recognition, signaling, and other essential biological processes. This entry describes a MazG related domain also designated as Designed helical repeat protein 10 (DHR10). This domain is also found at the N-terminal region of Nuf2 proteins pfam03800.


Pssm-ID: 436606 [Multi-domain]  Cd Length: 117  Bit Score: 52.21  E-value: 7.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   136 QKKLEMEKLQLQALEQEHKKLAARLEeergknkhVVLML---VKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEE 212
Cdd:pfam18595    1 SETLAEEKEELAELERKARELQAKID--------ALQVVekdLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEIE 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043   213 LATEKRRsaemEAQMEKQLsefdterEQLRAKLHREEAHTtdlKEEIDKMKKMIEQLKR 271
Cdd:pfam18595   73 LRELERR----EERLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
PHA02798 PHA02798
ankyrin-like protein; Provisional
750-859 8.36e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.77  E-value: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  750 TDCVRLLLNAEAQVNAADKNGFTPLCAAAA-----QGHFKCVELLIAYDANINHAADGGQTPLYLACKNG---NKECIKL 821
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 305855043  822 LLEAGTDRSVKTRDGWTPIHAAVDTGN---VDSLKLLMYHG 859
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG 171
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
40-276 1.09e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 56.69  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   40 ELRMLLSVMEGELEarDLVIEALRARRKEVFIQERYGRFNLNdpflalQRDYEAGASDKEKKPVCTNPLSIleavmAHCR 119
Cdd:COG0419   407 EIQEELEELEKELE--ELERELEELEEEIKKLEEQINQLESK------ELMIAELAGAGEKCPVCGQELPE-----EHEK 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  120 KMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNkhvVLMLVKECKQLSGKVLEEAQKLEEvmAKL 199
Cdd:COG0419   474 ELLELYELELEELE-EELSREKEEAELREEIEELEKELRELEEELIEL---LELEEALKEELEEKLEKLENLLEE--LEE 547
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  200 EEEKKKTSALEEELATEKRRSAEMEAQmEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSK 276
Cdd:COG0419   548 LKEKLQLQQLKEELRQLEDRLQELKEL-LEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSE 623
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
119-271 1.35e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 56.69  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKLE--MEKLQLQALEQEHKKLAARLEEERGKNKhvvlmLVKECKQLSGKVLEEA-QKLEEV 195
Cdd:COG0419   592 RERLKELKKKLKELEERLSQLEelLQSLELSEAENELEEAEEELESELEKLN-----LQAELEELLQAALEELeEKVEEL 666
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  196 MAKLEEEKKKTSAlEEELATEKRRSAEMEAQMEKQLSEFDTEREQLrAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419   667 EAEIRRELQRIEN-EEQLEEKLEELEQLEEELEQLREELEELLKKL-GEIEQLIEELESRKAELEELKKELEKLEK 740
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
37-271 1.46e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    37 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAgasdkekkpvctnplsiLE 112
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGE-----------------LE 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   113 AVMAHCRKMQERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKnkhvVLMLVKECKQLSGKVLEEAQKL 192
Cdd:TIGR02169  301 AEIASLERSIAEKERELEDAEERLAKLEAE---IDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAEL 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   193 EEVMAKLEEEKKKTSALEEEL--ATEKR-------------------RSAEMEAQM---EKQLSEFDTERE--------- 239
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYREKLekLKREInelkreldrlqeelqrlseELADLNAAIagiEAKINELEEEKEdkaleikkq 453
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 305855043   240 -----QLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:TIGR02169  454 ewkleQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
119-275 1.46e-07

Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 54.29  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvLMLVKECKQLS------GKVLEEAQKL 192
Cdd:COG1579    34 KKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEK-----LSAVKDERELRalnieiQIAKERINSL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  193 EEVMAKLEEEKKKtsaLEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEID-KMKKMIEQLKR 271
Cdd:COG1579   109 EDELAELMEEIEK---LEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELKEKLDpELLSEYERIRK 185

                  ....
gi 305855043  272 GNDS 275
Cdd:COG1579   186 NKKG 189
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
122-273 1.58e-07

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 55.59  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  122 QERMSTQLAAAESR--QKKLEMEKLQLQALEQEHKKLAARleEERGKNKHVvlmlvKECKQLSGKVLEEAQKLEEVMAKL 199
Cdd:COG4487    37 QSRILNTLEEFEKEanEKRAQYRSAKKKELSQLEEQLINQ--KKEQKNLFN-----EQIKQFELALQDEIAKLEALELLN 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  200 EEEKKKTSALEEELateKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK-KMIEQLKRGN 273
Cdd:COG4487   110 LEKDKELELLEKEL---DELSKELQKQLQNTAEIIEKKRENNKNEERLKFENEKKLEESLELEReKFEEQLHEAN 181
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
119-271 1.78e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKLEMEK-------LQLQALEQEHKKLAARLEEERGKNKHVVLML------VKECKQLSGKV 185
Cdd:PRK03918  213 SSELPELREELEKLEKEVKELEELKeeieeleKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekVKELKELKEKA 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  186 LE--------------------EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKqLSEFDTEREQLRAKL 245
Cdd:PRK03918  293 EEyiklsefyeeyldelreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKK 371
                         170       180
                  ....*....|....*....|....*..
gi 305855043  246 HREEAHTTDLK-EEIDKMKKMIEQLKR 271
Cdd:PRK03918  372 EELERLKKRLTgLTPEKLEKELEELEK 398
Ank_5 pfam13857
Ankyrin repeats (many copies);
722-774 1.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.96e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 305855043   722 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPL 774
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
147-277 2.00e-07

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 55.87  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  147 QALEQEHKKlaARLEEERGKNKHV---VLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELAtEKRRSAEM 223
Cdd:COG2433   392 EALSKVKEE--ERPREKEGTEEEErreITVYEKRIKKLEETVERLEEENSELKRELEELKREIEKLESELE-RFRREVRD 468
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  224 EAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKM--IEQLKRGNDSKP 277
Cdd:COG2433   469 KVRKDREIRARDRRIERLEKELEEKKKRVEELERKLAELRKMrkLELSGKGTPVKV 524
PTZ00121 PTZ00121
MAEBL; Provisional
53-287 2.15e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   53 EARDLVIEALRArrKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKkpvcTNPLSILEAVmahcRKMQE-RMSTQLAA 131
Cdd:PTZ00121 1234 EAKKDAEEAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAEEK----KKADEaKKAEEKKK 1303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  132 AESRQKKLE----MEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVmaKLEEEKKKTS 207
Cdd:PTZ00121 1304 ADEAKKKAEeakkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKAD 1381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  208 ALEEElATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEA-HTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTK 286
Cdd:PTZ00121 1382 AAKKK-AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE 1460

                  .
gi 305855043  287 D 287
Cdd:PTZ00121 1461 E 1461
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
127-250 2.32e-07

MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 51.94  E-value: 2.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   127 TQLAAAESRQKKLEMEKLQLQALEQEhkklaarlEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAKLEEEKKKT 206
Cdd:pfam05672   13 ARILAEKRRQAREQREREEQERLEKE--------EEER-----------LRREELRRRAEEERARREEEARRLEEERKRE 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 305855043   207 salEEELATEKRRSAEMEAQMEKQL-SEFDTEREQLRAKLhREEA 250
Cdd:pfam05672   74 ---EEERQRKAEEEAEEKEQREKEEqERLQKQKEEAEAKA-REEA 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-271 2.69e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  120 KMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKHVVLMLVKECKQLSGKvlEEAQKLEEVMA 197
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKR--LTGLTPEKLEK 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  198 KLEEEKKKTSALEEELATEKRRSAEME---AQMEKQLSEF---------------DTEREQLRAKLHREEAhttDLKEEI 259
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELkkakgkcpvcgreltEEHRKELLEEYTAELK---RIEKEL 468
                         170
                  ....*....|..
gi 305855043  260 DKMKKMIEQLKR 271
Cdd:PRK03918  469 KEIEEKERKLRK 480
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-294 3.28e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 3.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    39 SELRMLLSVMEGELEARDLVIEAL-RARRKEVFIQErygrfNLNDPFLALQRDYEAgasDKEKKPVCTNPLSILEAVMAH 117
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEIEQLeQEEEKLKERLE-----ELEEDLSSLEQEIEN---VKSELKELEARIEELEEDLHK 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   118 CRKMQERMSTQLAAAESRQKKLEMEKL---------QLQALEQEHKKLAARLE--EERGKNKHVVLMLVKECKQLSGKVL 186
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPEIQAELSKLeeevsrieaRLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEI 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   187 EEAQ-KLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQM---EKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKM 262
Cdd:TIGR02169  857 ENLNgKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
                          250       260       270
                   ....*....|....*....|....*....|..
gi 305855043   263 KKMIEQLKRGNDSKPSLSLPRKTKDRRLVSIS 294
Cdd:TIGR02169  937 EDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
29-271 3.32e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 55.15  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   29 KEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRAR---------RKEVFIQERygrfnlndpFLALQRDYEAGASDKE 99
Cdd:COG0419   308 EGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESEleelaeeknELAKLLEER---------LKELEERLEELEKELE 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  100 KKpvctnplsiLEAVMAHcRKMQERMSTQLAAAESRQKKLEMEKLQLQA-----------LEQEHKKLAARLEEER-GKN 167
Cdd:COG0419   379 KA---------LERLKQL-EEAIQELKEELAELSAALEEIQEELEELEKeleelereleeLEEEIKKLEEQINQLEsKEL 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  168 KHVVLMLVKECKQLSGK-------------------VLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQME 228
Cdd:COG0419   449 MIAELAGAGEKCPVCGQelpeehekellelyeleleELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALK 528
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 305855043  229 KQLSEFDTEREQLRAKL--HREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419   529 EELEEKLEKLENLLEELeeLKEKLQLQQLKEELRQLEDRLQELKE 573
PHA02884 PHA02884
ankyrin repeat protein; Provisional
739-843 3.65e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 53.83  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  739 SALYSAAKNGHTDCVRLLL----NAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQ-TPLYLACKN 813
Cdd:PHA02884   35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114
                          90       100       110
                  ....*....|....*....|....*....|
gi 305855043  814 GNKECIKLLLEAGTDRSVKTRDGWTPIHAA 843
Cdd:PHA02884  115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-270 3.68e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   59 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGASDKEKKPVCTNPLSI--LEAVMAHCRKMQERMSTQLAA 131
Cdd:PRK03918  393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  132 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKL-------EEVMAK 198
Cdd:PRK03918  471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLkgeikslKKELEK 550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  199 LEEEKKKTSALEEELATEKRRSAEMEAQME----KQLSEFDTE--------REQLRAK-----LHREEAHTTDLKEEIDK 261
Cdd:PRK03918  551 LEELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630

                  ....*....
gi 305855043  262 MKKMIEQLK 270
Cdd:PRK03918  631 AFEELAETE 639
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-271 3.98e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   49 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGASDKEKkpvctnplsileavMAH 117
Cdd:PRK03918  475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK--------------LIK 536
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  118 CRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLE---EAQKLEE 194
Cdd:PRK03918  537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdAEKELER 616
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTER--------EQLRAKLHREEAHTTDLKEEIDKMKKMI 266
Cdd:PRK03918  617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696

                  ....*
gi 305855043  267 EQLKR 271
Cdd:PRK03918  697 EKLKE 701
Ank_5 pfam13857
Ankyrin repeats (many copies);
788-843 3.98e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.98e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043   788 LLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAA 843
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
271-706 4.24e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  271 RGNDSKPSLSLPRKTKDR-RLVSISVATEGPMTRS----VACQTDLVTETAEPLKKLPLTVPVKPAAGSPLVSASAKGNA 345
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAarptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  346 CASAASvrpgierqvshgdligsslPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTVSPASG---HTPTPPPHSLHS 422
Cdd:PHA03247 2733 PALPAA-------------------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprRLTRPAVASLSE 2793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  423 PCANAPLHPGLNPRIQAArfrfQGSNANDPDQNGNTTQSPPSRDVSPTsrdtlvAKQLARNTVTQALSrftsppagapPR 502
Cdd:PHA03247 2794 SRESLPSPWDPADPPAAV----LAPAAALPPAASPAGPLPPPTSAQPT------APPPPPGPPPPSLP----------LG 2853
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  503 PGAPPTGDVGTYPPVGRTSLK--TPGGARVDRGNPPPIPPKKPGLSQTPSPPHPQlkvimdssrasstgikadnKTVASS 580
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQPERP-------------------PQPQAP 2914
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  581 PSSLPQgnrviNEENLSKSSSPQLPPKPSIDLTVAPagcavsalatsQVGAWPAETPGLNQPACSESSLVIPTTTAFRSS 660
Cdd:PHA03247 2915 PPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAP-----------TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 305855043  661 InPVSASSRRAGAS------DSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 706
Cdd:PHA03247 2979 V-PQPAPSREAPASstppltGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
705-841 5.01e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQ-VNAADKN----GFTPLCAAAA 779
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  780 QGHFKCVELLIAYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTDrsVKTRDGW--TPIH 841
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
38-272 5.90e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 54.38  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   38 KSELRMLlsvmEGELEARDLVIEAL--RARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKpvctnpLSILEAVM 115
Cdd:COG0419   273 EEELREL----ERLLEELEEKIERLeeLEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKL------EEKLEKLE 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  116 AHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvKECKQLSGKVLEEAQKLEEV 195
Cdd:COG0419   343 SELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELK-------EELAELSAALEEIQEELEEL 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  196 MAKLEEEKKKTSALEEELAT--EKRRSAEMEAQMEKQLSE-----------------------FDTEREQLRAKLHREEa 250
Cdd:COG0419   416 EKELEELERELEELEEEIKKleEQINQLESKELMIAELAGagekcpvcgqelpeehekellelYELELEELEEELSREK- 494
                         250       260
                  ....*....|....*....|..
gi 305855043  251 HTTDLKEEIDKMKKMIEQLKRG 272
Cdd:COG0419   495 EEAELREEIEELEKELRELEEE 516
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
110-268 6.19e-07

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 429718 [Multi-domain]  Cd Length: 488  Bit Score: 54.12  E-value: 6.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   110 ILEAVMAHCRKMQ-ERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKHVVLMLVKECKQLSGKV 185
Cdd:pfam07888   31 LLQNRLEECLQERaELLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKVEELEEKYKELSRSG 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEK----------QLSEFDTEREQLRAKLHREEAHTTDL 255
Cdd:pfam07888  111 EELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERmkervkkagaQRKEEEAERKQLQAKLQQTEEELRSL 190
                          170
                   ....*....|...
gi 305855043   256 KEEIDKMKKMIEQ 268
Cdd:pfam07888  191 SKEFQELRNSLAQ 203
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
119-261 6.46e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 54.40  E-value: 6.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMS---TQLAAAESRQKKLEMEKLqlqALEQEHKKLAAR---LEEERGKnkhvvlmLVKECKQL-------SGKV 185
Cdd:pfam01576   99 KKMQQHIQdleEQLEEEEAARQKLQLEKV---TTEAKIKKMEEDillLEDQNNK-------LQKERKLLeerisefTSNL 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQKL----------EEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDL 255
Cdd:pfam01576  169 AEEEEKSkslnklknkhEAMISDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQLAKKEEELQAA 248

                   ....*.
gi 305855043   256 KEEIDK 261
Cdd:pfam01576  249 LARLEE 254
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
119-263 7.75e-07

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 51.93  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERM---STQLAAAESRQKKLEME--KLQLQALEQEHK-KLAARLEEErgknkhvvlmlvkeckQLSGKVLEEAQKL 192
Cdd:COG1842    34 RDMESELakaRQALAQAIARQKQLERKleEAQARAEKLEEKaELALQAGNE----------------DLAREALEEKQSL 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043  193 EEVMAKLEEEkkktsalEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAhTTDLKEEIDKMK 263
Cdd:COG1842    98 EDLAKALEAE-------LQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKAAAKA-QEKVNRSLGGGS 160
PHA03095 PHA03095
ankyrin-like protein; Provisional
715-856 7.78e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  715 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKC--VELLI 790
Cdd:PHA03095  166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLL 244
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  791 AYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLM 856
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
174-275 1.17e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 53.29  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  174 LVKECKQLSGkvlEEAQKLEEVMAKLEEEKKKtsaLEEEL--ATEKRRSAE-MEAQMEKQLSEFDTEREQLRAKLHRE-- 248
Cdd:PRK00409  503 IIEEAKKLIG---EDKEKLNELIASLEELERE---LEQKAeeAEALLKEAEkLKEELEEKKEKLQEEEDKLLEEAEKEaq 576
                          90       100
                  ....*....|....*....|....*..
gi 305855043  249 EAhTTDLKEEIDKMKKMIEQLKRGNDS 275
Cdd:PRK00409  577 QA-IKEAKKEADEIIKELRQLQKGGYA 602
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
112-270 1.24e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 53.63  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   112 EAVMAHCRKMQ---ERMSTQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKHVVLMLVKECK------- 179
Cdd:pfam01576  906 ELLNDRLRKLTlqvEQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKYKSSIAALEAKiaqleeq 982
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   180 --------QLSGKVLEEAQK-LEEVMAKLEEEKKKTSALEEELatEKrRSAEMEaQMEKQLSEfdTEREQLRA-----KL 245
Cdd:pfam01576  983 leqesrerQAANKLVRRTEKkLKEVLLQVEDERRNADQYKDQA--EK-GNSRLK-QLKRQLEE--AEEEASRAnaarrKL 1056
                          170       180
                   ....*....|....*....|....*
gi 305855043   246 HREeahTTDLKEEIDKMKKMIEQLK 270
Cdd:pfam01576 1057 QRE---LDDATESAEAMNREVTTLR 1078
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
186-271 1.26e-06

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 433535 [Multi-domain]  Cd Length: 119  Bit Score: 48.73  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDT-----EREQLRA--KLHREEAHTTDLKEE 258
Cdd:pfam13863    2 LEKKREMFLVQLALDAKREEIQRLEELLKQREEELEKKEQELKEDLVKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81
                           90
                   ....*....|...
gi 305855043   259 IDKMKKMIEQLKR 271
Cdd:pfam13863   82 IKKLTAQLEELKS 94
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
73-264 1.34e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.50  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   73 ERYGRfnlndpflalQRDYEAGASDKEKKPvctnplsileavmahcRKMQERMSTQL----AAAESRQKKLEMEKLQLQA 148
Cdd:PRK09510   62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  149 lEQEHKKLAARLEEERGKNKHVVLMLVKECKQLsgKVLEEAQKLEEVMAKLEEEKKKtsalEEELATEKRRSAEMEAQME 228
Cdd:PRK09510  116 -QKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA--KAEAEAKRAAAAAKKAAAEAKK----KAEAEAAKKAAAEAKKKAE 188
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 305855043  229 KQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKK 264
Cdd:PRK09510  189 AEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
120-275 1.77e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 52.84  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  120 KMQERMSTQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKHvvlmLVKECKQLSGKVLE-EAQKLEEVMAK 198
Cdd:COG0419   171 KLSELLKEVIKEAKAKIEELE---GQLSELLEDIEDLLEALEEELKELKK----LEEIQEEQEEEELEqEIEALEERLAE 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  199 LEEEKK------------------KTSALEEELATEKRRSAEMEaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEID 260
Cdd:COG0419   244 LEEEKErleelkarlleiesleleALKIREEELRELERLLEELE-EKIERLEELEREIEELEEELEGLRALLEELEELLE 322
                         170
                  ....*....|....*
gi 305855043  261 KMKKMIEQLKRGNDS 275
Cdd:COG0419   323 KLKSLEERLEKLEEK 337
RmuC COG1322
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ...
120-269 1.83e-06

DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];


Pssm-ID: 224241 [Multi-domain]  Cd Length: 448  Bit Score: 52.39  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  120 KMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVlmlvkecKQLSGKVLEEAQKLEEVMAKL 199
Cdd:COG1322    28 GRLEQMLGELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELK-------ARLQQQLLQSREQLQLLIESL 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  200 EEEKKKTSALEEELATEK-RRSAEMEAQMEKQLSEF-----DTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:COG1322   101 AQLSSEFQELANEIFEELnRRLAELNQQNLKQLLKPlrevlEKFREQLEQRIHESAEERSTLLEEIDRLLGEIQQL 176
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
132-271 1.97e-06

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 434815 [Multi-domain]  Cd Length: 193  Bit Score: 49.89  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   132 AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVvlmlvkecKQLS-GKVLEEAQKLEevmakleeekKKTSA 208
Cdd:pfam15619   67 EEVRvlRERLRRSQEKERDLERKLKEKEAELLRLRDELKKL--------KKLSeDKNLAEREELQ----------KKLAQ 128
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   209 LEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam15619  129 LEAKLEEKEEKIQELERKLELEEKNFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKER 191
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-270 2.28e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  133 ESRQKKLEMEKLqLQALEQEHKKLAARLEEERGKNKHVvlmlvKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEe 212
Cdd:PRK03918  304 EYLDELREIEKR-LSRLEEEINGIEERIKELEEKEERL-----EELKKKLKELEKRLEELEERHELYEEAKAKKEELER- 376
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  213 laTEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:PRK03918  377 --LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-270 2.38e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  133 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKHVVLM-------LVKECKQLSGKVLEEAQKLEEVMAKLEEEK 203
Cdd:PRK03918  145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  204 KKTSALEEELatEKRRsaEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:PRK03918  224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
745-823 2.67e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.67e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  745 AKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLL 823
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
1070-1359 3.21e-06

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 51.62  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1070 NKAEQVTVLLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCLKHRQMaagfPCEIV 1149
Cdd:PRK11331  153 NSGKSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA----PQRVN 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1150 RAEVDADFSKEQLV-------------DLFISSACLiPVKQSPaNKKIIIILENLEKSSLSELLGDFLGPLEN----HST 1212
Cdd:PRK11331  229 MVQFHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENW 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043 1213 ESPCTFQKGNgmSECYYFHENCFLMGTI--AKACLQGSDLLVQQHFRWVqlrwDSEPmqGLLQRFLRRKVVNKfrGQVPS 1290
Cdd:PRK11331  307 SVPLTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPS 376
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043 1291 PCDPVCKTVDwalavwrQLNSCLARLGTpeaLLGPKY-----FLSCPVIPGHAQATvKWMSKLWNAVIAPRVQE 1359
Cdd:PRK11331  377 FVESLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
mukB PRK04863
chromosome partition protein MukB;
145-244 3.36e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.27  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  145 QLQALEQEHKKLAARLEEERGKNKhvvlmLVKECKQLSGKVLEEAQKLEEVMAKLEEEKkktsaleEELATEKRRSAEME 224
Cdd:PRK04863  514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581
                          90       100
                  ....*....|....*....|
gi 305855043  225 AQMEKQLSEFDTEREQLRAK 244
Cdd:PRK04863  582 MALRQQLEQLQARIQRLAAR 601
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-271 3.55e-06

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: 51.98  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    40 ELRMLLSVMEGELEA-----RDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAsdkekkpvctnpLSILEAV 114
Cdd:TIGR02168  695 ELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   115 MAHCRKMQERMSTQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEE 194
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELR-----------AELTLLNEEAANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQME----------KQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKK 264
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieeleSELEALLNERASLEEALALLRSELEELSEELRELES 908

                   ....*..
gi 305855043   265 MIEQLKR 271
Cdd:TIGR02168  909 KRSELRR 915
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
122-271 4.71e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 50.68  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvkeckqlsgkvlEEAQKLEEVMAKLEE 201
Cdd:pfam13868  215 QERKWRQKEREE-AEKKARQRQELQQAREEQIELKERRLAEEAEREE------------------EEFERMLRKQAEDEE 275
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043   202 EKKKTSALEEELATEKRRsaEMEAQMEkqlsefdtEREQLRAKLHREEAHTTD-LKEEIDKMKKMIEQLKR 271
Cdd:pfam13868  276 IEQEEAEKRREKRLEHRR--ELEKQIE--------ERERQRAAEREEELEEGErLREEEAERRERIEEERQ 336
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
122-290 4.75e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 51.70  E-value: 4.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlmlvkeckqLSGKvleeAQKLEEVM----A 197
Cdd:pfam01576   21 QQKAESELKELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRAR--------------LAAR----KQELEEILheleA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   198 KLEEEKKKTSALEeelaTEKRRSAEMEAQMEKQLSefdtEREQLRAKLHREEAhTTDlkeeiDKMKKMIEQLKRGNDSKP 277
Cdd:pfam01576   83 RLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLE----EEEAARQKLQLEKV-TTE-----AKIKKMEEDILLLEDQNN 148
                          170
                   ....*....|...
gi 305855043   278 SLSLPRKTKDRRL 290
Cdd:pfam01576  149 KLQKERKLLEERI 161
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-264 5.41e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 5.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    39 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGASDKEKKPV----CTNPLSILEAV 114
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESR 883
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   115 MAHCRKMQERMSTQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKHVVLML-----VKECKQLSGKVLEEA 189
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeeIPEEELSLEDVQAEL 960
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043   190 QKLEEVMAKLEEEKKKtsALEEELATEKRRSaEMEAQMEKqlseFDTEREQLRaklhreeahttDLKEEIDKMKK 264
Cdd:TIGR02169  961 QRVEEEIRALEPVNML--AIQEYEEVLKRLD-ELKEKRAK----LEEERKAIL-----------ERIEEYEKKKR 1017
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
110-257 5.66e-06

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 51.25  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  110 ILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLvkecKQLSGKVLEEA 189
Cdd:COG1196   370 LLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAEL----EELQTELEELN 445
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043  190 QKLEEVMAKLEEEKKKTSALEEELAT--EKRRSAEMEAQ-MEKQLSEFDTEREQLRAKLHREEAHTTDLKE 257
Cdd:COG1196   446 EELEELEEQLEELRDRLKELERELAElqEELQRLEKELSsLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
111-271 6.06e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 50.99  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  111 LEAVMAHCRKMQERMST-QLAAAESRQKKLEMEKLQL-----------QALEQEHKKLAARLEEERGKNKHVV--LMLVK 176
Cdd:PRK04778  258 IQDLKEQIDENLALLEElDLDEAEEKNEEIQERIDQLydilerevkarKYVEKNSDTLPDFLEHAKEQNKELKeeIDRVK 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  177 ECKQLSGKVLEEAQKLEEVMAKLE----------EEKKKT-SALEEELatekrrsaemeAQMEKQLSEFDTEREQLR--- 242
Cdd:PRK04778  338 QSYTLNESELESVRQLEKQLESLEkqydeiteriAEQEIAySELQEEL-----------EEILKQLEEIEKEQEKLSeml 406
                         170       180
                  ....*....|....*....|....*....
gi 305855043  243 AKLHREEAhttDLKEEIDKMKKMIEQLKR 271
Cdd:PRK04778  407 QGLRKDEL---EAREKLERYRNKLHEIKR 432
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
53-272 6.22e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 50.06  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   53 EARDLVIEA--LRARRKEVF--IQE-RYGRFNLNDPFLALQRDYEAGASDKEKKPVCTNPLSILEAVMAHCRKMQERMst 127
Cdd:COG1340    49 KVRELREKAqeLREERDEINeeVQElKEKRDEINAKLQELRKEYRELKEKRNEFNLGGRSIKSLEREIERLEKKQQTS-- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  128 QLAAAESRQ-----KKLEMEKLQLQALEQEHKKLAARLEEergknkhvVLMLVKECKQLSGKVLE---EAQKLEEVMAKL 199
Cdd:COG1340   127 VLTPEEERElvqkiKELRKELEDAKKALEENEKLKELKAE--------IDELKKKAREIHEKIQElanEAQEYHEEMIKL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  200 ----EEEKKKTSALEEELATEKRRSAEMEA---QMEKQLSEFDTEREQLRAKLhREEAHTTDLKEEIDKMKKMIEQLKRG 272
Cdd:COG1340   199 feeaDELRKEADELHEEFVELSKKIDELHEefrNLQNELRELEKKIKALRAKE-KAAKRREKREELKERAEEIYEKFKRG 277
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
119-263 6.70e-06

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 49.17  E-value: 6.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQE---RMSTQLAAAESRQKKLEMEklqLQALEQEhkklAARLEEERgknkhvvlmlvkeckqlsgkvleeaQKLEEV 195
Cdd:pfam00769   16 KQYEEetrKAQEELEESEETAELLEEK---LRVAEEE----AELLEQKA-------------------------QEAEEE 63
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043   196 MAKLEEEKKKTSALEEELATEKRrsaemEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK 263
Cdd:pfam00769   64 KERLEESAEMEAEEKEQLERELR-----EAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEK 126
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
122-275 7.52e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 7.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKHVVLMLV------------KECKQLSGK 184
Cdd:TIGR04523  403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   185 VLEEAQKLEEvmaKLEEEKKKTSALEEeLATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK- 263
Cdd:TIGR04523  477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDf 552
                          170       180
                   ....*....|....*....|....*..
gi 305855043   264 ---------------KMIEQLKRGNDS 275
Cdd:TIGR04523  553 elkkenlekeideknKEIEELKQTQKS 579
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
128-271 7.87e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 50.91  E-value: 7.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEA-QKLEEVM-------AKL 199
Cdd:COG0419   577 ELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEELESElEKLNLQAeleellqAAL 656
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  200 EEEKKKTSALEEELATEKRRsAEMEAQMEKQ---LSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG0419   657 EELEEKVEELEAEIRRELQR-IENEEQLEEKleeLEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEE 730
PTZ00121 PTZ00121
MAEBL; Provisional
132-298 8.88e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 8.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  132 AESRQKKLEMEKlqlQALEQEHKKLAARLEEERGKNKHVVlmlvKECKQLSGKVlEEAQKLEEVMAKLEEEKKKTSALEE 211
Cdd:PTZ00121 1433 ADEAKKKAEEAK---KADEAKKKAEEAKKAEEAKKKAEEA----KKADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKK 1504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  212 ElATEKRRSAEMEAQMEKQLSEfdtEREQLRAKLHREEAHTTDLKEEIDKMKKMiEQLKRGNDSKpSLSLPRKTKDRRLV 291
Cdd:PTZ00121 1505 A-AEAKKKADEAKKAEEAKKAD---EAKKAEEAKKADEAKKAEEKKKADELKKA-EELKKAEEKK-KAEEAKKAEEDKNM 1578

                  ....*..
gi 305855043  292 SISVATE 298
Cdd:PTZ00121 1579 ALRKAEE 1585
PHA02876 PHA02876
ankyrin repeat protein; Provisional
705-875 1.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH----------------------------------- 749
Cdd:PHA02876  275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdtenirtlimlgadvnaadrlyitplhqastldrn 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  750 TDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLA-CKNGNKECIKLLLEAGTD 828
Cdd:PHA02876  355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGAN 434
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 305855043  829 RSVKTRDGWTPIHAAVDTG-NVDSLKLLMYHGAPAHGNKLQEEPGLAI 875
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
45-286 1.14e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 50.21  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    45 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGASD-KE----------K 100
Cdd:pfam10174  438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   101 KPVCTNPLSI-LEAVMAHCRKMQERMSTQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKHVVLMLV---- 175
Cdd:pfam10174  515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVERLLgilr 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   176 -----KECKQ---------LSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAE--MEAQMEKQLSEFDTERE 239
Cdd:pfam10174  590 eveneKNDKDkkiaeleslTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQ 669
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   240 QLRA----------KLHREEAHTTDLK-------EEIDKMKKmiEQL------KRGNDSKPSLSLPRKTK 286
Cdd:pfam10174  670 ELDAtkarlsstqqSLAEKDGHLTNLRaerrkqlEEILEMKQ--EALlaaiseKDANIALLELSSSKKKK 737
fliH PRK06669
flagellar assembly protein H; Validated
125-270 1.20e-05

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 48.86  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  125 MSTQLAAAEsRQKKLEMEKLQLQALEQEHKklaarlEEERGKNKHVVLMLVKECKQLSGKVLEEAQkleevMAKLEEEKK 204
Cdd:PRK06669    7 KRSNVINKE-KLKTHEIQKYRFKVLSIKEK------ERLREEEEEQVEQLREEANDEAKEIIEEAE-----EDAFEIVEA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  205 KTSALEEEL--ATEKRRS--AEMEAQMEKQLSEFDTEREQL----RAKLHRE------EAHTTDLKEEIDKMKKMIEQLK 270
Cdd:PRK06669   75 AEEEAKEELlkKTDEASSiiEKLQMQIEREQEEWEEELERLieeaKAEGYEEgyekgrEEGLEEVRELIEQLNKIIEKLI 154
PRK12704 PRK12704
phosphodiesterase; Provisional
119-271 1.21e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKLEMEKLqLQAlEQEHKKLAARLEEE-RGKNKHVvlmlvkecKQLSGKVLEEAQKLEEVMA 197
Cdd:PRK12704   34 KEAEEEAKRILEEAKKEAEAIKKEAL-LEA-KEEIHKLRNEFEKElRERRNEL--------QKLEKRLLQKEENLDRKLE 103
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043  198 KLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLrAKLHREEAhttdlKEEIdkMKKMIEQLKR 271
Cdd:PRK12704  104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEA-----KEIL--LEKVEEEARH 169
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
111-249 1.22e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 48.08  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  111 LEAVMAHCRKMQERMSTQLAAAESRQKKLEM------EKLQLQALE--QEHKKLAARLEEERGKNKHVVLMLVKECKQLS 182
Cdd:COG1842    47 LAQAIARQKQLERKLEEAQARAEKLEEKAELalqagnEDLAREALEekQSLEDLAKALEAELQQAEEQVEKLKKQLAALE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  183 GKVLEEAQKLEEVMAKLEEEKK-----------KTSALEEELATEKRRSAEMEAQ--------------MEKQL------ 231
Cdd:COG1842   127 QKIAELRAKKEALKARKAAAKAqekvnrslgggSSSSAMAAFERMEEKIEEREARaeaaaelaegsgddLDKEFaqagaq 206
                         170
                  ....*....|....*...
gi 305855043  232 SEFDTEREQLRAKLHREE 249
Cdd:COG1842   207 SAVDSRLAALKARMKGPA 224
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
91-281 1.26e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    91 YEAGASDKEKKPvcTNPLSILEAVM----AHCRKMQERMSTQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEE 162
Cdd:pfam05483   61 YQEGLKDSDFEN--SEGLSRLYSKLykeaEKIKKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEE 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   163 ERGKNKHvvlmLVKEckqlSGKVLEEAQKLEEVMAKLEEekkKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQlr 242
Cdd:pfam05483  139 EIQENKD----LIKE----NNATRHLCNLLKETCARSAE---KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ-- 205
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 305855043   243 AKLHREEAHTTdLKEEIDKMKKMIEQLKRG-NDSKPSLSL 281
Cdd:pfam05483  206 AENARLEMHFK-LKEDHEKIQHLEEEYKKEiNDKEKQVSL 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
111-269 1.28e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  111 LEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvVLMLVKECKQLS-------- 182
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREE----LEKLEKEVKELEelkeeiee 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  183 -----GKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEK--QLSEFdteREQLRAKLHREEAHTTDL 255
Cdd:PRK03918  243 lekelESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRL 319
                         170
                  ....*....|....
gi 305855043  256 KEEIDKMKKMIEQL 269
Cdd:PRK03918  320 EEEINGIEERIKEL 333
Ank_4 pfam13637
Ankyrin repeats (many copies);
836-923 1.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   836 GWTPIHAAVDTGNVDSLKLLMYHGAPahgnklqeepglaifdldqeehhegtskpvvpadlINHADSEGWTAAHIAASKG 915
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD-----------------------------------INAVDGNGETALHFAASNG 45

                   ....*...
gi 305855043   916 FKNCLEVL 923
Cdd:pfam13637   46 NVEVLKLL 53
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
151-270 1.43e-05

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 48.82  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   151 QEHKKLAARLEEERGKNK---HVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQM 227
Cdd:pfam02841  155 EERDKLEAKYNQVPRKGVkaeEVLQEFLKSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMM 234
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 305855043   228 EKQLSEFDTEREQLRAKLHREEAHttdLKEEIDKM--KKMIEQLK 270
Cdd:pfam02841  235 EAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
128-271 1.62e-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: 49.68  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKHVVLMlvKECKQLSGKVLEEAQKLEEVMAKLEEE 202
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDElsqelSDASRKIGEIE--KEIEQLEQEEEKLKERLEELEEDLSSL 749
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   203 KKKTSALEEELATEKRRSAEMEAQMEK-QLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
803-828 1.79e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.79e-05
                            10        20
                    ....*....|....*....|....*.
gi 305855043    803 GQTPLYLACKNGNKECIKLLLEAGTD 828
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02876 PHA02876
ankyrin repeat protein; Provisional
780-867 1.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  780 QGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLKLLMYHG 859
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                  ....*...
gi 305855043  860 APAHGNKL 867
Cdd:PHA02876  235 SNINKNDL 242
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
116-270 2.20e-05

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 47.10  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   116 AHCRKMQERMSTQ--LAAAESRQKKLEMEKLQL--QALEQEHKKLAARL-EEERGKNKHVVLMLVKECKQLSGK---VLE 187
Cdd:pfam14662   16 NNQKLLQENSKLKatVETREETNAKLLEENLNLrkQAKSQQQAVQKEKLlEEELEDLKLIVNSLEEARRSLLAQnkqLEK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIE 267
Cdd:pfam14662   96 ENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEE 175

                   ...
gi 305855043   268 QLK 270
Cdd:pfam14662  176 ELR 178
PHA03100 PHA03100
ankyrin repeat protein; Provisional
722-798 2.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 2.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  722 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINH 798
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
96-290 2.33e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 49.27  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    96 SDKEKKPVCTNPLSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARlEEERGKNKhvvlmlv 175
Cdd:TIGR00606  214 QYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-KKQMEKDN------- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   176 kecKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTE------REQLRAKLHREE 249
Cdd:TIGR00606  286 ---SELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEH 362
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 305855043   250 AHTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKDRRL 290
Cdd:TIGR00606  363 IRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQ 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
39-280 2.48e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    39 SELRMLLSVMEGELEAR-----DLVIEALRARRKEVFIQERygRFNLNDPFLALQRDYEAGAS----DKEKKPVCTNPLS 109
Cdd:TIGR02168  270 EELRLEVSELEEEIEELqkelyALANEISRLEQQKQILRER--LANLERQLEELEAQLEELESkldeLAEELAELEEKLE 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   110 ILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAAR----------LEEERGKNKHVVLMLV 175
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNEierlearlerLEDRRERLQQEIEELL 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   176 KecKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFdterEQLRAKLHREEAHTTDL 255
Cdd:TIGR02168  428 K--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL----AQLQARLDSLERLQENL 501
                          250       260
                   ....*....|....*....|....*
gi 305855043   256 KEEIDKMKKMIEQLKRGNDSKPSLS 280
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLSGILGVLS 526
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
122-269 2.52e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  122 QERMSTQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKnkhvVLMLVKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:PRK02224  522 EELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEE----AREEVAELNSKLAELKERIESLERIRTL 597
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305855043  199 LEEEKKKTSALEEelATEKRRS-AEMEAQMEKQLSEFDTEREQLRAKLhrEEAHTTDLKEEIDKMKKMIEQL 269
Cdd:PRK02224  598 LAAIADAEDEIER--LREKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
118-251 2.93e-05

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 435966 [Multi-domain]  Cd Length: 127  Bit Score: 45.28  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   118 CRKMQERMSTQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkhvvlmLVKECKQLSgkvlEEA 189
Cdd:pfam17675    7 TDLLLEELDKQLEDAEKeRDayisflKKLEEESPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305855043   190 QKLEEVMAKLEEEKKKTSALEEELATEKRrsaemeaQMEKQLSEFDTEREQLRAKLHREEAH 251
Cdd:pfam17675   72 EELDAELEALEEELEALDQEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
707-844 2.95e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   707 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGHtDCVRLLLNAEAQ----------VNAADKNGF----T 772
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAafrksgplelANDQYTSEFtpgiT 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   773 PLCAAAAQGHFKCVELLIAYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTDrsVKTRD--G 836
Cdd:TIGR00870  131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208

                   ....*...
gi 305855043   837 WTPIHAAV 844
Cdd:TIGR00870  209 NTLLHLLV 216
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
37-270 3.12e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   37 SKSELRMLLSVMEGELEARDLVIEALRARRKEV----FIQERYGRFN-LNDPFLALQRDYEAGASDKEKKpvctnpLSIL 111
Cdd:PRK03918  253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkEKAEEYIKLSeFYEEYLDELREIEKRLSRLEEE------INGI 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  112 EAVMAHCRKMQERMS----------TQLAAAESRQKKLEMEKlQLQALEQEHKKLAARLEEERGKNKhvvLMLVKECKQl 181
Cdd:PRK03918  327 EERIKELEEKEERLEelkkklkeleKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKE---LEELEKAKE- 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  182 sgKVLEEAQKLEEVMAKLE-EEKKKTSALEE-------------ELATEKRR------SAEMEaQMEKQLSEFDTEREQL 241
Cdd:PRK03918  402 --EIEEEISKITARIGELKkEIKELKKAIEElkkakgkcpvcgrELTEEHRKelleeyTAELK-RIEKELKEIEEKERKL 478
                         250       260       270
                  ....*....|....*....|....*....|
gi 305855043  242 RAKLhrEEAHTTDLKE-EIDKMKKMIEQLK 270
Cdd:PRK03918  479 RKEL--RELEKVLKKEsELIKLKELAEQLK 506
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
707-792 3.34e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  707 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCV 786
Cdd:PTZ00322   86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                  ....*.
gi 305855043  787 ELLIAY 792
Cdd:PTZ00322  165 QLLSRH 170
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
119-269 3.43e-05

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 48.48  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERgKNKHVVLMLVKECKQLS-------GKVLE 187
Cdd:COG4372    80 RPQLRALRTELGTAQGEKRAAETEReaarSELQKARQEREAVRQELAAAR-QNLAKAQQELARLTKQAqdlqtrlKTLAE 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  188 EAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRA---KLHREEAHTTDLKEEIDKMKK 264
Cdd:COG4372   159 QRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQArteELARRAAAAQQTAQAIQQRDA 238

                  ....*
gi 305855043  265 MIEQL 269
Cdd:COG4372   239 QISQK 243
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
176-271 3.63e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.56  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  176 KECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEEL--ATEKRRSAEMEAQM-EKQLSEFDTEREQLRAKLHREEAHT 252
Cdd:COG1196   667 RELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLeeLRRQLEELERQLEElKRELAALEEELEQLQSRLEELEEEL 746
                          90
                  ....*....|....*....
gi 305855043  253 TDLKEEIDKMKKMIEQLKR 271
Cdd:COG1196   747 EELEEELEELQERLEELEE 765
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
710-860 3.94e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 3.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   710 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLNAEAQVNAADKngftpLCAAAAQGHFKC 785
Cdd:TIGR00870   24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   786 VELLIAY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTDRSVKT--------------RDGW 837
Cdd:TIGR00870   97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGE 176
                          170       180
                   ....*....|....*....|...
gi 305855043   838 TPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPA 199
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
136-276 4.15e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   136 QKKLEMEKLQLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAKLEEEKKK-----TSALE 210
Cdd:TIGR04523  245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQ-----------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043   211 EELATEKRRSAEMEAQM---EKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSK 276
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
51-289 4.37e-05

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 48.48  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   51 ELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKPVCT--NPLSILEAVMAHCRK---MQERM 125
Cdd:COG5281   364 EKLARVTAQGALNARLKLAQDDLTQAELNYAAADQAANQEGALNAREDEAEVLSTqeERRDILKNLLADAEKrtaRQEEL 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  126 STQLAAAESRQKKLEMEKLQLQALEQEH----KKLAARLEEERGKNKHVVLMLVKECK-QLSGKVLeeaqkleevmaKLE 200
Cdd:COG5281   444 NKALAKAKILQADKAAKAYQEDILQREAqsrgKTAAAERSQEQMTAALKALLAFQQQIaDLSGAKE-----------KAS 512
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  201 EEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEidKMKKMIEQLKRGND------ 274
Cdd:COG5281   513 DQKSLLWKAEEQYALLKEEAKQRQLQEQKALLEHKKETLEYTSQLAELLDQQADRFEL--SAQAAGSQKERGSDlyreal 590
                         250
                  ....*....|....*
gi 305855043  275 SKPSLSLPRKTKDRR 289
Cdd:COG5281   591 AQNAAALNKALNELA 605
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
120-271 5.25e-05

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 47.50  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  120 KMQERMSTQLAAAESRQKKLEMEKLQLQ--ALEQEHKKLAARLEEERGKNKHVVLMLvkecKQLSGKVLEEAQKLEEvma 197
Cdd:COG4487    64 KELSQLEEQLINQKKEQKNLFNEQIKQFelALQDEIAKLEALELLNLEKDKELELLE----KELDELSKELQKQLQN--- 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043  198 KLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEahttdLKEEIDKMKKMIEQLKR 271
Cdd:COG4487   137 TAEIIEKKRENNKNEERLKFENEKKLEESLELEREKFEEQLHEANLDLEFKE-----NEEQRESKWAILKKLKR 205
PHA02876 PHA02876
ankyrin repeat protein; Provisional
706-940 5.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  706 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKC 785
Cdd:PHA02876  148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  786 VELLIAYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTdrSVKTRDGW--TPIHAAVDTGNVDSL-KLLMYHGAPA 862
Cdd:PHA02876  227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvPKLLERGADV 300
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  863 HGNKLQEEPGLAIFDLDQEEHHEGTSKPVVPADlINHADSEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRT 940
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKT 377
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
120-270 5.64e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 47.85  E-value: 5.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   120 KMQ---ERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkhvvLMLVKECKQLSgkvlEEAQKLEEvm 196
Cdd:pfam01576  437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSSRLRQLE----DEKNSLQE-- 503
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043   197 aKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTeREQLRAKLHRE-EAHTTDLKE---EIDKMKKMIEQLK 270
Cdd:pfam01576  504 -QLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEA-LEEGRKRLQRElEALTQRLEEkaaAYDKLEKTKNRLQ 579
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
119-246 6.02e-05

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 45.04  E-value: 6.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAEsRQKKLEMEKLQLQALEQEHKKLaarlEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:pfam15346   37 AEVERRVEEARKIME-KQVLEELEREREAELEEERRKE----EEER-----------KKREELERILEENNRKIEEAQRK 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 305855043   199 LEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLH 246
Cdd:pfam15346  101 EAEERLAMLEEQRRMKEERQRREKEEEEREKREQQKILNKKNSRPKLS 148
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
123-248 6.25e-05

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 428669 [Multi-domain]  Cd Length: 860  Bit Score: 47.75  E-value: 6.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   123 ERMSTQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLvkECKQLSGKVLEEaqKLEEVMAKLEEE 202
Cdd:pfam05911  699 ENLEVELARCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 771
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043   203 KKKTSALEEELATEKRRSAEMEA-------QME----KQLSEFDTEREQLRAKLHRE 248
Cdd:pfam05911  772 QQKIEALEVELEEEKNSHEELLAkclelqeQLErnekKESSNCDAAQEDKKLQQEKE 828
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
159-290 6.86e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 47.85  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   159 RLEEERGKnKHVVLMLVKECKQLSGKVLEEaqkLEEVMAKLEEEKkktSALEEELATEKRRSAEMEaQMEKQLSEFDTER 238
Cdd:pfam01576    2 RQEEEMQA-KEEELQKVKEKQQKAESELKE---LEKKHQQLCEEK---NILAEQLQAETELFAEAE-EMRARLAARKQEL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   239 EQ----LRAKLHREEAHTTDLKEEIDKMKKMI----EQLKRGNDSKPSLSLPRKTKDRRL 290
Cdd:pfam01576   74 EEilheLEARLEEEEERSQQLQNEKKKMQQHIqdleEQLEEEEAARQKLQLEKVTTEAKI 133
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
319-723 6.87e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 6.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   319 LKKLPLTVPVKPAAGSPLVSASAKGNACASAASVRPGIERQVSHGDLIGSSLPTVPPPStdrieenGPSTGSTPdLTSSP 398
Cdd:pfam05109  421 FSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPA-------GTTSGASP-VTPSP 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   399 T--------ALPSTVSPASG-HTPTP----PPHSLHSPCANAPlHPGLNPRIQAARFRFQGSNANDPDQnGNTTQSPPSR 465
Cdd:pfam05109  493 SprdngtesKAPDMTSPTSAvTTPTPnatsPTPAVTTPTPNAT-SPTLGKTSPTSAVTTPTPNATSPTP-AVTTPTPNAT 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   466 -----DVSPTSRDTLVAKQLARNTVTQAlsrfTSPPAGAPPRPGAPPTGDVGTYPPVGRTSLKTPGGARVDRGNPPPIPP 540
Cdd:pfam05109  571 iptlgKTSPTSAVTTPTPNATSPTVGET----SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSL 646
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   541 KKPGLSQTPSP---------------PHPQ-LKVIMDSSRASSTGIKADNKTVASSPSSLPQ----GNRVIN----EENL 596
Cdd:pfam05109  647 RPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEVNV 726
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   597 SKSSSPQ---LPPKPSIDLTVAPAGCAVSALATSQVGAwpAETPGLNQPACSEsslviPTTTAFRSSINPVSassrRAGA 673
Cdd:pfam05109  727 TKGTPPKnatSPQAPSGQKTAVPTVTSTGGKANSTTGG--KHTTGHGARTSTE-----PTTDYGGDSTTPRT----RYNA 795
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   674 SDSLLVTASG-----WSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 723
Cdd:pfam05109  796 TTYLPPSTSSklrprWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
Ank_5 pfam13857
Ankyrin repeats (many copies);
755-810 7.44e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 7.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043   755 LLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLA 810
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
174-264 7.81e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.68  E-value: 7.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   174 LVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRS---AEMEAQMEKQLSEfdTEREQLRAKLHREEA 250
Cdd:pfam11600    6 SVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAkeeARRKKEEEKELKE--KERREKKEKDEKEKA 83
                           90
                   ....*....|....
gi 305855043   251 HTTDLKEEIDKMKK 264
Cdd:pfam11600   84 EKLRLKEEKRKEKQ 97
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];
129-269 7.81e-05

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];


Pssm-ID: 223783 [Multi-domain]  Cd Length: 161  Bit Score: 44.60  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  129 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQK-----LEEVMAKLEEE- 202
Cdd:COG0711    32 LKALDERQAKIADDLAEAERLKEEAQALLAEYEQEL-----------EEAREQASEIIEQAKKeaeqiAEEIKAEAEEEl 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  203 KKKTSALEEELATEKRRsaeMEAQMEKQLSEfdtEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:COG0711   101 ERIKEAAEAEIEAEKER---ALEELRAEVAE---LAVAIAEKLLGKKVDEAAQKDLIDAFIAELGEN 161
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
122-250 8.01e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 47.02  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  122 QERMSTQLAAAESRQKKLemeklqLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLEE 201
Cdd:COG4942   134 ALLVSPEDAQRSVRLAIY------YGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAKLAQLLEE 207
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 305855043  202 EKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHREEA 250
Cdd:COG4942   208 RKKTLAQLNSELSADQKKLEELRANesrLKNEIASAEAAAAKAREAAAAAEA 259
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
122-264 8.29e-05

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 46.87  E-value: 8.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  122 QERMSTQ----LAAAESRQKKLEMEKL----QLQALEQEHKKLA---ARLEEERGKNKhvvlmlvKECKQLsgKVLEEAQ 190
Cdd:COG3064   100 QERLKQLekerLKAQEQQKQAEEAEKQaqleQKQQEEQARKAAAeqkKKAEAAKAKAA-------AEAAKL--KAAAEAK 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  191 KLEEVMAKLEEEKKKTSaleEELATEKRRSAEMEAQMEKQLSEFDT-EREQLRAKLHREEAHTTDLKEEIDKMKK 264
Cdd:COG3064   171 KKAEEAAKAAEEAKAKA---EAAAAKKKAEAEAKAAAEKAKAEAEAkAKAEKKAEAAAEEKAAAEKKKAAAKAKA 242
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
129-271 8.55e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 45.77  E-value: 8.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  129 LAAAESRQKKLEMEklqLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLSgkvlEEAQKLEEVMAKLEEekKKTSA 208
Cdd:COG1842    19 LDKAEDPEKMLEQA---IRDMESELAKARQALAQ-----------AIARQKQLE----RKLEEAQARAEKLEE--KAELA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  209 L---EEELAtekRRSAEMEAQMEKQLSEFDTEREQLRAKLHReeahttdLKEEIDKMKKMIEQLKR 271
Cdd:COG1842    79 LqagNEDLA---REALEEKQSLEDLAKALEAELQQAEEQVEK-------LKKQLAALEQKIAELRA 134
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
769-797 9.05e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 9.05e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 305855043   769 NGFTPL-CAAAAQGHFKCVELLIAYDANIN 797
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
UPF0242 pfam06785
Uncharacterized protein family (UPF0242);
187-269 1.02e-04

Uncharacterized protein family (UPF0242);


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 45.20  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   187 EEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTER----EQLRAK--LHREEAHTT-DLKEEI 259
Cdd:pfam06785   87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRleseEQLAEKqlLINEYQQTIeEQRSVL 166
                           90
                   ....*....|
gi 305855043   260 DKMKKMIEQL 269
Cdd:pfam06785  167 EKRQDQIENL 176
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
302-688 1.05e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 436069 [Multi-domain]  Cd Length: 480  Bit Score: 46.83  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   302 TRSVACQTDLVTETAEPlkklpltvpvkpaAGSPLVSASAKGNACASAASVRPGIERQVSHGDLigSSLPTVPPpSTDRI 381
Cdd:pfam17823   80 TEVKAEHTPHGTDLSEP-------------ATREGAADGAASRALAAAASSSPSSAAQSAPTTI--AGLPSLAS-SAPMA 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   382 EenGPSTGSTpdlTSSPTALPSTVSPASgHTPTPP---------PHSLHSPCANAPLHPGLNPRIQAArfrfqGSNANDP 452
Cdd:pfam17823  144 A--APRTNAA---SNAPTAAASSTAAAS-GAPTTAassapatltPASGISTAATATGHPAAGTALAAV-----GNSSPAA 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   453 dqngnTTQSPPSRDVSPTSRDTLVAKqlARNTVTQALSRFTSPPAGAPPRPGAPPTGDVGTYPPVGRTSLKTPG---GAR 529
Cdd:pfam17823  213 -----GTVTAAVGTVTPAALATLAAA--AGTVASAAGTINTGDPHARRLSPAKHMPSDTSARNPAAPSGAQAQGliiQVS 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   530 VDRGNPPPIPPKKPGLSQTPSPPHPQlKVIMDSSRASSTGIKADNKTVASSPSSLPQGNRVINEENLSKSSSPQlpPKPS 609
Cdd:pfam17823  286 TDQPVHNTAGEPTPSPSNTTLEPNTP-KSVASTNLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPS--PLLP 362
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043   610 IDLTVAPAgcavSALATSQVGAwpAETPGLNQPAcsesslviPTTTAFRSSINPVSASSRRAGASDSLLVTASGWSPSL 688
Cdd:pfam17823  363 TQGAAGPG----ILLAPDQVAT--DATAGTASAG--------PTPRSSGDPKMLAMASCQLSTQGQYLVVTTDPLTPAL 427
PTZ00121 PTZ00121
MAEBL; Provisional
119-289 1.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLEEvMAK 198
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-AKK 1541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  199 LEEEKKktsALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHR--EEAHTTDLKEEIDKMKKM-IEQLKRGNDS 275
Cdd:PTZ00121 1542 AEEKKK---ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMkAEEAKKAEEA 1618
                         170
                  ....*....|....
gi 305855043  276 KPSLSLPRKTKDRR 289
Cdd:PTZ00121 1619 KIKAEELKKAEEEK 1632
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
93-245 1.08e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 281941 [Multi-domain]  Cd Length: 218  Bit Score: 45.45  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    93 AGASDKEKKPVctNPLSILEAvmaHCRKMQERMS---TQLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEErgknkh 169
Cdd:pfam04012   12 ANIHEGLDKAE--DPEKMLEQ---AIRDMQSELGkarQALAQVIARQKQLERK------LEEQ-KEQAKKLENK------ 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043   170 VVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKktsaleeelatekrRSAEMEAQMEKQLSEFDTEREQLRAKL 245
Cdd:pfam04012   74 ARAALTKGNEELAREALAEIATLEKLAEALETQLT--------------QQRSAVEQLRKQLAALETKIQQLKAKK 135
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
736-768 1.23e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 1.23e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 305855043   736 DGHSALYSAA-KNGHTDCVRLLLNAEAQVNAADK 768
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
111-267 1.23e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 281941 [Multi-domain]  Cd Length: 218  Bit Score: 45.06  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   111 LEAVMAHCRKMQERMSTQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKHvvlmLVKECKQLSGKVLEEAQ 190
Cdd:pfam04012   46 LAQVIARQKQLERKLEEQKEQAKKLENKAR------AALTKGNEELAREALAEIATLEK----LAEALETQLTQQRSAVE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   191 KLEEVMAKLEeekKKTSALEEELATEKRR--SAEMEAQMEKQLSEFDT--------------EREQLRAKLHREEAHTTD 254
Cdd:pfam04012  116 QLRKQLAALE---TKIQQLKAKKTALKARlkAAKAQEAVNTSLGSASTesatdsferieekiEEREARADAAAELASAQD 192
                          170
                   ....*....|...
gi 305855043   255 LKEEIDKMKKMIE 267
Cdd:pfam04012  193 LDAKLEAAGIQME 205
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
129-269 1.23e-04

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 43.93  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   129 LAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkhvvlmLVKECKQlsgkvleEAQKLeevmakLEEEKKKTSA 208
Cdd:TIGR01144   21 AKAIETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKD-------EAQEI------IENANKRGSE 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043   209 LEEELATEKRrsAEMEAQMEKQLSEFDTEREQLRAKLHREeahTTDL---------KEEIDK------MKKMIEQL 269
Cdd:TIGR01144   77 ILEEAKAEAR--EEREKIKAQARAEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKqaqkdlIDKLVAEL 147
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
176-270 1.23e-04

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223542 [Multi-domain]  Cd Length: 782  Bit Score: 46.78  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  176 KECKQlsgKVLEEA---QKLEEVMAKLEEEKkktsaleEELATEKRRSAEMEAQMEKQLSEFdTEREQLRAkLHREEAHT 252
Cdd:COG0466   178 LEEKQ---EILETLdvkERLEKLLDLLEKEI-------DLLQLEKRIRKKVKEQMEKSQREY-YLREQLKA-IQKELGED 245
                          90
                  ....*....|....*...
gi 305855043  253 TDLKEEIDKMKKMIEQLK 270
Cdd:COG0466   246 DDDKDEVEELREKIEKLK 263
TolA COG3064
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
113-250 1.24e-04

Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225606 [Multi-domain]  Cd Length: 387  Bit Score: 46.48  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  113 AVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQL---QALEQEHKKlaaRLEEERGK----------NKHVVLMLVKECK 179
Cdd:COG3064    59 AVVQQYGRIQSQQSSAKKGEQQRKKKEEQVAEELkpkQAAEQERLK---QLEKERLKaqeqqkqaeeAEKQAQLEQKQQE 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043  180 QLSGKVLEEAQKLEE--VMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQlRAKLHREEA 250
Cdd:COG3064   136 EQARKAAAEQKKKAEaaKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAKKKAEA-EAKAAAEKA 207
PHA02946 PHA02946
ankyin-like protein; Provisional
706-848 1.26e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  706 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFT 772
Cdd:PHA02946   28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043  773 PL--CAAAAQGHFKCVELLIAYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGN 848
Cdd:PHA02946  108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
123-271 1.33e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 46.69  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   123 ERMSTQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKHvvlmLVKECKQLSGKVLEEAQKLEEVMA---KL 199
Cdd:pfam01576   60 EEMRARLAA-----RKQELEEI-LHELE-------ARLEEEEERSQQ----LQNEKKKMQQHIQDLEEQLEEEEAarqKL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   200 EEEKKKTSA----LEEE---LATEKRRSAEMEAQMEKQLSEFDT----EREQLR--AKL-HREEAHTTDLKEEIDKMKKM 265
Cdd:pfam01576  123 QLEKVTTEAkikkMEEDillLEDQNNKLQKERKLLEERISEFTSnlaeEEEKSKslNKLkNKHEAMISDLEDRLKKEEKG 202

                   ....*....
gi 305855043   266 ---IEQLKR 271
Cdd:pfam01576  203 rqeLEKAKR 211
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
108-271 1.41e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 46.76  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   108 LSILEAVMAHCRKMQERMSTQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKHVV 171
Cdd:pfam12128  606 LDKAEEALQSAREKQAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   172 lMLVKECKQLSGKV---LEE--AQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLH 246
Cdd:pfam12128  686 -SLEAQLKQLDKKHqawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLG 764
                          170       180
                   ....*....|....*....|....*
gi 305855043   247 REEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam12128  765 VDPDVIAKLKREIRTLERKIERIAV 789
PHA02791 PHA02791
ankyrin-like protein; Provisional
737-849 1.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 45.42  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  737 GHSALYSAAKNGHTDCVRLLLNAEAQVNAADkNGFtPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNK 816
Cdd:PHA02791   30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107
                          90       100       110
                  ....*....|....*....|....*....|....
gi 305855043  817 ECIKLLLEAGTDRSVKTRDGW-TPIHAAVDTGNV 849
Cdd:PHA02791  108 QTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDV 141
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
769-797 1.55e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.55e-04
                            10        20
                    ....*....|....*....|....*....
gi 305855043    769 NGFTPLCAAAAQGHFKCVELLIAYDANIN 797
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PRK12704 PRK12704
phosphodiesterase; Provisional
175-271 1.64e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  175 VKECKQLSGKVLEEAQKLEEVMAKL------EEEKKKTSALEEELATEK-------RRSAEMEAQMEKQLSEFDTEREQL 241
Cdd:PRK12704   33 IKEAEEEAKRILEEAKKEAEAIKKEalleakEEIHKLRNEFEKELRERRnelqkleKRLLQKEENLDRKLELLEKREEEL 112
                          90       100       110
                  ....*....|....*....|....*....|....
gi 305855043  242 ---RAKLHREEAHTTDLKEEIDKM-KKMIEQLKR 271
Cdd:PRK12704  113 ekkEKELEQKQQELEKKEEELEELiEEQLQELER 146
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
179-464 1.66e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 427171 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   179 KQLSGKVLEEAQKLEEvMAKLEEEKKKTSALEEELATEKRrSAEMEAQMEKQLSEFDTEREQLRAklhreeahttdLKEE 258
Cdd:pfam03154   63 KKSSKKIKEEAPSPLK-SAKRQREKGASDTEEPERATAKK-SKTQEISRPNSPSEGEGESSDGRS-----------VNDE 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   259 IDKMKKMIEQLKRgnDSKPSLSLPRKTKDRrlvsisvategpmTRSVACQTDLvtETAEPLKKLPLTVPVKPAAGSPLVS 338
Cdd:pfam03154  130 GSSDPKDIDQDNR--STSPSIPSPQDNESD-------------SDSSAQQQIL--QTQPPVLQAQSGAASPPSPPPPGTT 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   339 ASAKGNACASAASVRPgierQVShgdligsslPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTVSPASGHTPTPPP- 417
Cdd:pfam03154  193 QAATAGPTPSAPSVPP----QGS---------PATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPs 259
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 305855043   418 ----HSLHSPCANAPLHPGLNPrIQAARFRFQGSNANDP---DQNGNTTQSPPS 464
Cdd:pfam03154  260 qvspQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVPPQPfplTPQSSQSQVPPG 312
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
121-234 1.88e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 433535 [Multi-domain]  Cd Length: 119  Bit Score: 42.57  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   121 MQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLSGKVLEEAQKLEEVMAKLE 200
Cdd:pfam13863   11 VQLALDAKREEIQRLEELLKQREEELEKKEQELKEDLVKFDK-----------FLKENDAKRRRALKKAEEETKLKKEKE 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 305855043   201 EEKKKTSALEEELATEKRRsaemeaqMEKQLSEF 234
Cdd:pfam13863   80 KEIKKLTAQLEELKSEISK-------LEETLEEY 106
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
803-834 1.95e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.95e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 305855043   803 GQTPLYLAC-KNGNKECIKLLLEAGTDRSVKTR 834
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
DUF4207 pfam13904
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several ...
130-233 2.01e-04

Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 433570 [Multi-domain]  Cd Length: 223  Bit Score: 44.70  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   130 AAAESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQklEEV 195
Cdd:pfam13904   65 AKQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEA 142
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 305855043   196 MAKLEE-EKKKTSALEE--ELATEKRRSAEMEAQMEKQLSE 233
Cdd:pfam13904  143 KEVLQEwELKKLEQQQRkrEEEQREQLKKEEEEQERKQLAE 183
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
705-856 2.32e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  705 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCE----DGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNG--FT------ 772
Cdd:cd22192    53 TALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknl 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  773 ------PLCAAAAQGHFKCVELLIAYDANInHAADG-GQTPLYL----ACKNGNKECIKLLLEA-GTDRS-----VKTRD 835
Cdd:cd22192   133 iyygehPLSFAACVGNEEIVRLLIEHGADI-RAQDSlGNTVLHIlvlqPNKTFACQMYDLILSYdKEDDLqpldlVPNNQ 211
                         170       180
                  ....*....|....*....|.
gi 305855043  836 GWTPIHAAVDTGNVDSLKLLM 856
Cdd:cd22192   212 GLTPFKLAAKEGNIVMFQHLV 232
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
133-271 2.42e-04

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: 46.12  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   133 ESRQKKLEMEKLQLQALEQEHKK--LAARLEEERGKNKHV---VLMLVKECKQLSGKVLE-EAQKLEEVMAKLEEEKKKT 206
Cdd:pfam02463  202 LKEQAKKALEYYQLKEKLELEEEylLYLDYLKLNEERIDLlqeLLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043   207 SALEEELA--TEKRRSAEMEAQMEKQLSEFDTEREQL-RAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam02463  282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
136-271 2.49e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   136 QKKLEMEKL---------QLQALEQEHKKLAARLEE---ERGKNKHVVLMLVKECKQLSGKV--LEEAQK-LEEVMAKLE 200
Cdd:TIGR04523  451 VKELIIKNLdntresletQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVkdLTKKISsLKEKIEKLE 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   201 EEKK----KTSALEEELatEKRRSAEMEAQMEKQLSEFDTEREQLR--------------AKLHREEAHTTDLKEEIDKM 262
Cdd:TIGR04523  531 SEKKekesKISDLEDEL--NKDDFELKKENLEKEIDEKNKEIEELKqtqkslkkkqeekqELIDQKEKEKKDLIKEIEEK 608

                   ....*....
gi 305855043   263 KKMIEQLKR 271
Cdd:TIGR04523  609 EKKISSLEK 617
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
128-245 2.56e-04

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 41.82  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   128 QLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkhvvLMLVKE---CKQLSGKVLEEaQKLEEVMAKLEEEKK 204
Cdd:pfam01920    3 KFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERKE 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 305855043   205 KtsaLEEELATekrrsaemeaqMEKQLSEFDTEREQLRAKL 245
Cdd:pfam01920   70 T---LEKEIKT-----------LEKQLEKLEKELEELKEEL 96
PTZ00121 PTZ00121
MAEBL; Provisional
119-321 2.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  119 RKMQERMSTQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlmlVKECKqlsgKVLEEAQKLEEVMAK 198
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKK--------ADEAK----KKAEEAKKKADEAKK 1504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  199 LEEEKKKtsALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDSKPS 278
Cdd:PTZ00121 1505 AAEAKKK--ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK 1582
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 305855043  279 LSLPRKTKDRRL--VSISVATEGPMTRSVACQTDLVTETAEPLKK 321
Cdd:PTZ00121 1583 AEEAKKAEEARIeeVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
64-270 2.77e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.73  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    64 ARRKEVFIQERygrfNLNDPFLALQRDYEAgasDKEKKPVCTNPLSIL--EAVMAHCRKMQER-MSTQLAAAESrQKKLE 140
Cdd:TIGR00618  365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILqrEQATIDTRTSAFRdLQGQLAHAKK-QQELQ 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   141 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKHVVLMLVKECKQLSGKVLEEAQKLEEVMAK--LEEEKK 204
Cdd:TIGR00618  437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscIHPNPA 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   205 KTSALEEELATEK-----RRSAEMEAQMEKQLSEFDTEREQ---LRAKLHREEAHT-------TDLKEEIDKMKKMIEQL 269
Cdd:TIGR00618  517 RQDIDNPGPLTRRmqrgeQTYAQLETSEEDVYHQLTSERKQrasLKEQMQEIQQSFsiltqcdNRSKEDIPNLQNITVRL 596

                   .
gi 305855043   270 K 270
Cdd:TIGR00618  597 Q 597
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
141-270 3.07e-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: 45.82  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   141 MEKLQLQA-LEQEHKKLAARLEEergKNKHVvlmLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRR 219
Cdd:TIGR02168  202 LKSLERQAeKAERYKELKAELRE---LELAL---LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043   220 SAEMEAQMEKQ----------LSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:TIGR02168  276 VSELEEEIEELqkelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
52-269 3.07e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   52 LEARDLVIEALRARRKEvfIQErygrfnLNDPFLALQRDYEAGASDKEkkpvctnplSILEAVmahcRKMQERMSTQLAA 131
Cdd:PRK02224  236 RDEADEVLEEHEERREE--LET------LEAEIEDLRETIAETERERE---------ELAEEV----RDLRERLEELEEE 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  132 AESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlmlVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEE 211
Cdd:PRK02224  295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  212 ELATEKRRSAEMEAQMEKQLSEFDTEREQLRAK-------LHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:PRK02224  367 ELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAEL 431
TACC pfam05010
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins ...
136-270 3.13e-04

Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins TACC 1, 2 and 3 the genes for which are found concentrated in the centrosomes of eukaryotic and may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumor suppressor (AZU-1). The functional homolog (Alp7) in Schizosaccharomyces pombe has been shown to be required for organisation of bipolar spindles.


Pssm-ID: 428254 [Multi-domain]  Cd Length: 201  Bit Score: 43.52  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   136 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKHVvlmlvkeckqlsGKVLEEAqklEEVMAKLEEEKKKtsalEE 211
Cdd:pfam05010    3 QKDLDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEEQK----QK 63
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043   212 ELAtekrrsaemEAQMEKQLSEfdteREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:pfam05010   64 ELS---------HQEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
LUC7 pfam03194
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
86-274 3.28e-04

LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).


Pssm-ID: 427192 [Multi-domain]  Cd Length: 246  Bit Score: 44.12  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    86 ALQRDYEAgASDKEKKPVCTnplsilEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEERG 165
Cdd:pfam03194   64 ALKADYEK-ASKRKKKYGYE------REFLRFLQKLIDDVDRKIRKGKQRLELTQEEIEQTDELKQEQISE---LEEKIK 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   166 KnkhvvlmLVKECKQL--SGKVlEEAQKLEEVMAKLEEEKKktsALEEELATEKRRSAEM-EAQME------KQLSEFDT 236
Cdd:pfam03194  134 K-------LLEEAEELgeEGNV-DEAQKLMKKVEELKEEKE---ELEQQYESLTKESAASqEKKMEvcevcgAFLIVNDA 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 305855043   237 ER---EQLRAKLH------REEAhtTDLKEEIDKmKKMIEQLKRGND 274
Cdd:pfam03194  203 DRrlaDHLTGKQHlgyakiRDTL--EELKEKIEE-RREEREERREKR 246
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
192-270 3.37e-04

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 431138 [Multi-domain]  Cd Length: 187  Bit Score: 43.33  E-value: 3.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043   192 LEEVMAKLEEEKKKtsaLEEELATEKRRSAEMEAQMEKQLSEfdtereqlraklhREEAHttdlKEEIDKMKKMIEQLK 270
Cdd:pfam10211  124 LEKKIADLEEEKEE---LEKQVAELKAKCEAIEKREEERRQA-------------EEKKH----AEEIAFLKKTNQQLK 182
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
735-915 3.40e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  735 EDGHSALYSAA---KNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGH-----------FKCVELLIAYDANINHAA 800
Cdd:cd21882    24 ATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADVSARA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  801 DG-------------GQTPLYLACKNGNKECIKLLLEAGTD-RSVKTRD--GWTPIHAAVDTGN--VDSLKLL--MYHGA 860
Cdd:cd21882   104 TGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYNLL 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  861 PAHGNKLQeepglaifdldqeehhegtskPVVPADLI-NHadsEGWTAAHIAASKG 915
Cdd:cd21882   184 LSYGAHLD---------------------PTQQLEEIpNH---QGLTPLKLAAVEG 215
PRK12705 PRK12705
hypothetical protein; Provisional
128-280 3.64e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 45.09  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  128 QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSgkvlEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PRK12705   40 QEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLD----ARAEKLDNLENQLEEREKALS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  208 ALEEELATEKR-------RSAEMEAQMEKQ--LSEFDTEREQLRAKLHR---EEAHTTDLKEEIDKMKKMIEQLKRGNDS 275
Cdd:PRK12705  116 ARELELEELEKqldnelyRVAGLTPEQARKllLKLLDAELEEEKAQRVKkieEEADLEAERKAQNILAQAMQRIASETAS 195

                  ....*
gi 305855043  276 KPSLS 280
Cdd:PRK12705  196 DLSVS 200
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-242 4.24e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  133 ESRQKKLEMEKLQLQALEQEHKKLAARLEEERGK-NKHVVLMLVKECKQLSGKVLEEAQKLEEVMAKLE--EEKKKTSA- 208
Cdd:PRK03918  615 EREEKELKKLEEELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEelEKRREEIKk 694
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 305855043  209 ----LEEELatEKRRSAEMEAQ-MEKQLSEFDTEREQLR 242
Cdd:PRK03918  695 tlekLKEEL--EEREKAKKELEkLEKALERVEELREKVK 731
TACC pfam05010
Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins ...
133-274 4.25e-04

Transforming acidic coiled-coil-containing protein (TACC); This family contains the proteins TACC 1, 2 and 3 the genes for which are found concentrated in the centrosomes of eukaryotic and may play a conserved role in organising centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumor suppressor (AZU-1). The functional homolog (Alp7) in Schizosaccharomyces pombe has been shown to be required for organisation of bipolar spindles.


Pssm-ID: 428254 [Multi-domain]  Cd Length: 201  Bit Score: 43.14  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   133 ESRQKKLEMEKLQLQALEQEHKKLAARLEE-ERGKNKhvvlmLVKECKQLSGkVLEEAQKLEEVMakleeeKKKTSALEE 211
Cdd:pfam05010   57 EEEQKQKELSHQEIQKVLEEKDQALADLNSvEKSFSD-----LFKRYEKQKE-VISGYKKNEEVL------KKCAQEYLA 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043   212 ELATEKRRSAEMEAQMEKQL-----------SEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGND 274
Cdd:pfam05010  125 RIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAQAETAALQASLRKEQMKVQSLERTLEQKTKENEELTKICD 198
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
119-290 4.39e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAEsRQKKLEMEKLQLqALEQEHKKLAARLEEERGKNKHV----VLMLVKECKQLSGKVLEEAQKLEE 194
Cdd:pfam17380  316 RKLEEAEKARQAEMD-RQAAIYAEQERM-AMERERELERIRQEERKRELERIrqeeIAMEISRMRELERLQMERQQKNER 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   195 VMAKLE---------EEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHR-EEAHTTDL--KEEIDKM 262
Cdd:pfam17380  394 VRQELEaarkvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEqERQQQVERlrQQEEERK 473
                          170       180
                   ....*....|....*....|....*...
gi 305855043   263 KKMIEQLKRGNDSKPSLSLPRKTKDRRL 290
Cdd:pfam17380  474 RKKLELEKEKRDRKRAEEQRRKILEKEL 501
DUF812 pfam05667
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ...
33-271 4.54e-04

Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.


Pssm-ID: 428574 [Multi-domain]  Cd Length: 601  Bit Score: 45.00  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    33 VDTLSKSELRMLLSVMEGELEARDL--VIEALRARRKEVFIQERYGRFNLNDPFlALQRDYEAGASDKEKKPVCTNPLSI 110
Cdd:pfam05667  253 AEQLRSAALASTEATSGASRSKQDLaeLLSSFGGSSTTDTNLTKGSRFTHTEKL-QFTNEEAPAATSSPPTKAETEEELQ 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   111 L--EAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknkhvvlMLVKEckqlsgKVLEE 188
Cdd:pfam05667  332 QqrEEELEELQEQLEELESSIEELEKEIKKLESSIKQVEEELEELKEQNEELEKQ---------YKVKK------KTLDL 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   189 AQKLEEVMAKLEEEKKKTSAleeelatekrRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEI----DKMKK 264
Cdd:pfam05667  397 LPDAEENIAKLQALVEASAQ----------RLVELAGQWEKHRVPLIEEYRALKEAKSNKESESQRKLEEIkelrEKIKE 466

                   ....*..
gi 305855043   265 MIEQLKR 271
Cdd:pfam05667  467 VAEEARS 473
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
130-295 4.80e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  130 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQK-LEEVMAKL-EEEKKKTS 207
Cdd:PRK00409  523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeADEIIKELrQLQKGGYA 602
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  208 ALEEELATEKRRS---AEMEAQMEKQLSEFDTEREQL--RAKLHR--------EEAHTTDLKEEID--KMKKMIEQLKRG 272
Cdd:PRK00409  603 SVKAHELIEARKRlnkANEKKEKKKKKQKEKQEELKVgdEVKYLSlgqkgevlSIPDDKEAIVQAGimKMKVPLSDLEKI 682
                         170       180
                  ....*....|....*....|...
gi 305855043  273 NDSKPSLSLPRKTKDRRLVSISV 295
Cdd:PRK00409  683 QKPKKKKKKKPKTVKPKPRTVSL 705
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
736-765 4.88e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 4.88e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 305855043    736 DGHSALYSAAKNGHTDCVRLLLNAEAQVNA 765
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK12704 PRK12704
phosphodiesterase; Provisional
51-228 4.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   51 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGASDKEKKpvctnpLSILEAVMahcRKMQERMSTQLA 130
Cdd:PRK12704   37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkhvvlmlvkeckqlsgKVLEEAQKLEEVMAKLEEEKKKT--SA 208
Cdd:PRK12704  104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162
                         170       180
                  ....*....|....*....|...
gi 305855043  209 LEEELATEKR---RSAEMEAQME 228
Cdd:PRK12704  163 VEEEARHEAAvliKEIEEEAKEE 185
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
371-704 5.14e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  371 PTVPPPStDRIEENGPSTGSTPDLTSSPTAL--------PSTVSPASGHTPTPPPHSLHSPCANAPLHPGLNPRIQAARF 442
Cdd:PHA03307   68 PTGPPPG-PGTEAPANESRSTPTWSLSTLAPasparegsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGP 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  443 RFQGSNANDPDQNGNTTQSPPSR-------DVSPTSRDTLVAKQLARNTVTQALSRFTSPPAGAPPRPGAPPTGDvgtyP 515
Cdd:PHA03307  147 PPAASPPAAGASPAAVASDAASSrqaalplSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPA----P 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  516 PVGRTSLKTPGGARVDRGNPPPIPPKKPGLSQTPSpPHPQLKVIMDSSRASSTGIKADNKTVASSPSSLPQGNRVINEEn 595
Cdd:PHA03307  223 APGRSAADDAGASSSDSSSSESSGCGWGPENECPL-PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSP- 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  596 lSKSSSPQLPPKPSIDLTVAPAGCAVSAlATSQVGAWPAETPGLNQPACSESslviPTTTAFRSSINPVSASSRRAGASD 675
Cdd:PHA03307  301 -SSPGSGPAPSSPRASSSSSSSRESSSS-STSSSSESSRGAAVSPGPSPSRS----PSPSRPPPPADPSSPRKRPRPSRA 374
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 305855043  676 SLLVTASGWSPS--------LTPLLMSGGPAPL-AGRP 704
Cdd:PHA03307  375 PSSPAASAGRPTrrraraavAGRARRRDATGRFpAGRP 412
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
803-828 5.27e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 5.27e-04
                           10        20
                   ....*....|....*....|....*.
gi 305855043   803 GQTPLYLACKNGNKECIKLLLEAGTD 828
Cdd:pfam13606    2 GNTPLHLAARNGNLEIVKLLLERGAD 27
COG5022 COG5022
Myosin heavy chain [General function prediction only];
123-342 5.64e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  123 ERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKN---KHVVLMLVKECkqlsgKVLEEAQKLEEVMAKL 199
Cdd:COG5022   810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSlkaKKRFSLLKKET-----IYLQSAQRVELAERQL 884
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  200 EEEK---KKTSALE------EELATEKRRSAEMEAQMEKQ-LSEFDTEREQL-------------------RAKLHREEA 250
Cdd:COG5022   885 QELKidvKSISSLKlvnlelESEIIELKKSLSSDLIENLEfKTELIARLKKLlnnidleegpsieyvklpeLNKLHEVES 964
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  251 HTTDLKEEIDKMKKMIEQLKRgnDSKPSLSLPRKTKdRRLVSISvategpmtrsvaCQTDLVTETAEPLKKLPLTVPVKP 330
Cdd:COG5022   965 KLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAELQ 1029
                         250
                  ....*....|..
gi 305855043  331 AAGSPLVSASAK 342
Cdd:COG5022  1030 SASKIISSESTE 1041
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
145-271 5.99e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  145 QLQALEQEHKKLAA---RLEEERGKnkhvvlmlVKECKQLSGKVLEE-AQKLEEVmAKLEEEKKKTSALEEELATEKRRS 220
Cdd:PRK02224  207 RLNGLESELAELDEeieRYEEQREQ--------ARETRDEADEVLEEhEERREEL-ETLEAEIEDLRETIAETEREREEL 277
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 305855043  221 AEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:PRK02224  278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
PHA02798 PHA02798
ankyrin-like protein; Provisional
751-859 6.16e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  751 DCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLIAYdanINHAAD------GGQTPLYLACKNGNK---ECIKL 821
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM---IENGADttlldkDGFTMLQVYLQSNHHidiEIIKL 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 305855043  822 LLEAGTD-RSVKTRDGWTPIHA----AVDTGNVDSLKLLMYHG 859
Cdd:PHA02798  167 LLEKGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFVDNG 209
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
142-273 6.23e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumor suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 429649 [Multi-domain]  Cd Length: 353  Bit Score: 43.82  E-value: 6.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   142 EKLQLQALEQEHKKLAARLEEERgknkhvvlmlvkeckqlsgkVLEEAQKLEEVmAKLEEEKKKTSA--LEEELATEKRR 219
Cdd:pfam07767  198 QELLQKAVEAEKKRLKEEEKLER--------------------VLEKIAESAAT-AEAREEKRKTKAqrNKEKRRKEEER 256
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 305855043   220 SAEMEAQMEKQLSEFDTEREqLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGN 273
Cdd:pfam07767  257 EAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKKL 309
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
126-271 6.79e-04

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: 44.58  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   126 STQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvVLMLVKECKQLSGKVLEEAqklEEVMAKLEEEKKK 205
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEE---EKEKKLQEEELKL 290
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   206 TSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEID-------KMKKMIEQLKR 271
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKeleikreAEEEEEEELEK 363
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
835-860 6.88e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 6.88e-04
                            10        20
                    ....*....|....*....|....*.
gi 305855043    835 DGWTPIHAAVDTGNVDSLKLLMYHGA 860
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
NOPS_NONA_like cd12945
NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from ...
199-242 6.93e-04

NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from invertebrate species; The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension , found in Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA), Chironomus tentans hrp65 gene encoding protein Hrp65 and similar proteins. D. melanogaster NONA is involved in eye development and behavior, and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies.


Pssm-ID: 240580 [Multi-domain]  Cd Length: 100  Bit Score: 40.42  E-value: 6.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 305855043  199 LEEEKKKTSALEEELATEKRRsaeMEAQMEKQLSEFDTE--REQLR 242
Cdd:cd12945    58 HELYKQKEEALKRELKMEEEK---LEAQMEYARYEHETEllREQLR 100
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
82-275 7.73e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.04  E-value: 7.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    82 DPFLALQRDYEAGASDKEKKpvctnpLSILEAVMAhcRKMqermstqlaaaesrqKKLEMEKLQLQALEQEHKKLAARLE 161
Cdd:pfam10174  582 ERLLGILREVENEKNDKDKK------IAELESLTL--RQM---------------KEQNKKVANIKHGQQEMKKKGAQLL 638
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   162 EERGKNKhvvlMLVKECKQLSgKVLEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSE-FDTEREQ 240
Cdd:pfam10174  639 EEARRRE----DNLADNSQQL-QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEA 713
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 305855043   241 LRAKLHREEAHTTDLKEEIDKMKKMIEQ---LKRGNDS 275
Cdd:pfam10174  714 LLAAISEKDANIALLELSSSKKKKTQEEvmaLKREKDR 751
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
138-276 7.75e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   138 KLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGK--VLEEAQK---------------LEEVMAKLE 200
Cdd:TIGR04523  198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKttEISNTQTqlnqlkdeqnkikkqLSEKQKELE 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   201 EEKKKTSALEEELAT--------EKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRG 272
Cdd:TIGR04523  278 QNNKKIKELEKQLNQlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357

                   ....
gi 305855043   273 NDSK 276
Cdd:TIGR04523  358 NSEK 361
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
53-254 7.91e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 43.52  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   53 EARDLVIE---ALRARRKEVF--IQERY----------GRFNLNDPFL-ALQRDYEagasdKEKKPVCTNPLSI-----L 111
Cdd:COG1340    62 EERDEINEevqELKEKRDEINakLQELRkeyrelkekrNEFNLGGRSIkSLEREIE-----RLEKKQQTSVLTPeeereL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  112 EAVMAHCRKMQERMSTQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQK 191
Cdd:COG1340   137 VQKIKELRKELEDAKKALEENEKLKELKA-EIDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEADELRKEADELHEE 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  192 LEEVMAKLEEEKKKTSALEEELA-TEKR----RSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTD 254
Cdd:COG1340   216 FVELSKKIDELHEEFRNLQNELReLEKKikalRAKEKAAKRREKREELKERAEEIYEKFKRGEKLTTE 283
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];
184-271 8.09e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion];


Pssm-ID: 223783 [Multi-domain]  Cd Length: 161  Bit Score: 41.90  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  184 KVLEEAQKL-EEVMAKLEEEKKKTSALEE-------ELATEKRRSAEMEAQ--MEKQLSEFDTEREQLRAKLHREEAHTT 253
Cdd:COG0711    51 RLKEEAQALlAEYEQELEEAREQASEIIEqakkeaeQIAEEIKAEAEEELEriKEAAEAEIEAEKERALEELRAEVAELA 130
                          90
                  ....*....|....*...
gi 305855043  254 DLKEEIDKMKKMIEQLKR 271
Cdd:COG0711   131 VAIAEKLLGKKVDEAAQK 148
PHA02884 PHA02884
ankyrin repeat protein; Provisional
741-858 8.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  741 LYSAAKNGHtDCVRLLLNAEAQVNA-ADKNGFTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLA---CKNGNK 816
Cdd:PHA02884   75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNNFLA 153
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 305855043  817 ECIKllleagtDRSVKTrdgwTPIHAAVDTGNVDSLKLLMYH 858
Cdd:PHA02884  154 FMIC-------DNEISN----FYKHPKKILINFDILKILVSH 184
PHA02875 PHA02875
ankyrin repeat protein; Provisional
774-859 8.81e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  774 LCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNVDSLK 853
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                  ....*.
gi 305855043  854 LLMYHG 859
Cdd:PHA02875   86 ELLDLG 91
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
127-270 8.86e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  127 TQLAAAEsrqKKLEMEKLQLQALEQEhkklAARLEEERGKNKhvvlmlvkeckqlsgkvleeaQKLEEVMAKLEEEKKKt 206
Cdd:cd16269   191 QALTEKE---KEIEAERAKAEAAEQE----RKLLEEQQRELE---------------------QKLEDQERSYEEHLRQ- 241
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043  207 saLEEELATEKRRsaeMEAQMEKQLSefdtEREQLRAKLHREEahttdLKEEIDKMKKMIEQLK 270
Cdd:cd16269   242 --LKEKMEEEREN---LLKEQERALE----SKLKEQEALLEEG-----FKEQAELLQEEIRSLK 291
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
94-250 9.75e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    94 GASDKEKKPVCTNPLSILEAVM-------AHCRKMQERMSTQLAAAESRQKKLEMEKLQL---QALEQEH-KKLAARLEE 162
Cdd:TIGR02794   21 GSLYHSVKPEPGGGAEIIQAVLvdpgavaQQANRIQQQKKPAAKKEQERQKKLEQQAEEAekqRAAEQARqKELEQRAAA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   163 ErgknkhvvlmlvKECKQLsgkvlEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLR 242
Cdd:TIGR02794  101 E------------KAAKQA-----EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163

                   ....*...
gi 305855043   243 AKLHREEA 250
Cdd:TIGR02794  164 AKKKAEEA 171
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
119-271 1.00e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHK-KLAARLEEERGKNKHVVLMLVKECKQlsgKVLEEAQKLEEVMA 197
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKA---KQAAEAKAKAEAEA 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   198 ----------KLEEEKKKTSALEEEL-ATEKRRSAEMEAQmEKQLSEFDTEREQLRAKlhreeAHTTDLKEEID-KMKKM 265
Cdd:TIGR02794  141 erkakeeaakQAEEEAKAKAAAEAKKkAEEAKKKAEAEAK-AKAEAEAKAKAEEAKAK-----AEAAKAKAAAEaAAKAE 214

                   ....*.
gi 305855043   266 IEQLKR 271
Cdd:TIGR02794  215 AEAAAA 220
PRK00106 PRK00106
ribonuclease Y;
140-271 1.02e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 43.70  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  140 EMEKLQLQALEQEHKKLAARLEEERgknKHVVLMLVKECKQLSGKVLEEAQkleevmaklEEEKKKTSALEEELATEKRR 219
Cdd:PRK00106   31 EAAELTLLNAEQEAVNLRGKAERDA---EHIKKTAKRESKALKKELLLEAK---------EEARKYREEIEQEFKSERQE 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  220 SAEMEAQMEKQLSEFDTEREQLRAK---LHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:PRK00106   99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
130-269 1.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  130 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkhvvlmlvkeckqlsgkvLEEAQKLEEVMAKLEEEKKktsAL 209
Cdd:PRK02224  469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERRE---DL 521
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305855043  210 EEELATEKRRSAEMEAQME---KQLSEFDTEREQLRAKL---------HREEAHT-----TDLKEEIDKMKKMIEQL 269
Cdd:PRK02224  522 EELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAaeaeeeaeeAREEVAElnsklAELKERIESLERIRTLL 598
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
40-267 1.09e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    40 ELRMLLSVMEGELE--ARDLVIEALRARRKEvfiQERYGRFNLNDPfLALQRDYEAGASDKEKKPVC-TNPLSILEAVMA 116
Cdd:TIGR00618  640 ELALKLTALHALQLtlTQERVREHALSIRVL---PKELLASRQLAL-QKMQSEKEQLTYWKEMLAQCqTLLRELETHIEE 715
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   117 HCRKMQErmstQLAAAESRQKKLEmeklqlqaleQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVLEEAQKLeevm 196
Cdd:TIGR00618  716 YDREFNE----IENASSSLGSDLA----------AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG---- 777
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305855043   197 AKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEidKMKKMIE 267
Cdd:TIGR00618  778 AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE--KSATLGE 846
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
115-244 1.12e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 43.17  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  115 MAHCRKMQERMSTQLAAAESRQKKlemEKLQLQALEQEHKKLAARLEEErgknkhvvlmlvkeckqlsgkVLEEAQKLEE 194
Cdd:COG4942   173 LAAVRAEIAAEQAELTTLLSEQRA---QQAKLAQLLEERKKTLAQLNSE---------------------LSADQKKLEE 228
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 305855043  195 VMAKLEEEKKKTSALEEELAT--EKRRSAEMEAQMEKQLSEfdtEREQLRAK 244
Cdd:COG4942   229 LRANESRLKNEIASAEAAAAKarEAAAAAEAAAARARAAEA---KRTGETYK 277
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
97-266 1.14e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 43.61  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    97 DKEKKPVCTNPLSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEE-ERGKNK-----HV 170
Cdd:pfam01576  508 EEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRE---LEALTQRLEEKAAAYDKlEKTKNRlqqelDD 584
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   171 VLMLVKECKQLSGKvLEEAQKLEEVMakLEEEKKKTSALEEElatekRRSAEMEAQmekqlsefdtEREQLRAKLHREEA 250
Cdd:pfam01576  585 LLVDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARYAEE-----RDRAEAEAR----------EKETKALSLARALE 646
                          170
                   ....*....|....*.
gi 305855043   251 HTTDLKEEIDKMKKMI 266
Cdd:pfam01576  647 EALDAKEELERQNKQL 662
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
112-268 1.26e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.05  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  112 EAVMAHCRKMQERMSTQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkhvvlmlvKECKQLSGKVLEEAQK 191
Cdd:cd00176    75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  192 LEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTER-EQLRAKLHReeahttdLKEEIDKMKKMIEQ 268
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
mukB PRK04863
chromosome partition protein MukB;
53-243 1.32e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   53 EARDLVIEALRARRKEVFIQERYG--RFNLND--PFLALQRDYEAGASDKEKK-PVCTNPLSILEAVMAHCRKMQERMST 127
Cdd:PRK04863  493 EAWDVARELLRRLREQRHLAEQLQqlRMRLSEleQRLRQQQRAERLLAEFCKRlGKNLDDEDELEQLQEELEARLESLSE 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  128 QLAaaESRQKKLEMEKlQLQALEQEHKKLAARLEEERgkNKHVVLMLVKECkqlSGKVLEEAQKLEEVMAKLEEEKKKTS 207
Cdd:PRK04863  573 SVS--EARERRMALRQ-QLEQLQARIQRLAARAPAWL--AAQDALARLREQ---SGEEFEDSQDVTEYMQQLLERERELT 644
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 305855043  208 ALEEELATEKRRsaeMEAQMEKqLSEFDT-EREQLRA 243
Cdd:PRK04863  645 VERDELAARKQA---LDEEIER-LSQPGGsEDPRLNA 677
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
172-322 1.40e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 43.17  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  172 LMLVKECKQLSGKVLEEAQK-LEEVMAKLEEEKKKTSALEEELATEKRRSaemeAQMEKQLSEFDTEREQLRAKLHREEA 250
Cdd:COG4942    26 VLAAAFSAAADDKQLKQIQKeIAALEKKIREQQDQRAKLEKQLKSLETEI----ASLEAQLIETADDLKKLRKQIADLNA 101
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  251 HTTDLK----EEIDKMKKMIEQLKRGNDsKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLVTETAEPLKKL 322
Cdd:COG4942   102 RLNALEvqerEQRRRLAEQLAALQRSGR-NPPPALLVSPEDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAV 176
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
99-270 1.43e-03

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 42.88  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   99 EKKPVCTNPLSileavmahCRKMQErmSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKhvvlmlvKEC 178
Cdd:COG4487     4 IKVPIQTKPFT--------IPKCED--SIKGEQARYKQIEQEDQSRILNTLEEFEKEANEKRAQYRSAKK-------KEL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  179 KQLSGKVLEEAqklEEVMAKLEEEKKKtsalEEELATEKRRSAEMEAQMEKqlsEFDTEREQLRAKL-HREEAHTTDLKE 257
Cdd:COG4487    67 SQLEEQLINQK---KEQKNLFNEQIKQ----FELALQDEIAKLEALELLNL---EKDKELELLEKELdELSKELQKQLQN 136
                         170
                  ....*....|...
gi 305855043  258 EIDKMKKMIEQLK 270
Cdd:COG4487   137 TAEIIEKKRENNK 149
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
160-270 1.47e-03

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  160 LEEERGknkhvVLMLVKECKQLSGKVLEEAQKLEEVMAKLEEEKKKTSALEEElATEKRRSAEMEAQMEK--------QL 231
Cdd:COG1196   161 IEEAAG-----VSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQ-AEKAERYQELKAELRElelalllaKL 234
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 305855043  232 SEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELK 273
PARM pfam17061
PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present ...
323-419 1.71e-03

PARM; Human PARM-1 is a mucin-like, androgen-regulated transmembrane protein that is present in most tissues, with high levels in the heart, kidney and placenta. It has been shown to be induced and expressed in prostate after castration and may have a role in cell proliferation and immortalisation in prostate cancer.


Pssm-ID: 435714 [Multi-domain]  Cd Length: 296  Bit Score: 42.15  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   323 PLT-VPVKPAAGSPLVSASAKGNACASAASVRPGIERQVSHGDLIGSSLPTVPPPStdrIEENGPSTGSTPDLTSSPTAL 401
Cdd:pfam17061  103 HLTpTPEEHSSGTPEASVPATGSQSPAESPTLTSPQAPASSPSSLSTSPPEVSSAS---VSTNHSSAETSTQPTGAPTTP 179
                           90
                   ....*....|....*....
gi 305855043   402 PS-TVSPASGHTPTPPPHS 419
Cdd:pfam17061  180 ESpTEEHSSGHTPTSHATS 198
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
119-168 1.78e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 37.91  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 305855043  119 RKMQERMstqlAAAESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 168
Cdd:cd14686     4 RRERNRE----AARRSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
372-483 1.88e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.74  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  372 TVPPPSTDRIEENGPSTGSTPDL----TSSPTALPSTVSPASGHTPTPPPHSLhsPCANAPLHPGLNPriQAARFRFQGS 447
Cdd:PRK14959  396 TIPTPGTQGPQGTAPAAGMTPSSaapaTPAPSAAPSPRVPWDDAPPAPPRSGI--PPRPAPRMPEASP--VPGAPDSVAS 471
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 305855043  448 NANDPDQNGNTTQSPPSRDVSPTSRDTLVAKQLARN 483
Cdd:PRK14959  472 ASDAPPTLGDPSDTAEHTPSGPRTWDGFLEFCQGRN 507
PHA03247 PHA03247
large tegument protein UL36; Provisional
335-711 1.89e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  335 PLVSASAKGNAcASAASVRPGIERQV-----SHGDLIGSSLPTVP----PPstdriEENGPST-GSTPDLTSSPTALPST 404
Cdd:PHA03247 2435 PFVSPGGDVLA-GLAADGDPFFARTIlgapfSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDA 2508
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  405 vSPASGHtptPPPHSLHSPCANAPLHPGLNPRIQAARfRFQGSNANDPDQNGNTTQSPPSRDVS-PTSRDTlvakqlARN 483
Cdd:PHA03247 2509 -PPAPSR---LAPAILPDEPVGEPVHPRMLTWIRGLE-ELASDDAGDPPPPLPPAAPPAAPDRSvPPPRPA------PRP 2577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  484 TVTQALSRFTSPPAGAPPRPGAPPTGDVGTYP--------PVGRTSLKTPGGARVDRGNPPPippkkpGLSQTPSPPHPQ 555
Cdd:PHA03247 2578 SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRgpappsplPPDTHAPDPPPPSPSPAANEPD------PHPPPTVPPPER 2651
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  556 LKVIMDSSRASSTGiKADNKTVASSPSSLPQGNR-------VINEENLSKSSSPQLPPKP-------SIDLTVAPAGCAV 621
Cdd:PHA03247 2652 PRDDPAPGRVSRPR-RARRLGRAAQASSPPQRPRrraarptVGSLTSLADPPPPPPTPEPaphalvsATPLPPGPAAARQ 2730
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  622 SALATSQVGAWPAETPGLNQPACSESSLVIPTTTAFRSSI---NPVSASSRR------AGASDSLLVTASGWSPSLTPLL 692
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAppaAPAAGPPRRltrpavASLSESRESLPSPWDPADPPAA 2810
                         410       420
                  ....*....|....*....|....*...
gi 305855043  693 MSG---------GPAPLAGRPTLLQQAA 711
Cdd:PHA03247 2811 VLApaaalppaaSPAGPLPPPTSAQPTA 2838
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
186-267 1.98e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organisation and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 425563 [Multi-domain]  Cd Length: 235  Bit Score: 41.55  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQ-KLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKqlsefdTErEQLRAKLHR-EEAHTTdlKEEIDKMK 263
Cdd:pfam00261   10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELER------TE-ERLAEALEKlEEAEKA--ADESERGR 80

                   ....
gi 305855043   264 KMIE 267
Cdd:pfam00261   81 KVLE 84
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
120-246 2.00e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224300 [Multi-domain]  Cd Length: 119  Bit Score: 39.60  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  120 KMQERMSTQLAAAESRQKKLEMEKLQLQALEQEhkklaarleeergknkhvvlmlVKECKqlsgKVLEEAQKLEE--VMA 197
Cdd:COG1382     3 QLPPEVQAQLAQLQQLQQQLQKVILQKQQLEAQ----------------------LKEIE----KALEELEKLDEdaPVY 56
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  198 KL------EEEKKK-TSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLH 246
Cdd:COG1382    57 KKvgnllvKVSKEEaVDELEERKETLELRIKTLEKQEEKLQERLEELQSEIQKALG 112
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
130-258 2.01e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 425897 [Multi-domain]  Cd Length: 135  Bit Score: 40.00  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   130 AAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKNkhvvlmlvkeckqlsgkvlEEAQKLEEVMAKLEEEKK-KTSA 208
Cdd:pfam00836   24 PSANAPPKLSPTPKKKDSSLEEIQKKLEA--AEERRKS-------------------LEAQKLKQLAEKREKEEEaLQKA 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 305855043   209 LEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEE 258
Cdd:pfam00836   83 LEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEHEKHVEEVRKN 132
PHA02917 PHA02917
ankyrin-like protein; Provisional
786-858 2.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.68  E-value: 2.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305855043  786 VELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAV-DTGNVDSLKLLMYH 858
Cdd:PHA02917  435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCH 508
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
123-271 2.19e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 42.75  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  123 ERMSTQLAAAESRQKKLEM----EKLQL---------QALEQE----------HKKLAARLEEERGKNKHVVL--MLVKE 177
Cdd:COG4477   258 ERLKEQLVENSELLTQLELdeaeEELGLiqekieslyDLLEREveaknvveenLPILPDYLEKAKENNEHLKEeiERVKE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  178 CKQLSGkvlEEAQKLEEVMAKLEEEKKKTSALEEELATEKRRSAEME---AQMEKQLSEFDTEREQLRAKLHREEAHTTD 254
Cdd:COG4477   338 SYRLAE---TELGSVRKFEKELKELESVLDEILENIEAQEVAYSELQdnlEEIEKALTDIEDEQEKVQEHLTSLRKDELE 414
                         170
                  ....*....|....*..
gi 305855043  255 LKEEIDKMKKMIEQLKR 271
Cdd:COG4477   415 ARENLERLKSKLHEIKR 431
HOOK pfam05622
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ...
119-294 2.24e-03

HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas the central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head.


Pssm-ID: 428548 [Multi-domain]  Cd Length: 526  Bit Score: 42.35  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAESRQKKLEME-KLQLQ---ALEQEHKKLAARLEEERGKNKHVVLM---LVKECKQLSgKVLEEAQK 191
Cdd:pfam05622  302 REKLTELQALLEDANRRKNELETQnRLANQrilELQQQVEELQKALQEQGSKAEDSSLLkqkLEEHLEKLH-EAQEELQK 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   192 ----LEEVMAKLEEEKKKTSALEEELateKRRSAEMEAqME-------------------KQLSEFDTEREQLRAKLHRE 248
Cdd:pfam05622  381 kkeqLEELEPKVDSNLQKIDELQEAL---RKKDEDMKA-MEerykkyvekaksviktldpKQNPASPPEIQALRNQLLEK 456
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 305855043   249 EAHTTDLKEEIDKMK---KMIEQLKRGNDSKPSLSLPRKTKDRRLVSIS 294
Cdd:pfam05622  457 DKKIEHLERDYEKSKlqrEQEEKLIVTAWYNLGLALHREAIESRLAGLS 505
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
121-230 2.33e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 40.16  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   121 MQERMSTQLAAAE------------SRQKKLEMEKLQLQALEQEhKKLAARLEEERgknkhvvlmlvkecKQLSGKVLEE 188
Cdd:pfam15236   44 LEERERKRQKALEhqnaikkqleekERQKKLEEERRRQEEQEEE-ERLRREREEEQ--------------KQFEEERRKQ 108
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 305855043   189 AQKlEEVMakleeeKKKTSALEEELAtekrrSAEMEAQMEKQ 230
Cdd:pfam15236  109 KEK-EEAM------TRKTQALLQAMQ-----KAQELAQRLKQ 138
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
40-269 2.51e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 42.45  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    40 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGASDKEKKPVCTNPLSI-LEAVMAhc 118
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLEEETAQKNAALKKLR----ELEAQLSELQEDLESERAARAKAEKQRRDLGEeLEALKT-- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 rKMQERMSTQLAAAESRQKKlEMEKLQLQ-ALEQEHKKLAARLEEERGKNKHVVLMLVKECKQL--SGKVLEEA-QKLEE 194
Cdd:pfam01576  307 -ELEDTLDTTAAQQELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrNKASLEKAkQALES 384
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043   195 VMAKLEEEKKKTSALEEELATEKRRsaemeaqMEKQLSEfdtereqLRAKLHREEAHTTDLKEEIDKMKKMIEQL 269
Cdd:pfam01576  385 ENAELQAELRSLQQAKQDSEHKRKK-------LEGQLQE-------LQSRLSESERQRAELAEKLSKLQSELESV 445
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
129-289 2.58e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 42.38  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  129 LAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkhvvlMLVkeckqLSGKVLEEAqkLEEVMAK-LEEEKKKTS 207
Cdd:COG2433   347 LAAA---YKAYLAYKPKLEKVERKLPELGIWKDVERIK------ALV-----IRGYPLAEA--LSKVKEEeRPREKEGTE 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  208 ALEEELATEKRRsaEMEAQmEKQLSEFDTEREQLRAKLHReeahttdLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKD 287
Cdd:COG2433   411 EEERREITVYEK--RIKKL-EETVERLEEENSELKRELEE-------LKREIEKLESELERFRREVRDKVRKDREIRARD 480

                  ..
gi 305855043  288 RR 289
Cdd:COG2433   481 RR 482
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
184-276 2.62e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.79  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  184 KVLEEAQKleevmaKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEI--DK 261
Cdd:cd16269   191 QALTEKEK------EIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSK 264
                          90
                  ....*....|....*
gi 305855043  262 MKKMIEQLKRGNDSK 276
Cdd:cd16269   265 LKEQEALLEEGFKEQ 279
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
119-226 2.64e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkhvvlmlvKECKQLSGKVLEEAQKLEEVMAK 198
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEWKLEQLAADLSKYEQE 470
                           90       100
                   ....*....|....*....|....*...
gi 305855043   199 LEEEKKKTSALEEELATEKRRSAEMEAQ 226
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQ 498
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
122-270 2.70e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLaaaESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKEckQLSGKvleeAQKLEEVMAKLEE 201
Cdd:TIGR04523  262 QNKIKKQL---SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--ELKNQ----EKKLEEIQNQISQ 332
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305855043   202 EKKKTSALEEELAtekrrsaemeaQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLK 270
Cdd:TIGR04523  333 NNKIISQLNEQIS-----------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
Ank_2 pfam12796
Ankyrin repeats (3 copies);
840-955 2.74e-03

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   840 IHAAVDTGNVDSLKLLMYHGAPAhgnklqeepglaifdldqeehhegtskpvvpadliNHADSEGWTAAHIAASKGFKNC 919
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADA-----------------------------------NLQDKNGRTALHLAAKNGHLEI 45
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 305855043   920 LEVLCRHGGLepeRRDKCNRTAHDVAT-----DDCKHLLEN 955
Cdd:pfam12796   46 VKLLLEHADV---NLKDNGRTALHYAArsghlEIVKLLLEK 83
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
119-271 2.89e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 434789 [Multi-domain]  Cd Length: 374  Bit Score: 41.95  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAESR-------QKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK----HVVLMLVKECKQLSGK 184
Cdd:pfam15558   79 RRRRDRREKQVIEKESRwreqaedQENQRQEKLERAAQEAEQRKQcqEQNLkEKEEELQAlreqNGLQLQERLEQACHKR 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   185 VLEEAQKLEEVMAKLEEEKKKTSALEEELatEKRRSAEME---AQMEKQLSEFDTEREQLRAKLHREeahttdLKEEIDK 261
Cdd:pfam15558  159 QLKELEEQKKVQENNLSELLNHQARKVLV--DCQAKAEELlrrLSLEQSLQRSQENYEQLVEERHRE------LREKAQK 230
                          170
                   ....*....|
gi 305855043   262 MKKMIEQLKR 271
Cdd:pfam15558  231 EEEQFQRAKL 240
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
140-294 3.02e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  140 EMEKLQLQALEQEHKKLAARLEEErGknkhvvLMLVKECKQLS-----GKVLEEAQKLEEVMAKLEEEKKKTSALEEELA 214
Cdd:PRK05771    5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  215 TEKRRSAEmEAQmEKQLSEFDTEREQLRAKLHREeahtTDLKEEIDKMKKMIEQLK--RGNDSKPSLSLPRKTKDRRLVS 292
Cdd:PRK05771   78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151

                  ..
gi 305855043  293 IS 294
Cdd:PRK05771  152 VP 153
PHA02859 PHA02859
ankyrin repeat protein; Provisional
786-859 3.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  786 VELLIAYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNV--DSLKLLMYHG 859
Cdd:PHA02859   69 LKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSG 148
PRK00106 PRK00106
ribonuclease Y;
112-266 3.39e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 41.78  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  112 EAVMAHCRKMQERMSTQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkhvVLMLVKECKQLSGK 184
Cdd:PRK00106   52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  185 --VLEEA-QKLEEVMAKLEEEKKKTSALEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDK 261
Cdd:PRK00106  124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203

                  ....*
gi 305855043  262 MKKMI 266
Cdd:PRK00106  204 MAKDL 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
725-826 3.46e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  725 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFKCVELLI-------AYDANIN 797
Cdd:PHA03095  245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALaknpsaeTVAATLN 324
                          90       100       110
                  ....*....|....*....|....*....|
gi 305855043  798 HAADGGQTPLYlackNGNKEC-IKLLLEAG 826
Cdd:PHA03095  325 TASVAGGDIPS----DATRLCvAKVVLRGA 350
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
150-271 3.72e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  150 EQEHKKLAARLEEERGKNKHvvlmlvKECKQLSGKVLEEAQKLEEVMAK--LEEEKKKTSALEEELATEKRRSAEMEAQM 227
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQ------QQAEELQQKQAAEQERLKQLEKErlAAQEQKKQAEEAAKQAALKQKQAEEAAAK 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 305855043  228 EKQLSEFDTEREQLR----AKLHREEAhttDLKEEIDKMKKMIEQLKR 271
Cdd:PRK09510  141 AAAAAKAKAEAEAKRaaaaAKKAAAEA---KKKAEAEAAKKAAAEAKK 185
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
122-248 3.85e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 40.69  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLAAAESRQKKLEMEKlQLQALEQE---HKKLAARLEEERGKNKHVVLMLVKEckQLSGKVLEEAQKLEEVMAK 198
Cdd:pfam00769   78 KEQLERELREAQEEVARLEEES-ERKEEEAErlqEELEEAREEEEEAKEKLLAASTSPS--HHHSEESENEDDEEEEESY 154
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043   199 LEEEKKKTSALEEELA---TEKRRSAEMEA--QMEKQLSEFDTEREQLRA--------KLHRE 248
Cdd:pfam00769  155 EGGSAELSNDGDMDQLsdrIEEERVTEAEKneRLQKQLKALKSELAQARDetkqtqndILHEE 217
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
88-270 3.92e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 41.64  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043    88 QRDYEAGASDKEKKPVCTNPLSILEAVMahcRKMQERMSTQLAAAE----------SRQKKLEMEKLQLQALEQEHKKLA 157
Cdd:pfam05557   62 KREAEAEEALREQAELNRLKKKNLEALN---KKLNEKESQLADAREvisclknelsELRRQIQRQELELSSTNSELEELQ 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   158 ARLEEERGK-NKHVVLMLVKECKQLSGKVLEEA-QKLEEVMAKLEEEKKKTSALEEELAtekrRSAEMEAQMEKQLSE-- 233
Cdd:pfam05557  139 ERLDLQKAKaQEAEQLRQNLEAQQSSLAEAEQRiKELEFEIQSQEQDSEIVKNSKSELA----RIPELERELERLREHnk 214
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 305855043   234 -----------FDTEREQLRAKLHREEahttDLKEEIDKMK----KMIEQLK 270
Cdd:pfam05557  215 hlnenienkllLKEEVEDLKRKLEREE----GYREELATLElekeKLEQELK 262
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
122-273 4.11e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.73  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKEcKQLSGKVLEEAQKLEEVMakleE 201
Cdd:pfam10174   95 QDFTTSPVDGEDKFSTP-ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQ-KQTLGARDESIKKLLEML----Q 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   202 EKKKTSALEEELATEKRRSAEMEAQ---MEKQLSEFDTEREQLRAKLHR------EEAHTTDLKEEIDKMKKMIEQLKRG 272
Cdd:pfam10174  169 SKGLPKKSGEEDWERTRRIAEAEMQlghLEVLLDQKEKENIHLREELHRrnqlqpDPAKTKALQTVIEMKDTKISSLERN 248

                   .
gi 305855043   273 N 273
Cdd:pfam10174  249 I 249
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
174-264 4.28e-03

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 39.09  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   174 LVKECKQLSGKVLEEAQKLEEvMAKLEEEKKKTSALEEELATEKRRSAEMEAQMekQLSEFDTEREQLRAKLHREEAhtt 253
Cdd:pfam05103   37 LIRENAELKEKIEELEEKLAH-YKNLEETLQNTLILAQETAEEVKANAQKEAEL--IIKEAEAKAERIVDDANNEVK--- 110
                           90
                   ....*....|.
gi 305855043   254 DLKEEIDKMKK 264
Cdd:pfam05103  111 KINDEIEELKR 121
PHA03247 PHA03247
large tegument protein UL36; Provisional
327-713 4.46e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  327 PVKPAAGSplvsASAKGNACASAASVR-PGIERqvshGDLIGSSLPTVPPPSTDRIEENGPSTGSTPDLTSSPTALPSTV 405
Cdd:PHA03247 2577 PSEPAVTS----RARRPDAPPQSARPRaPVDDR----GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP 2648
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  406 SPASGHTPTPPPHSLH--------SPCANAPLHpglNPRIQAARFRFqGSNAN--DPDQNGNTTQSPPSRDVSPTSRDTL 475
Cdd:PHA03247 2649 PERPRDDPAPGRVSRPrrarrlgrAAQASSPPQ---RPRRRAARPTV-GSLTSlaDPPPPPPTPEPAPHALVSATPLPPG 2724
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  476 VAKQLARNTVTQAlsrftsppAGAPPRPGAPPTGDVGTYPPVGRTSLKTPGGARVDRGnpppippkkpglsqTPSPPHPQ 555
Cdd:PHA03247 2725 PAAARQASPALPA--------APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA--------------PAAGPPRR 2782
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  556 LKVIMDSSRASSTGIKADNKTVASSPSSLPQGNRVineENLSKSSSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAE 635
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA---LPPAASPAGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAP 2858
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305855043  636 TPGLNQPACSESSLVIPTTtafrSSINPVSASSRRAgasdsllVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 713
Cdd:PHA03247 2859 GGDVRRRPPSRSPAAKPAA----PARPPVRRLARPA-------VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
184-271 5.17e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 427600 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 5.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   184 KVLEEAQKLEEVMAKLEEEKKKtsaleeelatekrrsaeMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMK 263
Cdd:pfam03938    9 KILEESPEGKAAQAQLEKKFKK-----------------RQKELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71

                   ....*...
gi 305855043   264 KMIEQLKR 271
Cdd:pfam03938   72 QELQQLQQ 79
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
137-278 5.38e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 40.03  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  137 KKLEMEKLQLQALEQEHKKLAARLEEergknkhvvlmLVKECKQLsGKVLEE-AQKLEEvMAKLEEEKKKT--SALEEEL 213
Cdd:cd07596     4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElgEALSKLG 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305855043  214 ATEKRRSAEMEAQMEKQLSEF-DTEREQLR----AKL---HREEA--HTTDLKEEIDKMKKMIEQLKRGNDSKPS 278
Cdd:cd07596    71 KAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
129-271 5.45e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 41.16  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  129 LAAAESRQKKLEMEKLQLQALEQEhkKLAARLEEERGKNKhvvLMLVKECKQLsgkVLEEAQKLEEVMAKLEEEKKKTSA 208
Cdd:COG4372    73 VFQLDDIRPQLRALRTELGTAQGE--KRAAETEREAARSE---LQKARQEREA---VRQELAAARQNLAKAQQELARLTK 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043  209 LEEELATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:COG4372   145 QAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLAT 207
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
835-860 5.46e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 5.46e-03
                           10        20
                   ....*....|....*....|....*..
gi 305855043   835 DGWTPIHAAVD-TGNVDSLKLLMYHGA 860
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGA 27
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
119-274 6.30e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 40.31  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   119 RKMQERMSTQLAAAESRQKK----LEMEKLQLQAleqehkkLAARLEEERGKNKhvvlmlvKECKQLSGKVLEEAQKLEE 194
Cdd:pfam00769   57 AQEAEEEKERLEESAEMEAEekeqLERELREAQE-------EVARLEEESERKE-------EEAERLQEELEEAREEEEE 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQmEKQLSEFDTEREQLRAKLHREEAHTT-------------DLKEEIDK 261
Cdd:pfam00769  123 AKEKLLAASTSPSHHHSEESENEDDEEEEESY-EGGSAELSNDGDMDQLSDRIEEERVTeaeknerlqkqlkALKSELAQ 201
                          170       180
                   ....*....|....*....|...
gi 305855043   262 MK---KM-------IEQLKRGND 274
Cdd:pfam00769  202 ARdetKQtqndilhEENVRAGRD 224
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
111-338 6.60e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 40.86  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  111 LEAVMAHCRKMQERMSTQLAAAESRQKKLE-----MEKlQLQALEQEHKKLAARLEE------ERGKNKHVVLMLVKE-- 177
Cdd:COG4942    64 LEKQLKSLETEIASLEAQLIETADDLKKLRkqiadLNA-RLNALEVQEREQRRRLAEqlaalqRSGRNPPPALLVSPEda 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  178 -----CKQLSGKV----LEEAQKLEEVMAKLEEEKKKTSA-------LEEELATEKRRSA-------EMEAQMEKQLSEF 234
Cdd:COG4942   143 qrsvrLAIYYGALnparAERIDALKATLKQLAAVRAEIAAeqaelttLLSEQRAQQAKLAqlleerkKTLAQLNSELSAD 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  235 DTEREQLRAKlhreeahTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKTKDRRLVSISVATEGPMTRSVACQTDLvte 314
Cdd:COG4942   223 QKKLEELRAN-------ESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKPTAPEKMLISSTGGF--- 292
                         250       260
                  ....*....|....*....|....
gi 305855043  315 tAEPLKKLPltvpvKPAAGSPLVS 338
Cdd:COG4942   293 -GALRGQLA-----WPVTGRILRR 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
771-968 7.97e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  771 FTPLCAAAAQGHFKCVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKtrDGWTPIHAAVDTGNVD 850
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF--YTLVAIKDAFNNRNVE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043  851 SLKLLMYhgapahgNKLQEEPGLAIFDLDQEEHHEGTSKPVVPADLINHAD------SEGWTAAHIAASKGFKNCLEVLC 924
Cdd:PHA02878  116 IFKIILT-------NRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADinmkdrHKGNTALHYATENKDQRLTELLL 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043  925 RHGGlEPERRDKCNRTAHDVAT-----DDCKHLLENLNALKI-------PLRISVG 968
Cdd:PHA02878  189 SYGA-NVNIPDKTNNSPLHHAVkhynkPIVHILLENGASTDArdkcgntPLHISVG 243
DUF4355 pfam14265
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ...
195-270 8.85e-03

Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.


Pssm-ID: 405026 [Multi-domain]  Cd Length: 119  Bit Score: 37.67  E-value: 8.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305855043   195 VMAKLEEEKKKTSALEEELATEKRRSAEMEAQmEKQlsefDTEREQLRAKLHREEAHTTdLKEEIDKMKKMIEQLK 270
Cdd:pfam14265    8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
117-272 8.90e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 40.91  E-value: 8.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   117 HCRKMQERMSTQLAA--AESRQKKLEM-EKLQLQALEQEHkkLAARLEEERGKNkhvvLMLVKECKQLSGKvLEEAQKL- 192
Cdd:pfam01576  405 HKRKKLEGQLQELQSrlSESERQRAELaEKLSKLQSELES--VSSLLNEAEGKN----IKLSKDVSSLESQ-LQDTQELl 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   193 -EEVMAKLEeekkktsaleeeLATEKRRSAEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKR 271
Cdd:pfam01576  478 qEETRQKLN------------LSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEE 545

                   .
gi 305855043   272 G 272
Cdd:pfam01576  546 G 546
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
186-270 9.57e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 431934 [Multi-domain]  Cd Length: 151  Bit Score: 38.45  E-value: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   186 LEEAQKLEEVMAKLEEEK----KKTSALEEELAtekrrsaemEAQMEKQLSEFDtEReQLRAKLHREEAHTTDLKEEIDK 261
Cdd:pfam11559   51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLE---------DLERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119

                   ....*....
gi 305855043   262 MKKMIEQLK 270
Cdd:pfam11559  120 LKNALQQIK 128
PHA02795 PHA02795
ankyrin-like protein; Provisional
787-849 9.60e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157  Cd Length: 437  Bit Score: 40.36  E-value: 9.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305855043  787 ELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPIHAAVDTGNV 849
Cdd:PHA02795  205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
122-226 9.87e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 429739 [Multi-domain]  Cd Length: 127  Bit Score: 37.99  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305855043   122 QERMSTQLAAAESRQKKLeMEKLQLQAL---------EQE---HKKLAARLEEERGKNKHVVLMLVKECKQLsgkvlEEA 189
Cdd:pfam07926    8 IKRLKEEAADAEAQLQKL-QEDLEKQAEiareaqqnyERElvlHAEDIKALQALREELNELKAEIAELKAEA-----ESA 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 305855043   190 Q-KLEEVMAKLEEEKKktsALEEELATEKRRSAEMEAQ 226
Cdd:pfam07926   82 KaELEESEESWEEQKK---RLEKELSELEKRIEDLNEQ 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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