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Conserved domains on  [gi|2462616488|ref|XP_054215162|]
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cortactin-binding protein 2 isoform X1 [Homo sapiens]

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 ...
 18-162 2.02e-49

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: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 173.94  E-value: 2.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   18 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 92
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 136
Cdd:pfam09727   82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161

                          170       180
                   ....*....|....*....|....*.
gi 2462616488  137 KLAARLEEERGKNKQVVLMLVKECKQ 162
Cdd:pfam09727  162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
680-952 3.49e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 3.49e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  680 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 759
Cdd:COG0666     41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  760 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 839
Cdd:COG0666    121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  840 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGG 919
Cdd:COG0666    201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462616488  920 LEPERRDKCNRTVHDVATDDCKHLLENLNALKI 952
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 105-246 1.39e-12

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 69.18  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 174
Cdd:COG1579     34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 246
Cdd:COG1579    113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 333-700 1.25e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.80  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  333 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 407
Cdd:PHA03247  2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  408 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 485
Cdd:PHA03247  2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  486 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 561
Cdd:PHA03247  2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  562 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 630
Cdd:PHA03247  2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  631 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 689
Cdd:PHA03247  2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827

                          410
                   ....*....|.
gi 2462616488  690 AGRPTLLQQAA 700
Cdd:PHA03247  2828 LPPPTSAQPTA 2838
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 18-162 2.02e-49

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: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 173.94  E-value: 2.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   18 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 92
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 136
Cdd:pfam09727   82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161

                          170       180
                   ....*....|....*....|....*.
gi 2462616488  137 KLAARLEEERGKNKQVVLMLVKECKQ 162
Cdd:pfam09727  162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
680-952 3.49e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 3.49e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  680 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 759
Cdd:COG0666     41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  760 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 839
Cdd:COG0666    121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  840 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGG 919
Cdd:COG0666    201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462616488  920 LEPERRDKCNRTVHDVATDDCKHLLENLNALKI 952
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
730-817 1.27e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.42  E-value: 1.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  730 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 809
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2462616488  810 LLLEAGTN 817
Cdd:pfam12796   79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 703-849 9.83e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 9.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  703 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 780
Cdd:PHA03100   119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  781 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 849
Cdd:PHA03100   181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-253 1.35e-12

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: 73.18  E-value: 1.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   19 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAGAGDKEKkpvctnplsiLE 94
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIAS----------LE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   95 AVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNRE 230
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKY 467

                          250       260
                   ....*....|....*....|...
gi 2462616488  231 EAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQR 490
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 105-246 1.39e-12

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 69.18  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 174
Cdd:COG1579     34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 246
Cdd:COG1579    113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-253 3.69e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 71.63  E-value: 3.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  189 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168  347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 101-253 5.81e-12

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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 69.18  E-value: 5.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 176
Cdd:pfam13868   80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  177 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:pfam13868  155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233


                   ...
gi 2462616488  251 LKR 253
Cdd:pfam13868  234 RQE 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-253 2.25e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCK 101
Cdd:COG1196    257 ELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  102 KMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 177
Cdd:COG1196    309 ERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAKL---EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:COG1196    389 LEALraaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                   ..
gi 2462616488  252 KR 253
Cdd:COG1196    469 LE 470
PTZ00121 PTZ00121
MAEBL; Provisional
 101-271 3.61e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 3.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 180
Cdd:PTZ00121  1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  181 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 253
Cdd:PTZ00121  1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465

                          170
                   ....*....|....*...
gi 2462616488  254 GSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAK 1483
PHA03247 PHA03247
large tegument protein UL36; Provisional
 333-700 1.25e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.80  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  333 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 407
Cdd:PHA03247  2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  408 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 485
Cdd:PHA03247  2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  486 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 561
Cdd:PHA03247  2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  562 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 630
Cdd:PHA03247  2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  631 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 689
Cdd:PHA03247  2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827

                          410
                   ....*....|.
gi 2462616488  690 AGRPTLLQQAA 700
Cdd:PHA03247  2828 LPPPTSAQPTA 2838
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
9-253 1.78e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    9 KKKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvct 87
Cdd:PRK03918   198 KEKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK----- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   88 nplsiLEAVMAHCKKMQERMSAQLAAAESRQKklEMEKLQLQALEQEhkklaaRLEEERGKNKQVVLMLVKECKQLSgkv 167
Cdd:PRK03918   257 -----LEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYI------KLSEFYEEYLDELREIEKRLSRLE--- 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 iEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMRK 246
Cdd:PRK03918   321 -EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLEK 391


                   ....*..
gi 2462616488  247 MIEQLKR 253
Cdd:PRK03918   392 ELEELEK 398
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 349-718 1.35e-08

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 characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 59.78  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  349 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 428
Cdd:pfam03154  179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  429 AARFRFQGnandpdqngnTTQSPPSRDVSPTSrdnlvAKQLARNTVTQALSRftSPQAGAPSRP--------GVPPTGDV 500
Cdd:pfam03154  244 SPHPPLQP----------MTQPPPPSQVSPQP-----LPQPSLHGQMPPMPH--SLQTGPSHMQhpvppqpfPLTPQSSQ 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  501 GTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVAST 569
Cdd:pfam03154  307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQM 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  570 PSSLPQGNRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS 648
Cdd:pfam03154  387 NSNLPPPPALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQ 455

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  649 --SINPVSASSCRPGASDSLLvTASGWSPSLTPlLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 718
Cdd:pfam03154  456 vpSQSPFPQHPFVPGGPPPIT-PPSGPPTSTSS-AMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 694-830 1.52e-06

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: 53.09  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 768
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  769 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 830
Cdd:cd22192     99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 696-833 1.25e-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: 50.08  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  696 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 762
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  763 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 826
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209


                   ....*..
gi 2462616488  827 TPVHAAV 833
Cdd:TIGR00870  210 TLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 792-817 2.08e-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: 42.57  E-value: 2.08e-05
                            10        20
                    ....*....|....*....|....*.
gi 2462616488   792 GQTPLYLACKNGNKECIKLLLEAGTN 817
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 111-258 6.41e-05

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: 45.90  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  111 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 177
Cdd:cd00176     32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 243
Cdd:cd00176    112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190

                          170
                   ....*....|....*
gi 2462616488  244 MRKMIEQLKRGSDSK 258
Cdd:cd00176    191 LNERWEELLELAEER 205
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 149-250 8.09e-05

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: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 8.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   149 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 224
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82

                            90       100
                    ....*....|....*....|....*.
gi 2462616488   225 AKLNREEAhttdlkEEIDKMRKMIEQ 250
Cdd:smart00935   83 QDLQKRQQ------EELQKILDKINK 102
growth_prot_Scy NF041483
polarized growth protein Scy;
94-252 4.28e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.20  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   94 EAVMAHCKkmqERMSAQLAAAES------RQKKLEMEKL------QLQALEQEHKKLA--ARLEEERgknkqvvlmLVKE 159
Cdd:NF041483   282 EKVVAEAK---EAAAKQLASAESaneqrtRTAKEEIARLvgeatkEAEALKAEAEQALadARAEAEK---------LVAE 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  160 CKQLSGKVIEE---------AQKLEDVMAKLEEEKKKTNELEEElSAEKRRsTEMEAQMEKQLSEFDTEREQLR--AKLN 228
Cdd:NF041483   350 AAEKARTVAAEdtaaqlakaARTAEEVLTKASEDAKATTRAAAE-EAERIR-REAEAEADRLRGEAADQAEQLKgaAKDD 427

                          170       180
                   ....*....|....*....|....*.
gi 2462616488  229 REE--AHTTDLKEEIDKMRKMIEQLK 252
Cdd:NF041483   428 TKEyrAKTVELQEEARRLRGEAEQLR 453
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 101-150 2.00e-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: 2.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  101 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 150
Cdd:cd14686      4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 18-162 2.02e-49

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: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 173.94  E-value: 2.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   18 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 92
Cdd:pfam09727    2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 136
Cdd:pfam09727   82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161

                          170       180
                   ....*....|....*....|....*.
gi 2462616488  137 KLAARLEEERGKNKQVVLMLVKECKQ 162
Cdd:pfam09727  162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
680-952 3.49e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 3.49e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  680 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 759
Cdd:COG0666     41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  760 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 839
Cdd:COG0666    121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  840 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGG 919
Cdd:COG0666    201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462616488  920 LEPERRDKCNRTVHDVATDDCKHLLENLNALKI 952
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
694-936 1.49e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 773
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  774 CVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHG 853
Cdd:COG0666    102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  854 nsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVH 933
Cdd:COG0666    177 -------------------------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTAL 223


                   ...
gi 2462616488  934 DVA 936
Cdd:COG0666    224 DLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
730-817 1.27e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.42  E-value: 1.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  730 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 809
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2462616488  810 LLLEAGTN 817
Cdd:pfam12796   79 LLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
707-946 6.53e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.80  E-value: 6.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  707 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANIN 786
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  787 HAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHGnsfneeesessvf 866
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  867 dldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVHDVA-----TDDCK 941
Cdd:COG0666    144 ------------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVK 203


                   ....*
gi 2462616488  942 HLLEN 946
Cdd:COG0666    204 LLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
696-786 1.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  696 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSaEAQVNAADkNGFTPLCAAAAQGHFECV 775
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|.
gi 2462616488  776 ELLISYDANIN 786
Cdd:pfam12796   78 KLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
763-849 1.11e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 1.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  763 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSvkTTDGWTPVHAAVDTGNVDSLK 842
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 2462616488  843 LLMYHRI 849
Cdd:pfam12796   79 LLLEKGA 85
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 703-849 9.83e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 9.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  703 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 780
Cdd:PHA03100   119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  781 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 849
Cdd:PHA03100   181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 714-833 1.38e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.16  E-value: 1.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  714 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ 793
Cdd:PHA02874   112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462616488  794 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 833
Cdd:PHA02874   192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 694-848 5.87e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 5.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 773
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  774 CVELLISYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTNRSVKTTD--GWTPVHAAVDTG-NVDSLKLLMYHR 848
Cdd:PHA02874   205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHK 278
PHA03095 PHA03095
ankyrin-like protein; Provisional
 695-844 6.74e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 6.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  695 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLSAEAQVNAADKNGFTPL-CAAAAQ 769
Cdd:PHA03095    15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  770 GHFECVELLISYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD--SLKLL 844
Cdd:PHA03095    95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 699-848 1.97e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 1.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  699 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 778
Cdd:PHA02875     9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  779 ISYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 848
Cdd:PHA02875    88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 711-845 7.01e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.07  E-value: 7.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  711 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAA 789
Cdd:PHA02878   152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  790 DGGQTPLYLA---CKngNKECIKLLLEAGTNRSVKTT-DGWTPVHAAVDTGnvDSLKLLM 845
Cdd:PHA02878   232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLL 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
796-926 7.05e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 7.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  796 LYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHripahgnsfneeesessvfdldggeesp 875
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  876 egiskpvVPADLINHanreGWTAAHIAASKGFKNCLEILCRHgGLEPERRD 926
Cdd:pfam12796   53 -------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 699-845 4.63e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.52  E-value: 4.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  699 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 778
Cdd:PLN03192   532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  779 ISYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLM 845
Cdd:PLN03192   611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-253 1.35e-12

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: 73.18  E-value: 1.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   19 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAGAGDKEKkpvctnplsiLE 94
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIAS----------LE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   95 AVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNRE 230
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKY 467

                          250       260
                   ....*....|....*....|...
gi 2462616488  231 EAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQR 490
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 704-847 1.38e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.22  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  704 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLSAEAQVNAADKN-GFTPLCAAAAQGHFECVEL 777
Cdd:PHA02878   113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  778 LISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDT-GNVDSLKLLMYH 847
Cdd:PHA02878   187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 105-246 1.39e-12

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 69.18  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 174
Cdd:COG1579     34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 246
Cdd:COG1579    113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
726-779 1.44e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 1.44e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  726 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLI 779
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 694-847 3.18e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 3.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LSAEA 750
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  751 QVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 830
Cdd:PHA02874   116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          170
                   ....*....|....*..
gi 2462616488  831 AAVDTGNVDSLKLLMYH 847
Cdd:PHA02874   196 NAAEYGDYACIKLLIDH 212
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-253 3.69e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 71.63  E-value: 3.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  189 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168  347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-254 4.03e-12

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: 71.64  E-value: 4.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    6 GFLKKKEFDVDTLS-KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGAGDKE 81
Cdd:TIGR02169  658 GSRAPRGGILFSRSePAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   82 KKPvctnplSILEAVMAHCKKMQErmsaQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERGKNKQVVLMLV 157
Cdd:TIGR02169  734 KLK------ERLEELEEDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKL 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  158 KE-CKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTEREQLRAKLNREEAH 233
Cdd:TIGR02169  804 EEeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESR 883

                          250       260
                   ....*....|....*....|.
gi 2462616488  234 TTDLKEEIDKMRKMIEQLKRG 254
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERK 904
Ank_4 pfam13637
Ankyrin repeats (many copies);
761-812 4.09e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 4.09e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  761 TPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 812
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
105-279 5.15e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.57  E-value: 5.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 179
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  180 KLEEEKKKTNELEEELSAEKRRSTEMEAQM-------EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:COG4717    154 RLEELRELEEELEELEAELAELQEELEELLeqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233

                          170       180
                   ....*....|....*....|....*..
gi 2462616488  253 rgsDSKPSLSLPRKTKDRRLVSISVGT 279
Cdd:COG4717    234 ---NELEAAALEERLKEARLLLLIAAA 257
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 101-253 5.81e-12

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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 69.18  E-value: 5.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 176
Cdd:pfam13868   80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  177 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:pfam13868  155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233


                   ...
gi 2462616488  251 LKR 253
Cdd:pfam13868  234 RQE 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-304 1.75e-11

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: 69.32  E-value: 1.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   97 MAHCKKMQERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAhtTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEAANLRERLESLER 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  254 GSDSKpslslprKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKL 304
Cdd:TIGR02168  832 RIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-253 2.25e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCK 101
Cdd:COG1196    257 ELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  102 KMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 177
Cdd:COG1196    309 ERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAKL---EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:COG1196    389 LEALraaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                   ..
gi 2462616488  252 KR 253
Cdd:COG1196    469 LE 470
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 680-845 3.46e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 3.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  680 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLSAEAQVNA 754
Cdd:PHA02875    53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  755 ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDG-WTPVHAAV 833
Cdd:PHA02875   131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210

                          170
                   ....*....|..
gi 2462616488  834 DTGNVDSLKLLM 845
Cdd:PHA02875   211 ENNKIDIVRLFI 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
694-796 3.49e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 3.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 773
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                           90       100
                   ....*....|....*....|...
gi 2462616488  774 CVELLISYDANINHAADGGQTPL 796
Cdd:COG0666    267 IVKLLLLALLLLAAALLDLLTLL 289
PTZ00121 PTZ00121
MAEBL; Provisional
 101-271 3.61e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 3.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 180
Cdd:PTZ00121  1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  181 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 253
Cdd:PTZ00121  1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465

                          170
                   ....*....|....*...
gi 2462616488  254 GSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAK 1483
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 92-253 1.05e-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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 65.33  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   92 ILEAVMAHCKKMQ------ERMSAQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLE---EERGKNKQVVLMLVKECKQ 162
Cdd:pfam13868   23 ERDAQIAEKKRIKaeekeeERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEeqiEEREQKRQEEYEEKLQERE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  163 LSGKVIEEAQkLEDVMAKLEEEKKKTNELEE--ELSAEKRRSTEMEAQMEK----QLSEFDTEREQLRAKLNREEAHTTD 236
Cdd:pfam13868  102 QMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEEReedeRILEYLKEKAEREEEREAEREEIEE 180

                          170
                   ....*....|....*...
gi 2462616488  237 LKE-EIDKMRKMIEQLKR 253
Cdd:pfam13868  181 EKErEIARLRAQQEKAQD 198
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 118-253 1.22e-10

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 60.29  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEMEKLQLQALEQEHKKLAARLEeergknkqVVLMLVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 197
Cdd:pfam18595    1 SSTLAEEKEELAELERKARELQAKID--------ALQVVEKDLR----SCIKLLEEIEAELAKLEEAKKKLKELRDALEE 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  198 EKRRSTEMEA---QMEKQLsefdterEQLRAKLNREEAHTtdlKEEIDKMRKMIEQLKR 253
Cdd:pfam18595   69 KEIELRELERreeRLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 90-259 1.65e-10

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 64.79  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQA-LEQEHKKLAARLEE--ERGKNKQVVLML---------- 156
Cdd:COG4942     57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRAlyRLGRQPPLALLLspedfldavr 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  157 --------VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 228
Cdd:COG4942    137 rlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462616488  229 REEAHTTDLKEEIDKMRKMIEQLKRGSDSKP 259
Cdd:COG4942    217 ELQQEAEELEALIARLEAEAAAAAERTPAAG 247
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 712-847 1.67e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  712 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGH-----FECVELLISYDANIN 786
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  787 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDS--LKLLMYH 847
Cdd:PHA03100   101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 120-313 1.91e-10

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: 65.90  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  120 KLEMEKLQLQALEQEHKKlaarleEERGKNKQVVLMLVKeckqlsgkVIEEAQKLEDVMAKLEEEKKKTNELEEElsaEK 199
Cdd:pfam05483  216 KLKEDHEKIQHLEEEYKK------EINDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK---TK 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  200 RRSTEMEAQMEKQlSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGT 279
Cdd:pfam05483  279 LQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462616488  280 EGTVTRSVACQTDLVTENADHMKKLPLTMPVKPS 313
Cdd:pfam05483  358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-252 2.14e-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: 65.86  E-value: 2.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    1 MDGSPGFLKKKEFDVDTLSKsELRMLLSVMEGELEARDLVIEAL-RARRKEVFIQErygrfNLNDPFLALQRDYEAgagD 79
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLeQEEEKLKERLE-----ELEEDLSSLEQEIEN---V 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   80 KEKkpvctnplsiLEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQ-----LQALEQEHKKLAARLEEERGKNKQVVL 154
Cdd:TIGR02169  757 KSE----------LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  155 ---MLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELsAEKRRStemEAQMEKQLSEFDTEREQLRAKLNREE 231
Cdd:TIGR02169  827 ekeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-EELEAA---LRDLESRLGDLKKERDELEAQLRELE 902

                          250       260
                   ....*....|....*....|.
gi 2462616488  232 AHTTDLKEEIDKMRKMIEQLK 252
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELK 923
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
119-258 2.20e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 64.54  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  119 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 198
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  199 KR---RSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 258
Cdd:COG4372     86 NEqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 12-253 5.62e-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: 64.70  E-value: 5.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   12 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGAGDKEKKpvct 87
Cdd:TIGR02169  167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKE---- 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   88 nplsILEavmahckKMQERMSAQLAAAESRQKKLEMEKLQL--------QALEQEHKKLAARLEEERGKNKQVVLMLVKE 159
Cdd:TIGR02169  234 ----ALE-------RQKEAIERQLASLEEELEKLTEEISELekrleeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAE 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  160 CKQLSGKVIEEAQKLEDV---MAKLEEEKKKT----NELEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:TIGR02169  303 IASLERSIAEKERELEDAeerLAKLEAEIDKLlaeiEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDK 378

                          250       260
                   ....*....|....*....|.
gi 2462616488  233 HTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKR 399
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 92-250 9.68e-10

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 62.99  E-value: 9.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   92 ILEAVMAHCkkMQER---MSAQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKQVVLMLVKECKQLSG 165
Cdd:pfam07888   31 LLQNRLEEC--LQERaelLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  166 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK----------QLSEFDTEREQLRAKLNREEAHTT 235
Cdd:pfam07888  109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELR 188

                          170
                   ....*....|....*
gi 2462616488  236 DLKEEIDKMRKMIEQ 250
Cdd:pfam07888  189 SLSKEFQELRNSLAQ 203
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
129-254 9.75e-10

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 63.34  E-value: 9.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  129 QALE-QEHKKLAARLEEERGKNKQVVLML---VKECKQLSGKViEEAQKL-EDVMAKLEEEKKKTNELEEELSaEKRRST 203
Cdd:COG2433    380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQV-ERLEAEvEELEAELEEKDERIERLERELS-EARSEE 457

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  204 EMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:COG2433    458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-256 9.92e-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: 63.54  E-value: 9.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEA-----RDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAgdkekkpvctnpLSILEAV 96
Cdd:TIGR02168  695 ELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   97 MAHCKKMQERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSGKVIEEAQ 172
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 KLEDvmakLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:TIGR02168  839 RLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914


                   ....
gi 2462616488  253 RGSD 256
Cdd:TIGR02168  915 RELE 918
Ank_2 pfam12796
Ankyrin repeats (3 copies);
694-756 1.03e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 1.03e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAD 756
Cdd:pfam12796   32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
 333-700 1.25e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.80  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  333 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 407
Cdd:PHA03247  2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  408 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 485
Cdd:PHA03247  2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  486 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 561
Cdd:PHA03247  2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  562 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 630
Cdd:PHA03247  2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  631 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 689
Cdd:PHA03247  2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827

                          410
                   ....*....|.
gi 2462616488  690 AGRPTLLQQAA 700
Cdd:PHA03247  2828 LPPPTSAQPTA 2838
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 20-249 1.36e-09

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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 63.27  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   20 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGAGDKEKkpvctnplsiLEAVM-- 97
Cdd:pfam01576   70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKLQ----------LEKVTte 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   98 AHCKKMQER--MSAQLAAAESRQKKL--------------EMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEC 160
Cdd:pfam01576  131 AKIKKLEEDilLLEDQNSKLSKERKLleeriseftsnlaeEEEKAKsLSKLKNKHEAMISDLEERLKKEEKGRQELEKAK 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  161 KQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQ----------MEKQLSEFDTEREQLRAKLNRE 230
Cdd:pfam01576  211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKA 290

                          250
                   ....*....|....*....
gi 2462616488  231 EAHTTDLKEEIDKMRKMIE 249
Cdd:pfam01576  291 EKQRRDLGEELEALKTELE 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 93-253 1.46e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESR--QKKLEMEKLQ-----LQALEQEHKKLAARLE-------EERGKNKQVVLMLVK 158
Cdd:COG1196    244 LEAELEELEAELEELEAELAELEAEleELRLELEELEleleeAQAEEYELLAELARLEqdiarleERRRELEERLEELEE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  159 ECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLK 238
Cdd:COG1196    324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                          170
                   ....*....|....*
gi 2462616488  239 EEIDKMRKMIEQLKR 253
Cdd:COG1196    404 ELEEAEEALLERLER 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-253 1.55e-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: 63.15  E-value: 1.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   33 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHCKKMQERMSAQLA 112
Cdd:TIGR02168  221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  113 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEaqKLEDVMAKLEEEKKKTNELE 192
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEE--KLEELKEELESLEAELEELE 364

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  193 EELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLK 428
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 22-253 1.72e-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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 61.47  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGAGDKEKKpvctnplsILEAVMAHCK 101
Cdd:pfam13868   99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKELEKEEERE--------EDERILEYLK 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  102 KMQERM-----------------SAQLAA--AESRQKKLEMEKLQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECK 161
Cdd:pfam13868  163 EKAEREeereaereeieeekereIARLRAqqEKAQDEKAERDELRAKLYQEEQERKERQKErEEAEKKARQRQELQQARE 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  162 QLsgkvIEEAQKLEDVMAKLEEE-----KKKTNELE--EELSAEKRR------STEMEAQMEkqlsefdtEREQLRAKLN 228
Cdd:pfam13868  243 EQ----IELKERRLAEEAEREEEefermLRKQAEDEeiEQEEAEKRRmkrlehRRELEKQIE--------EREEQRAAER 310

                          250       260
                   ....*....|....*....|....*.
gi 2462616488  229 REEAHT-TDLKEEIDKMRKMIEQLKR 253
Cdd:pfam13868  311 EEELEEgERLREEEAERRERIEEERQ 336
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
9-253 1.78e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.77  E-value: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    9 KKKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvct 87
Cdd:PRK03918   198 KEKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK----- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   88 nplsiLEAVMAHCKKMQERMSAQLAAAESRQKklEMEKLQLQALEQEhkklaaRLEEERGKNKQVVLMLVKECKQLSgkv 167
Cdd:PRK03918   257 -----LEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYI------KLSEFYEEYLDELREIEKRLSRLE--- 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 iEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMRK 246
Cdd:PRK03918   321 -EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLEK 391


                   ....*..
gi 2462616488  247 MIEQLKR 253
Cdd:PRK03918   392 ELEELEK 398
PTZ00121 PTZ00121
MAEBL; Provisional
 101-303 2.09e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLML----VKECKQLSGKVIEEAQKLED 176
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeeAKKAEELKKKEAEEKKKAEE 1720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  177 VMAKLEEEKKKTNELEEELSAEKRRSTEM--EAQMEKQLSEFDTEREQLRAKLNREEAHTtdLKEEIDKmrkmieqlkrg 254
Cdd:PTZ00121  1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDE----------- 1787

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  255 SDSKPSLSLPRKTKDRR---------------LVSISVGTEGTVTRSVACQTDLVTENADHMKK 303
Cdd:PTZ00121  1788 EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-252 2.54e-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: 62.38  E-value: 2.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    8 LKKKEFDVDTLSkSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagagdkekkpvct 87
Cdd:TIGR02168  717 LRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---------------- 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   88 nplsiLEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkv 167
Cdd:TIGR02168  780 -----AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS--- 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 iEEAQKLEDVMAKLEEEKkktNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnreEAHTTDLKEEIDKMRKM 247
Cdd:TIGR02168  852 -EDIESLAAEIEELEELI---EELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREK 923


                   ....*
gi 2462616488  248 IEQLK 252
Cdd:TIGR02168  924 LAQLE 928
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-253 3.97e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 3.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196    241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  184 EKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG1196    321 LEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-252 6.16e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 6.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   41 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI--LEAVMAHCKKMQERMSAQLAA 113
Cdd:PRK03918   393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  114 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKK 187
Cdd:PRK03918   471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  188 TNELEEELSA--EKRRSTEME-AQMEKQLSEFDTE----------------REQLRAK-----LNREEAHTTDLKEEIDK 243
Cdd:PRK03918   551 LEELKKKLAEleKKLDELEEElAELLKELEELGFEsveeleerlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630


                   ....*....
gi 2462616488  244 MRKMIEQLK 252
Cdd:PRK03918   631 AFEELAETE 639
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 703-845 8.61e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 8.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  703 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYD 782
Cdd:PHA02874    12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  783 AN-------------INHAADGG----------QTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 839
Cdd:PHA02874    92 VDtsilpipciekdmIKTILDCGidvnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171


                   ....*.
gi 2462616488  840 SLKLLM 845
Cdd:PHA02874   172 IIKLLL 177
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-252 9.08e-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: 60.46  E-value: 9.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   20 KSELRMLLSVMEGELEArdlviEALRARRKEVFIQE-RYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMA 98
Cdd:TIGR02168  241 LEELQEELKEAEEELEE-----LTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   99 HCKKMQERMSAQLAAAESR-----------QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV----------VLMLV 157
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  158 KECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME-AQMEKQLSEFDTEREQLRAKLNREEAHTTD 236
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEE 472

                          250
                   ....*....|....*.
gi 2462616488  237 LKEEIDKMRKMIEQLK 252
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 109-246 9.98e-09

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 57.63  E-value: 9.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEekKKT 188
Cdd:COG1579     17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGN--VRN 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  189 NE----LEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 246
Cdd:COG1579     88 NKeyeaLQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
694-746 1.18e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.18e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 746
Cdd:pfam13637    3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 118-245 1.29e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 54.54  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEMEKlQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSgkviEEAQKLEdvmakleeekKKTNELEEELsA 197
Cdd:pfam20492    6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLE----------QKRQEAEEEK-E 65

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  198 EKRRSTEMEA----QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:pfam20492   66 RLEESAEMEAeekeQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAR 117
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 113-252 1.32e-08

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 57.24  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  113 AAESRQKKLemekLQLQALEQEhkklAARLEEERGKnkqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELE 192
Cdd:COG1579      1 AMPEDLRAL----LDLQELDSE----LDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE 65

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  193 EELSAEKRRSTEMEAQM-----EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:COG1579     66 LEIEEVEARIKKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 349-718 1.35e-08

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 characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 59.78  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  349 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 428
Cdd:pfam03154  179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  429 AARFRFQGnandpdqngnTTQSPPSRDVSPTSrdnlvAKQLARNTVTQALSRftSPQAGAPSRP--------GVPPTGDV 500
Cdd:pfam03154  244 SPHPPLQP----------MTQPPPPSQVSPQP-----LPQPSLHGQMPPMPH--SLQTGPSHMQhpvppqpfPLTPQSSQ 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  501 GTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVAST 569
Cdd:pfam03154  307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQM 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  570 PSSLPQGNRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS 648
Cdd:pfam03154  387 NSNLPPPPALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQ 455

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  649 --SINPVSASSCRPGASDSLLvTASGWSPSLTPlLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 718
Cdd:pfam03154  456 vpSQSPFPQHPFVPGGPPPIT-PPSGPPTSTSS-AMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 763-852 1.71e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  763 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 842
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                           90
                   ....*....|
gi 2462616488  843 LLMYHRIPAH 852
Cdd:PTZ00322   166 LLSRHSQCHF 175
PTZ00121 PTZ00121
MAEBL; Provisional
 101-271 1.86e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVMA 179
Cdd:PTZ00121  1336 KKAEEaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELK 1411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  180 KLEEEKKKTNELEEElSAEKRRSTEMEAQME--KQLSEFDTEREQLR-----------------AKLNREEAHTTD-LKE 239
Cdd:PTZ00121  1412 KAAAAKKKADEAKKK-AEEKKKADEAKKKAEeaKKADEAKKKAEEAKkaeeakkkaeeakkadeAKKKAEEAKKADeAKK 1490

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462616488  240 EIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121  1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PTZ00121 PTZ00121
MAEBL; Provisional
 101-266 2.04e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAAR-------LEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 172
Cdd:PTZ00121  1540 KKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 KLEDVMAKLEEEKKKTNEL-----EEELSAEKRRSTEMEAQMEKqlsefdterEQLRAKLNREEAHTTDLKEEIDKMRKM 247
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKA---------AEEAKKAEEDKKKAEEAKKAEEDEKKA 1690

                          170
                   ....*....|....*....
gi 2462616488  248 IEQLKRGSDSKPSLSLPRK 266
Cdd:PTZ00121  1691 AEALKKEAEEAKKAEELKK 1709
PTZ00121 PTZ00121
MAEBL; Provisional
 101-380 2.68e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---R-LEEERGKNKQV--VLMLVKECKQLSGKVIEEAQKL 174
Cdd:PTZ00121  1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKkAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKA 1649

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELSAEKRRSTEM------EAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:PTZ00121  1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeedEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENK 1729

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  246 KMIEQLKRGS--DSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVKPST------GSP 317
Cdd:PTZ00121  1730 IKAEEAKKEAeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkdifdnFAN 1809

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  318 LVSANAKGS--VCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSST 380
Cdd:PTZ00121  1810 IIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-260 2.75e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   92 ILEAVMAHCKKMQErMSAQLAAAES---------RQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVLMLVKE 159
Cdd:COG4913    253 LLEPIRELAERYAA-ARERLAELEYlraalrlwfAQRRLELLEAELEELRAELARLEAeleRLEARLDALREELDELEAQ 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  160 CKQLSGKVIEEAQK--------LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE 231
Cdd:COG4913    332 IRGNGGDRLEQLEReierlereLEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411

                          170       180
                   ....*....|....*....|....*....
gi 2462616488  232 AHTTDLKEEIDKMRKMIEQLKRGSDSKPS 260
Cdd:COG4913    412 AALRDLRRELRELEAEIASLERRKSNIPA 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
31-252 3.24e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   31 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGAGDKEKkpvctnpLSILEAVMAH 99
Cdd:PRK03918   475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK-------LIKLKGEIKS 543

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  100 CKKMQERmsaqLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE---------- 169
Cdd:PRK03918   544 LKKELEK----LEELKKKLAELEKK---LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekeler 616

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  170 -------EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME--------AQMEKQLSEFDTEREQLRAKLNREEAHT 234
Cdd:PRK03918   617 eekelkkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696

                          250
                   ....*....|....*...
gi 2462616488  235 TDLKEEIDKMRKMIEQLK 252
Cdd:PRK03918   697 EKLKEELEEREKAKKELE 714
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
103-253 4.71e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.22  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  103 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLE 182
Cdd:COG4372     29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELE 104

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  183 EEKKKTNELE---EELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4372    105 SLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
PTZ00121 PTZ00121
MAEBL; Provisional
 74-269 5.34e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 5.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   74 EAGAGDKEKKPVCTNPLSilEAVMAHCKKMQERMSAqlaaaESRQKKLEMEKlqlqaLEQEHKKLAARLEEERGKnkqvv 153
Cdd:PTZ00121  1241 EAKKAEEERNNEEIRKFE--EARMAHFARRQAAIKA-----EEARKADELKK-----AEEKKKADEAKKAEEKKK----- 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  154 lmlVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRA-KLNREEA 232
Cdd:PTZ00121  1304 ---ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEA 1376

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462616488  233 httdlKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 269
Cdd:PTZ00121  1377 -----KKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 103-232 6.55e-08

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 52.61  E-value: 6.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  103 MQERMsaqlaaaesRQKKLEMEKLQLQALEQEHKklAARLEEERGKNKQvvlmlvkECKQLSgkviEEAQKLEDVMAKLE 182
Cdd:pfam20492   11 LEERL---------KQYEEETKKAQEELEESEET--AEELEEERRQAEE-------EAERLE----QKRQEAEEEKERLE 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462616488  183 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnrEEA 232
Cdd:pfam20492   69 ESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL--EEA 116
Ank_4 pfam13637
Ankyrin repeats (many copies);
794-844 7.25e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 7.25e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  794 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLL 844
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 30-301 7.42e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 57.49  E-value: 7.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   30 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGAGDKEKKpvctnpLSILEAVMAH 99
Cdd:pfam01576  775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEearasrdeilAQSKESEKK------LKNLEAELLQ 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  100 ckkMQErmsaQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKQVVLML-------VK 158
Cdd:pfam01576  845 ---LQE----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEARiaqLEEELEEEQSNTELLndrlrksTL 917

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  159 ECKQLSGKVIEE---AQKLEDVMAKLE----EEKKKTNELEEELSAEKRRS-TEMEA---QMEKQLSEFDTEREQLRAKL 227
Cdd:pfam01576  918 QVEQLTTELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKSKFKSSiAALEAkiaQLEEQLEQESRERQAANKLV 997

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  228 NREEAHTTDLKEEIDKMRKMIEQLKRGSDsKPSLSLprKTKDRRLVSisvgTEGTVTRSVA----CQTDL--VTENADHM 301
Cdd:pfam01576  998 RRTEKKLKEVLLQVEDERRHADQYKDQAE-KGNSRM--KQLKRQLEE----AEEEASRANAarrkLQRELddATESNESM 1070
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 55-215 8.52e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 56.35  E-value: 8.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   55 ERYGRfnlndpflalQRDYEAGAGDKEKKPvctnplsileavmahcKKMQERMSAQL----AAAESRQKKLEMEKLQLQA 130
Cdd:PRK09510    62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  131 lEQEHKKLAARLEEErgKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME 210
Cdd:PRK09510   116 -QKKQAEEAAKQAAL--KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192


                   ....*
gi 2462616488  211 KQLSE 215
Cdd:PRK09510   193 AKAAA 197
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-250 1.07e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEH--------KKLAARLEEERGKNKQVVLMLVKECK 161
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLA 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  162 QLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEkrrstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 241
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-------LAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442


                   ....*....
gi 2462616488  242 DKMRKMIEQ 250
Cdd:COG4913    443 LALRDALAE 451
PHA03247 PHA03247
large tegument protein UL36; Provisional
 253-695 1.10e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  253 RGSDSKPSLSLPRKTKDR-RLVSISVGTEGTVTRSVACQTDLVTENAD--HMKKLPLTMPVKPSTGSPLVSANAKGSVCT 329
Cdd:PHA03247  2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  330 SATMARPGidrqasygdligasvpafPPPSANkieenGPSTGSTPDPTsSTPPLPSNAAPPTA-QTPGIAPQNSQAPPMH 408
Cdd:PHA03247  2733 PALPAAPA------------------PPAVPA-----GPATPGGPARP-ARPPTTAGPPAPAPpAAPAAGPPRRLTRPAV 2788

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  409 SLHSPCANTSLHPGLNPRIQAArfrfqgnANDPDQNGNTTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGA 488
Cdd:PHA03247  2789 ASLSESRESLPSPWDPADPPAA-------VLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPP 2848

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  489 PSRPG--VPPTGDVGTHPPVGRTSLKTHGVAR--VDRGNPPPIPPKKPGLSQTPSPPHPQlkviidssrasntgakvdnK 564
Cdd:PHA03247  2849 SLPLGgsVAPGGDVRRRPPSRSPAAKPAAPARppVRRLARPAVSRSTESFALPPDQPERP-------------------P 2909

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  565 TVASTPSSLPQgnrviNEENLPKSSSPQLPPKPSIDLTVAPAgcAVSALATSQVGAWPAATPGLNQPAcsdSSLVIPTTI 644
Cdd:PHA03247  2910 QPQAPPPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAPT--TDPAGAGEPSGAVPQPWLGALVPG---RVAVPRFRV 2979

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  645 AFCSSINPVSASSCRPgASDSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 695
Cdd:PHA03247  2980 PQPAPSREAPASSTPP-LTGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-253 1.63e-07

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: 56.29  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   33 ELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGAGDKEKK------------PVCTNPLSILEAVMAHC 100
Cdd:pfam17380  311 EVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEERkrelerirqeeiAMEISRMRELERLQMER 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAA-------ESRQKKL-----EMEKL----------QLQALEQEHKKLAARL-EEERGKNKQVVLMLV 157
Cdd:pfam17380  388 QQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIraeqeearqrEVRRLEEERAREMERVrLEEQERQQQVERLRQ 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  158 KECKQLSGKVIEEAQKLEDvmAKLEEEKKKT--NELEEELSA---EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDR--KRAEEQRRKIleKELEERKQAmieEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ 545

                          250       260
                   ....*....|....*....|..
gi 2462616488  233 HTTDLKEEI-DKMRKMIEQLKR 253
Cdd:pfam17380  546 QEMEERRRIqEQMRKATEERSR 567
PHA03247 PHA03247
large tegument protein UL36; Provisional
 350-702 1.90e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  350 ASVPAFPPPSANKIEENGPStGSTPDPTSSTPPlPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQA 429
Cdd:PHA03247  2586 ARRPDAPPQSARPRAPVDDR-GDPRGPAPPSPL-PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  430 AR-FRFQGNANDPdqngnttQSPPSRDVSPTSRDNLVA-KQLAR---------NTVTQALSRFTSPQAGAPSRPGVPPTG 498
Cdd:PHA03247  2664 PRrARRLGRAAQA-------SSPPQRPRRRAARPTVGSlTSLADpppppptpePAPHALVSATPLPPGPAAARQASPALP 2736

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  499 DVGTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR 578
Cdd:PHA03247  2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  579 VINEENLPkssSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAATPGLNQPACSDSSLVIPTTiafcsSINPVSASSC 658
Cdd:PHA03247  2817 ALPPAASP---AGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA-----PARPPVRRLA 2887

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2462616488  659 RPGASDSllvTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 702
Cdd:PHA03247  2888 RPAVSRS---TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 694-833 2.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF 772
Cdd:PHA02876   275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  773 -ECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 833
Cdd:PHA02876   355 kDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
PTZ00121 PTZ00121
MAEBL; Provisional
 101-272 2.53e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKqlsgKVIEEAQKLEDVMAK 180
Cdd:PTZ00121  1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  181 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRKMiEQLKRGSDSKPS 260
Cdd:PTZ00121  1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKADELKKA-EELKKAEEKKKA 1566

                          170
                   ....*....|..
gi 2462616488  261 LSLPRKTKDRRL 272
Cdd:PTZ00121  1567 EEAKKAEEDKNM 1578
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-253 2.85e-07

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: 55.83  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARDLVIEALRARRKEVfIQERYGRFNLNDP-FLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHC 100
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREaLDELRAELTLLNEEAANL---RERLESLERRIAAT 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnKQVVLMLVKEckqlsgkvieeaqKLEDVMAK 180
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRS-------------ELEELSEE 902

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  181 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLEN 979
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 136-240 3.90e-07

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: 51.21  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  136 KKLAARLEEERGKNKQVVLMLVKECKQ-LSGKVIEEAQK-----LEDVMAKLEEEKKKTNELEEELsAEKRRSTEmEAQ- 208
Cdd:pfam15346   22 KRVEEELEKRKDEIEAEVERRVEEARKiMEKQVLEELERereaeLEEERRKEEEERKKREELERIL-EENNRKIE-EAQr 99

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462616488  209 --MEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 240
Cdd:pfam15346  100 keAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
88-251 3.92e-07

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 52.52  E-value: 3.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   88 NPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEeergknkqvvLMLVKECKQLSGKV 167
Cdd:COG1842     23 DPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLER---QLEELEAEAEKWEEKAR----------LALEKGREDLAREA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 IEEAQKLEDVMAKLEEEKKKTNELEEELsaekrrsTEMEAQMEKQLSEFDTEREQLRAKLNREEA-----------HTTD 236
Cdd:COG1842     90 LERKAELEAQAEALEAQLAQLEEQVEKL-------KEALRQLESKLEELKAKKDTLKARAKAAKAqekvnealsgiDSDD 162

                          170
                   ....*....|....*
gi 2462616488  237 LKEEIDKMRKMIEQL 251
Cdd:COG1842    163 ATSALERMEEKIEEM 177
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 104-272 4.38e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.18  E-value: 4.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSA---QLAAAESRQKKLEMEklqLQALEQEHKKLAA---RLEEERgknkQVVLMLVKECKQLSGKVIEEAQKLEDV 177
Cdd:pfam01576    4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEeknALQEQL----QAETELCAEAEEMRARLAARKQELEEI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 M----AKLEEEKKKTNELEeelsAEKRRSTEMEAQMEKQLSefdtEREQLRAKLNREEAhTTDlkeeiDKMRKMIEQLKR 253
Cdd:pfam01576   77 LheleSRLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLD----EEEAARQKLQLEKV-TTE-----AKIKKLEEDILL 142

                          170
                   ....*....|....*....
gi 2462616488  254 GSDSKPSLSLPRKTKDRRL 272
Cdd:pfam01576  143 LEDQNSKLSKERKLLEERI 161
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 163-257 4.90e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 54.83  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  163 LSGKVIEEAQ--------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnREEAH- 233
Cdd:PRK00409   499 LPENIIEEAKkligedkeKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQq 577

                           90       100
                   ....*....|....*....|....*
gi 2462616488  234 -TTDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:PRK00409   578 aIKEAKKEADEIIKELRQLQKGGYA 602
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 313-712 4.94e-07

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: 54.92  E-value: 4.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  313 STGSPLVSANAKGSVCTSATMARPGIdrqASYGDLIGASVPAFPPPSANKIEENGPsTGSTPDPTSSTPPLPSNAAPPTa 392
Cdd:pfam05109  414 TTTHKVIFSKAPESTTTSPTLNTTGF---AAPNTTTGLPSSTHVPTNLTAPASTGP-TVSTADVTSPTPAGTTSGASPV- 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  393 qTPGIAPQN----SQAP----PMHSLHSPCAN-TSLHPGLNPRIQAARFRFQGNANdpDQNGNTTQSPPSRDVSP---TS 460
Cdd:pfam05109  489 -TPSPSPRDngteSKAPdmtsPTSAVTTPTPNaTSPTPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNATSPTPavtTP 565

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  461 RDNLVAKQLARNTVTQALSRFTsPQAGAPSRPGVPPTGDVGTH-------------PPVGRTSLKTHGVARVDRGNPPPI 527
Cdd:pfam05109  566 TPNATIPTLGKTSPTSAVTTPT-PNATSPTVGETSPQANTTNHtlggtsstpvvtsPPKNATSAVTTGQHNITSSSTSSM 644

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  528 PPKKPGLSQTPSP---------------PHPQ-LKVIIDSSRASNTGAKVDNKTVASTPSSLPQ----GNRVIN----EE 583
Cdd:pfam05109  645 SLRPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEV 724

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  584 NLPKSSSPQLPPKPSidltvAPAGCAVSA-LATSQVGAWPAATPGLNQPACSDSSLVIPTTIAFCSSINP---VSASSCR 659
Cdd:pfam05109  725 NVTKGTPPKNATSPQ-----APSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPrtrYNATTYL 799

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  660 PGASDSLLvtASGWSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 712
Cdd:pfam05109  800 PPSTSSKL--RPRWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-237 5.76e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 5.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKvIEEAQKLEDVMAKLEEEKKKT 188
Cdd:COG4913    668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE----LKGEIGRLEKE-LEQAEEELDELQDRLEAAEDL 742

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462616488  189 NELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDL 237
Cdd:COG4913    743 ARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 93-413 6.05e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.68  E-value: 6.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGK-NKQVVLMlvkeckQLSG------ 165
Cdd:COG3883     32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARAL------YRSGgsvsyl 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  166 -------------------KVIEEAQKleDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 226
Cdd:COG3883    106 dvllgsesfsdfldrlsalSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  227 LNREEAhttDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTEnadhmkklpl 306
Cdd:COG3883    184 LAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG---------- 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  307 tmpvkpstGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSN 386
Cdd:COG3883    251 --------AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322

                          330       340
                   ....*....|....*....|....*..
gi 2462616488  387 AAPPTAQTPGIAPQNSQAPPMHSLHSP 413
Cdd:COG3883    323 VGGASAGGGGGSGGGGGSSGGGSGGGG 349
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 117-251 7.12e-07

MAP7 (E-MAP-115) family; The organization 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-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 50.42  E-value: 7.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  117 RQKKLEMEKLQLQALEQEhkklaarlEEERgknkqvvlmLVKEckQLSGKVIEEAQKLEDVMAKLEEEKKKTnelEEELS 196
Cdd:pfam05672   21 RQAREQREREEQERLEKE--------EEER---------LRKE--ELRRRAEEERARREEEARRLEEERRRE---EEERQ 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  197 AEKRRSTEMEAQMEKQlsefdterEQLRAKLNREEAHTTdLKEEIDKMRKMIEQL 251
Cdd:pfam05672   79 RKAEEEAEEREQREQE--------EQERLQKQKEEAEAK-AREEAERQRQEREKI 124
Ank_5 pfam13857
Ankyrin repeats (many copies);
711-763 7.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 7.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  711 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPL 763
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-253 7.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 7.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAA--ESRQKKLEMEKLQLQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQKLE 175
Cdd:COG1196    219 KEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  176 DVMAKLEEEKKKTNELE---EELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:COG1196    299 RLEQDIARLEERRRELEerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378


                   .
gi 2462616488  253 R 253
Cdd:COG1196    379 E 379
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 728-832 8.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 52.68  E-value: 8.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  728 SALYSAAKNGHTDCVRLLL----SAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ-TPLYLACKN 802
Cdd:PHA02884    35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462616488  803 GNKECIKLLLEAGTNRSVKTTDGWTPVHAA 832
Cdd:PHA02884   115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 104-258 8.28e-07

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: 53.87  E-value: 8.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKQVVLMLV------------KECKQLSGK 166
Cdd:TIGR04523  403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  167 VIEEAQKLEDvmaKLEEEKKKTNELEEeLSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM-- 244
Cdd:TIGR04523  477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdf 552

                          170
                   ....*....|....*..
gi 2462616488  245 ---RKMIEQLKRGSDSK 258
Cdd:TIGR04523  553 elkKENLEKEIDEKNKE 569
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 734-812 8.32e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 8.32e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  734 AKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 812
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00121 PTZ00121
MAEBL; Provisional
 101-271 9.10e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 9.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSA-QLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDvm 178
Cdd:PTZ00121  1528 KKAEEAKKAdEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEED--------------KNMALRKAEEAKKAEE-- 1591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  179 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLK--EEIDKMRKMIEQLKR 253
Cdd:PTZ00121  1592 -ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKA 1670

                          170
                   ....*....|....*...
gi 2462616488  254 GSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEK 1688
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
93-251 9.38e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 9.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKECKQLSGKvIEEAQ 172
Cdd:PRK03918   167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEE-IEELE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 ----KLEDVMAKLEEEKKKT----NELE---EELSAEKRRSTEMEAQMEK--QLSEFdteREQLRAKLNREEAHTTDLKE 239
Cdd:PRK03918   245 keleSLEGSKRKLEEKIRELeeriEELKkeiEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRLEE 321

                          170
                   ....*....|..
gi 2462616488  240 EIDKMRKMIEQL 251
Cdd:PRK03918   322 EINGIEERIKEL 333
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 127-252 1.09e-06

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 53.80  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  127 QLQALEQEHKKLAARLEEErgknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 206
Cdd:COG3096    513 RLQQLRAQLAELEQRLRQQ-----QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL-------EELEEQAAEAVEQR 580

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  207 AQMEKQLSEFDTEREQLRAK----------LNREEAHT----TDLKEEIDKMRKMIEQLK 252
Cdd:COG3096    581 SELRQQLEQLRARIKELAARapawlaaqdaLERLREQSgealADSQEVTAAMQQLLERER 640
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-271 1.11e-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: 53.53  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 179
Cdd:TIGR02169  218 KEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  180 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR--GSDS 257
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVD 377

                          170
                   ....*....|....
gi 2462616488  258 KPSLSLPRKTKDRR 271
Cdd:TIGR02169  378 KEFAETRDELKDYR 391
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
113-258 1.13e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.22  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  113 AAESRQKKLEMEKLQ--LQALE--QEHKKLaaRLEEERgknkqvvlMLVKECKQLSgKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:COG1340    101 LAELNKAGGSIDKLRkeIERLEwrQQTEVL--SPEEEK--------ELVEKIKELE-KELEKAKKALEKNEKLKELRAEL 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  189 NELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKlnREEAHTT-----------------------DLKEEID 242
Cdd:COG1340    170 KELRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKE--ADELHKEiveaqekadelheeiielqkelrELRKELK 247

                          170
                   ....*....|....*.
gi 2462616488  243 KMRKMIEQLKRGSDSK 258
Cdd:COG1340    248 KLRKKQRALKREKEKE 263
mukB PRK04863
chromosome partition protein MukB;
127-226 1.39e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.42  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  127 QLQALEQEHKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 206
Cdd:PRK04863   514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581

                           90       100
                   ....*....|....*....|
gi 2462616488  207 AQMEKQLSEFDTEREQLRAK 226
Cdd:PRK04863   582 MALRQQLEQLQARIQRLAAR 601
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 694-830 1.52e-06

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: 53.09  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 768
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  769 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 830
Cdd:cd22192     99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-232 1.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL--------------EELEEALAELEEEEEEEEEALEE 446

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462616488  184 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-201 2.02e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   21 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagAGDKEKKPVCTNP---------LS 91
Cdd:COG4942     65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR-----LGRQPPLALLLSPedfldavrrLQ 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   92 ILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKV---I 168
Cdd:COG4942    140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaelQ 219

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2462616488  169 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 201
Cdd:COG4942    220 QEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 105-252 2.11e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 52.87  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKQVVLMLVKECK---------------QLSGKV 167
Cdd:pfam01576  920 EQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeqleqesrerQAANKL 996

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 IEEAQK-LEDVMAKLEEEKKKTNELEEElsAEKrrSTEMEAQMEKQLSEfdTEREQLRA-----KLNREeahTTDLKEEI 241
Cdd:pfam01576  997 VRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKLQRE---LDDATESN 1067

                          170
                   ....*....|.
gi 2462616488  242 DKMRKMIEQLK 252
Cdd:pfam01576 1068 ESMNREVSTLK 1078
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
107-252 2.40e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 51.45  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  107 MSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKQLSGKVIEEAQKLEDVMAKLE 182
Cdd:COG1340      6 LSSSLEELEEKIEELREEieelKEKRDELNEELKELAEKRDELNAQ--------VKELREEAQELREKRDELNEKVKELK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  183 EEK----KKTNELEEEL------SAEKRRSTEMEAQMEKQLSEFdtEREQLRAKLNREE-----AHTTDLKEEIDKMRKM 247
Cdd:COG1340     78 EERdelnEKLNELREELdelrkeLAELNKAGGSIDKLRKEIERL--EWRQQTEVLSPEEekelvEKIKELEKELEKAKKA 155


                   ....*
gi 2462616488  248 IEQLK 252
Cdd:COG1340    156 LEKNE 160
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 168-253 2.67e-06

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 47.95  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT-----EREQLRA--KLNREEAHTTDLKEE 240
Cdd:pfam13863    2 LEKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81

                           90
                   ....*....|...
gi 2462616488  241 IDKMRKMIEQLKR 253
Cdd:pfam13863   82 IKKLTAQIEELKS 94
Ank_5 pfam13857
Ankyrin repeats (many copies);
782-832 2.87e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  782 DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAA 832
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-252 3.05e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  115 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKQVVLM-------LVKECKQLSGKVIEEAQKLEDVMAKLEEEK 185
Cdd:PRK03918   145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  186 KKTNELEEELsaEKRRstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:PRK03918   224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
PHA02798 PHA02798
ankyrin-like protein; Provisional
 739-845 3.24e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.76  E-value: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  739 TDCVRLLLSAEAQVNAADKNGFTPLCAAAA-----QGHFECVELLISYDANINHAADGGQTPLYLACKNG---NKECIKL 810
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462616488  811 LLEAGTNRSVKTTDGWTPVHAAVDTGN---VDSLKLLM 845
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 696-781 3.45e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 3.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  696 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECV 775
Cdd:PTZ00322    86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                   ....*.
gi 2462616488  776 ELLISY 781
Cdd:PTZ00322   165 QLLSRH 170
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 105-256 3.98e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 51.71  E-value: 3.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKQvvlmLVKECKQLSGKVI--------EEA--QKL 174
Cdd:pfam01576   60 EEMRARLAA-----RKQELEEI-LHELE-------SRLEEEEERSQQ----LQNEKKKMQQHIQdleeqldeEEAarQKL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 --EDV-----MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL-----KEEid 242
Cdd:pfam01576  123 qlEKVtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLeerlkKEE-- 200

                          170
                   ....*....|....
gi 2462616488  243 KMRKMIEQLKRGSD 256
Cdd:pfam01576  201 KGRQELEKAKRKLE 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 118-258 4.06e-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: 51.56  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEMEKLQLQALEQEHKKLAARLEeergkNKQvvlmlvKECKQLSGKVIEEAQKLEDVMAKLEEEKKK-----TNELE 192
Cdd:TIGR04523  245 TTEISNTQTQLNQLKDEQNKIKKQLS-----EKQ------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  193 EELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 258
Cdd:TIGR04523  314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-253 4.28e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:COG1196    639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---------EELAERLAEEELELEEALLAEEEEEREL 709

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  189 NELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG1196    710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 101-253 4.58e-06

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: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 50.81  E-value: 4.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSaQLAAAESRQKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK---QVVLMLVKEckqlsgkvIEEAQKL 174
Cdd:pfam15558   87 KQVIEKES-RWREQAEDQENQRQEKLERARQEAEQRKQcqEQRLkEKEEELQAlreQNSLQLQER--------LEEACHK 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 EDVMAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRAKLNRE---EAHTTDLKEEIDKMRKMIEQ 250
Cdd:pfam15558  158 RQLKEREEQKKVQENNLSELLNHQARkVLVDCQAKAEELLRRLSLEQSLQRSQENYEqlvEERHRELREKAQKEEEQFQR 237


                   ...
gi 2462616488  251 LKR 253
Cdd:pfam15558  238 AKW 240
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 100-233 4.75e-06

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: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 47.59  E-value: 4.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  100 CKKMQERMSAQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkqvvlmLVKECKQLSgkviEEA 171
Cdd:pfam17675    7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  172 QKLEDVMAKLEEEKKKTNELEEELSAEKRrstemeaQMEKQLSEFDTEREQLRAKLNREEAH 233
Cdd:pfam17675   72 EELDAELEALEEELEALDEEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 8-248 5.65e-06

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: 51.38  E-value: 5.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    8 LKKKEFDVDTLSKsELRMLLSVMEGELEARDlviEALRARRKEV-FIQERYGRFnlndpflaLQRDYEAGAGDKEKKPVC 86
Cdd:pfam12128  285 SAELNQLLRTLDD-QWKEKRDELNGELSAAD---AAVAKDRSELeALEDQHGAF--------LDADIETAAADQEQLPSW 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   87 TNPLSILEAVMA----------------------HCKKMQERMSAQLAAA-ESRQKKLEMEKLQLQALEQE-HKKLAARL 142
Cdd:pfam12128  353 QSELENLEERLKaltgkhqdvtakynrrrskikeQNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQALESElREQLEAGK 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  143 EEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEdvmakLEEEKKKTNELEEELsaEKRRSTEMEAQMEkqLSEFDTEREQ 222
Cdd:pfam12128  433 LEFNEEEYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERAREEQ--EAANAEVERLQSE--LRQARKRRDQ 503

                          250       260
                   ....*....|....*....|....*.
gi 2462616488  223 LRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam12128  504 ASEALRQASRRLEERQSALDELELQL 529
PRK12704 PRK12704
phosphodiesterase; Provisional
 108-253 5.78e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.93  E-value: 5.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  108 SAQLAAAESRQKK-LEMEKLQLQALEQEhKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKK 186
Cdd:PRK12704    30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNE-----FEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  187 KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR------EEAhttdlKEEIdkMRKMIEQLKR 253
Cdd:PRK12704   104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEA-----KEIL--LEKVEEEARH 169
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
101-236 6.06e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 6.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEME------KLQLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKVIEEA 171
Cdd:COG1340    143 KELEKELEKAKKALEKNEKLKELRaelkelRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKEADELHKEIVEAQ 222

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  172 QKLEDVMAKLEEEKKKTNELEEELSaeKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTD 236
Cdd:COG1340    223 EKADELHEEIIELQKELRELRKELK--KLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 90-252 7.55e-06

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: 48.25  E-value: 7.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   90 LSILEAVMAHCKKMQERMS---AQLAAAESRQKKLEMEKLQL--QALEQEHKKLAAR-LEEERGKNKQVVLMLVKECKQL 163
Cdd:pfam14662    7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQKEKlLEEELEDLKLIVNSLEEARRSL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  164 SGK---VIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 240
Cdd:pfam14662   87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166

                          170
                   ....*....|..
gi 2462616488  241 IDKMRKMIEQLK 252
Cdd:pfam14662  167 VEEYSSIEEELR 178
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 133-252 7.89e-06

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: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 49.59  E-value: 7.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  133 QEHKKLAARLEEERGKNKQVVLMLVKECKqlSGKVIEEA-----QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 207
Cdd:pfam02841  155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ--SKEAVEEAilqtdQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQ 232

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462616488  208 QMEKQLSEFDTEREQLRAKLNREEAHttdLKEEIDKM--RKMIEQLK 252
Cdd:pfam02841  233 MMEAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
128-253 9.56e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  128 LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 207
Cdd:COG4717     44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462616488  208 QmeKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4717    124 L--LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 101-258 1.09e-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: 50.49  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKE-------CKQLSGKVIE 169
Cdd:pfam05483   91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKEnnatrhlCNLLKETCAR 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  170 EAQKledvMAKLEEEKKKTNELEEELSaekrrstemeAQMEKQLSEFDTEREQlrAKLNREEAHTTdLKEEIDKMRKMIE 249
Cdd:pfam05483  167 SAEK----TKKYEYEREETRQVYMDLN----------NNIEKMILAFEELRVQ--AENARLEMHFK-LKEDHEKIQHLEE 229


                   ....*....
gi 2462616488  250 QLKRGSDSK 258
Cdd:pfam05483  230 EYKKEINDK 238
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 695-844 1.11e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  695 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFEC 774
Cdd:PHA02876   148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  775 VELLISYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTnrSVKTTDGW--TPVHAAVDTGNVDSL--KLL 844
Cdd:PHA02876   227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvpKLL 294
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 115-245 1.13e-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: 47.38  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  115 ESRQKKLEMEKLQLQAlEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQ-KLEDVMAKLEEEKKKTNELEE 193
Cdd:pfam11600    5 KSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKEKDE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  194 ELSAEKRRSTEmEAQMEKQlsefdterEQLRAKL--NREEAHTTDLKEEIDKMR 245
Cdd:pfam11600   80 KEKAEKLRLKE-EKRKEKQ--------EALEAKLeeKRKKEEEKRLKEEEKRIK 124
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-253 1.13e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEmEKLQLQALEQEHKKL--------------AARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:COG4717    347 EELQELLREAEELE-EELQLEELEQEIAALlaeagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 --EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK-----QLSEFDTEREQLRAKLNR--EEAHTTDLKEEIdkMR 245
Cdd:COG4717    426 deEELEEELEELEEELEELEEELEELREELAELEAELEQleedgELAELLQELEELKAELRElaEEWAALKLALEL--LE 503


                   ....*...
gi 2462616488  246 KMIEQLKR 253
Cdd:COG4717    504 EAREEYRE 511
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 711-787 1.18e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 1.18e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  711 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINH 787
Cdd:PHA03100   177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 99-271 1.23e-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: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   99 HCKKMQERMSAQLAAAESRQKKL--EMEKLQlQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:pfam05483  524 NCKKQEERMLKQIENLEEKEMNLrdELESVR-EEFIQKGDEVKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:pfam05483  603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682

                          170
                   ....*....|....*...
gi 2462616488  254 GSDSKPSLslpRKTKDRR 271
Cdd:pfam05483  683 IADEAVKL---QKEIDKR 697
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 696-833 1.25e-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: 50.08  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  696 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 762
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  763 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 826
Cdd:TIGR00870  132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209


                   ....*..
gi 2462616488  827 TPVHAAV 833
Cdd:TIGR00870  210 TLLHLLV 216
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 100-257 1.51e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. 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 this 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. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 49.69  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  100 CKKMQERMSAQLAAAES--------RQKKLEMEKLQLQALEQEHKKLAARLEEERGKN--KQVVLMLVKE---CKQLSGK 166
Cdd:pfam05622  213 YKKLEEKLEALQKEKERliierdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNlaAEIMPAEIREkliRLQHENK 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  167 VIEEAQ------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTERE---QLRAKLNREEAHT 234
Cdd:pfam05622  293 MLRLGQegsyreRLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKLEEHLEKL 372

                          170       180
                   ....*....|....*....|...
gi 2462616488  235 TDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:pfam05622  373 HEAQSELQKKKEQIEELEPKQDS 395
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
141-253 1.74e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  141 RLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----------LEEELSAEKRRSTEMEAQM 209
Cdd:COG4372      3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREeleqareeleqLEEELEQARSELEQLEEEL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462616488  210 E---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4372     83 EelnEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-251 1.80e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 177
Cdd:PRK02224   519 EDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEV----AELNSKLAELKERIESLERI 594

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  178 MAKLEEEKKKTNELEEElsAEKRRS-TEMEAQMEKQLSEFDTEREQLRAKLnrEEAHTTDLKEEIDKMRKMIEQL 251
Cdd:PRK02224   595 RTLLAAIADAEDEIERL--REKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 792-817 2.08e-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: 42.57  E-value: 2.08e-05
                            10        20
                    ....*....|....*....|....*.
gi 2462616488   792 GQTPLYLACKNGNKECIKLLLEAGTN 817
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-283 2.10e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEckqlsgkvIEEAQKLEDVMA 179
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELE 424

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  180 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR---KMIEQLKRGSD 256
Cdd:COG1196    425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLLLLEAEADYE 504

                          170       180
                   ....*....|....*....|....*...
gi 2462616488  257 SKPSLSLPRKTKD-RRLVSISVGTEGTV 283
Cdd:COG1196    505 GFLEGVKAALLLAgLRGLAGAVAVLIGV 532
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 758-786 2.30e-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: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 2.30e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462616488  758 NGFTPL-CAAAAQGHFECVELLISYDANIN 786
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 168-258 2.31e-05

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 organization 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: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 47.72  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 IEEAQ-KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHTTdlKEEIDKMRK 246
Cdd:pfam00261   10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKL------EEAEKA--ADESERGRK 81

                           90
                   ....*....|..
gi 2462616488  247 MIEQLKRGSDSK 258
Cdd:pfam00261   82 VLENRALKDEEK 93
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 758-786 2.39e-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: 42.57  E-value: 2.39e-05
                            10        20
                    ....*....|....*....|....*....
gi 2462616488   758 NGFTPLCAAAAQGHFECVELLISYDANIN 786
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-246 2.40e-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: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknKQVVLMLVKECKQlsgKVIEEAQ 172
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALEN---KIEDDEE 968

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 KLEDVMAKLEEEKKK---TNEL-EEELSAEKRRSTEMEAQMEkqlsEFDTEREQLR---AKLNREEahTTDLKEEIDKMR 245
Cdd:TIGR02168  969 EARRRLKRLENKIKElgpVNLAaIEEYEELKERYDFLTAQKE----DLTEAKETLEeaiEEIDREA--RERFKDTFDQVN 1042


                   .
gi 2462616488  246 K 246
Cdd:TIGR02168 1043 E 1043
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-246 2.52e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLE-----EERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMA 179
Cdd:COG4913    610 AKLAALEAELAELEEElaeaEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELE-AELERLDASSDDLA 688

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  180 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR-EEAHTTDLKEEIDKMRK 246
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFA 756
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 96-252 2.81e-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: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 48.90  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   96 VMAHCKKMQERMSA-QLAAAESRQKKLEMEKLQLQaleqehkKLAArleEERGKNKQVVLmlvKECKQLSGKVIEEA-QK 173
Cdd:pfam05911    5 VKQHAKVAEEAVSGwEKAEAEALALKQQLESVTLQ-------KLTA---EERAAHLDGAL---KECMQQLRNVKEEQeQK 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  174 LEDV-MAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMI 248
Cdd:pfam05911   72 IHDVvLKKTKEWEKIKAELEAKLVETEQELLRAAAE-NDALSRSLQERENLLMKLSEEksqaEAEIEALKSRLESCEKEI 150


                   ....
gi 2462616488  249 EQLK 252
Cdd:pfam05911  151 NSLK 154
PHA03369 PHA03369
capsid maturational protease; Provisional
 200-633 2.94e-05

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 48.84  E-value: 2.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  200 RRSTEMEAQMEKQLSEFDTEREQlraKLNREEAHTTDLKEEIDKMRKMIEQLKrgsDSKPSLSLPRKTKDRRLVS--ISV 277
Cdd:PHA03369   257 RQGEAPLNALLEILKAKNAEMPG---TLNPSFGSSDESPEWKTFYEALADQLN---NLYKLLRTIYKHKDETVIEqyLIE 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  278 GTEGTVTrsvacqtdlVTENADHMKKLPLTMPVKPStgSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPP 357
Cdd:PHA03369   331 GRKLFST---------INGLKAHNEILKTASLTAPS--RVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSP 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  358 PSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAP-PMHSLhspcantsLHPGLNPRIQAARFRFQG 436
Cdd:PHA03369   400 MTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPiSMANM--------VYPGHPQEHGHERKRKRG 471

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  437 NANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSrPGVPPTGDVGTHPPVGRTSLKT--H 514
Cdd:PHA03369   472 GELKEELIETLKLVKKLKEEQESLAKELEATAHKSEIKKIAESEFKNAGAKTAA-ANIEPNCSADAAAPATKRARPEtkT 550

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  515 GVARVDRgnPPPIPPKKPGLSQTPSPPHPQLKVIIdsSRASNTGAKVDN--KTVASTPSSLPQGNRVINEENLPKSSSPQ 592
Cdd:PHA03369   551 ELEAVVR--FPYQIRNMESPAFVHSFTSTTLAAAA--GQGSDTAEALAGaiETLLTQASAQPAGLSLPAPAVPVNASTPA 626

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2462616488  593 LPPKPSIDLTVAPAGCAVSALATSQvgawPAATPGLNQPAC 633
Cdd:PHA03369   627 STPPPLAPQEPPQPGTSAPSLETSL----PQQKPVLSKGAF 663
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 46-252 3.38e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.81  E-value: 3.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   46 ARRKEVFIQERygrfNLNDPFLALQRDYEAgagDKEKKPVCTNPLSILEAVMAHCKKMQERMSA---QLAAAESrQKKLE 122
Cdd:TIGR00618  365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDlqgQLAHAKK-QQELQ 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  123 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKQVVLMLVKECKQLSGKVIEEAQ---------------- 172
Cdd:TIGR00618  437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQeepcplcgscihpnpa 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 ---------------KLEDVMAKLEEEKKKTnelEEELSAEKRRSTEMEAQMEkqlsEFDTEREQLRAKLNReeahttdL 237
Cdd:TIGR00618  517 rqdidnpgpltrrmqRGEQTYAQLETSEEDV---YHQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNR-------S 582

                          250
                   ....*....|....*
gi 2462616488  238 KEEIDKMRKMIEQLK 252
Cdd:TIGR00618  583 KEDIPNLQNITVRLQ 597
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 80-302 3.44e-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: 48.89  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   80 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVK- 158
Cdd:TIGR00606  216 KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKv 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  159 ------ECKQL----SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTERE--QL 223
Cdd:TIGR00606  296 fqgtdeQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQslAT 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  224 RAKLNREEaHTTDLKEEID-----KMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGtVTRSVACQTDLVTENA 298
Cdd:TIGR00606  376 RLELDGFE-RGPFSERQIKnfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG-LGRTIELKKEILEKKQ 453


                   ....
gi 2462616488  299 DHMK 302
Cdd:TIGR00606  454 EELK 457
PHA03095 PHA03095
ankyrin-like protein; Provisional
 704-852 3.55e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  704 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKNGFTPLCAAAAqgHFECVELLISY 781
Cdd:PHA03095   166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLP 242

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  782 ----DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRIPAH 852
Cdd:PHA03095   243 lliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 115-253 4.05e-05

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: 48.43  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  115 ESRQKKLEMEKLQLQALEQEHKK--LAAR---LEEERGKNKQVVLMLVKECKQLSGKVIE-EAQKLEDVMAKLEEEKKKT 188
Cdd:pfam02463  202 LKEQAKKALEYYQLKEKLELEEEylLYLDylkLNEERIDLLQELLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  189 NELEEELS--AEKRRSTEMEAQMEKQLSEFDTEREQL-RAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:pfam02463  282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-207 4.40e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   21 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGAGDKEKKPV----CTNPLSILEAV 96
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESR 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   97 MAHCKKMQERMSAQLAAAESRQKKLEME-----------KLQLQALEQEHKKL--AARLEEERGKNKQVVLMLVKECKql 163
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQiekkrkrlselKAKLEALEEELSEIedPKGEDEEIPEEELSLEDVQAELQ-- 961

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  164 sgKVIEEAQKLEDV---------------------MAKLEEEKKKTNELEEELSaEKRRSTEMEA 207
Cdd:TIGR02169  962 --RVEEEIRALEPVnmlaiqeyeevlkrldelkekRAKLEEERKAILERIEEYE-KKKREVFMEA 1023
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 69-253 4.56e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. 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 this 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. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 48.15  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   69 LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL-QLQALEQEHKKLAARLEEERG 147
Cdd:pfam05622  249 LQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLtELQQLLEDANRRKNELETQNR 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  148 KNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA---KLEEEKKKTNELEEELSAEKRRSTEMEAqmeKQLSEFDTEREQLR 224
Cdd:pfam05622  329 LANQRILELQQQVEELQKALQEQGSKAEDSSLlkqKLEEHLEKLHEAQSELQKKKEQIEELEP---KQDSNLAQKIDELQ 405

                          170       180
                   ....*....|....*....|....*....
gi 2462616488  225 AKLNREEahttdlkeeiDKMRKMIEQLKR 253
Cdd:pfam05622  406 EALRKKD----------EDMKAMEERYKK 424
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
172-272 4.95e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.21  E-value: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  172 QKLEDVMAKLEEEKKKTNELEEELS--AEKRRS-----TEMEAQMEKQLSEFDTEREQLR-AKLNREEahttdLKEEIDK 243
Cdd:COG1340     15 EKIEELREEIEELKEKRDELNEELKelAEKRDElnaqvKELREEAQELREKRDELNEKVKeLKEERDE-----LNEKLNE 89

                           90       100
                   ....*....|....*....|....*....
gi 2462616488  244 MRKMIEQLKRGSDSKPSLSLPRKTKDRRL 272
Cdd:COG1340     90 LREELDELRKELAELNKAGGSIDKLRKEI 118
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 97-251 5.01e-05

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: 45.09  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   97 MAHCKKMqerMSAQLAAA-ESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkqvvlmLVKECKQLSGKVIEEAqkle 175
Cdd:TIGR01144    9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENA---- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  176 dvmakleeeKKKTNELEEELSAEKRrsTEMEAQMEKQLSEFDTEREQLRAKLNREeahTTDL---------KEEIDKM-- 244
Cdd:TIGR01144   71 ---------NKRGSEILEEAKAEAR--EEREKIKAQARAEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKQaq 136


                   ....*..
gi 2462616488  245 RKMIEQL 251
Cdd:TIGR01144  137 KDLIDKL 143
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 769-848 5.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  769 QGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 848
Cdd:PHA02876   155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 104-246 5.08e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.43  E-value: 5.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQ-------EHKKLAARLEEErgknkQVVLMLVKEC-KQLSGKVIEEAQKLE 175
Cdd:TIGR00618  151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQlalmefaKKKSLHGKAELL-----TLRSQLLTLCtPCMPDTYHERKQVLE 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  176 DVMAKLEEEKKKTNELEEELSaEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRK 246
Cdd:TIGR00618  226 KELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARK 291
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 110-257 5.18e-05

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: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 46.21  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  110 QLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEergknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTN 189
Cdd:pfam04012   44 ALAQTIARQKQLERR------LEQQ-TEQAKKLEE------KAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQR 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  190 EleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNreeahTTDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:pfam04012  111 S--------------AVEQLRKQLAALETKIQQLKAKKN-----LLKARLKAAKAQEAVQTSLGSLST 159
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 22-251 5.37e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI-LEAVMAHC 100
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQISELQEDLESERAARNKAEKQRRDLGEeLEALKTEL 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQlaaAESRQKKlEMEKLQLQ-ALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviEEAQKLEDVMA 179
Cdd:pfam01576  309 EDTLDTTAAQ---QELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQ 380

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  180 KLEEEkkkTNELEEELSAEKRRSTEMEAQMEKQlsefDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:pfam01576  381 ALESE---NAELQAELRTLQQAKQDSEHKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 2-258 5.42e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 48.03  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    2 DGSPGFLKKKEFDVDTL-----SKSELRMLLSVMEGEleaRDLVIEALRarrkevfIQERYGRFNLNDPFLALQRDYEAG 76
Cdd:COG5185     93 KLDTKILQEYVNSLIKLpnyewSADILISLLYLYKSE---IVALKDELI-------KVEKLDEIADIEASYGEVETGIIK 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   77 AGDKEKKPVCTNPLSILEAVMAHCKKMQErmsaqlaaaESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVlm 155
Cdd:COG5185    163 DIFGKLTQELNQNLKKLEIFGLTLGLLKG---------ISELKKAEPSGTVnSIKESETGNLGSESTLLEKAKEIINI-- 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  156 lvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRA--KLNREEA 232
Cdd:COG5185    232 --EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAeSSKRLNENANNLIKQFENTKEKIAEytKSIDIKK 309

                          250       260
                   ....*....|....*....|....*...
gi 2462616488  233 HTTDLKEEIDKMR--KMIEQLKRGSDSK 258
Cdd:COG5185    310 ATESLEEQLAAAEaeQELEESKRETETG 337
Ank_5 pfam13857
Ankyrin repeats (many copies);
750-799 5.80e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 5.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462616488  750 AQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA 799
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 111-258 6.41e-05

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: 45.90  E-value: 6.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  111 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 177
Cdd:cd00176     32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 243
Cdd:cd00176    112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190

                          170
                   ....*....|....*
gi 2462616488  244 MRKMIEQLKRGSDSK 258
Cdd:cd00176    191 LNERWEELLELAEER 205
PTZ00121 PTZ00121
MAEBL; Provisional
 101-271 6.49e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKlEMEKLQLQAlEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVM-- 178
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAK-KADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKka 1524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  179 --AKLEEEKKKTNEL---EEELSAEK-RRSTEMEAQMEKQLSEFDTEREQLRAKLNR--------EEAHTTDLKEEIDKM 244
Cdd:PTZ00121  1525 deAKKAEEAKKADEAkkaEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkaEEARIEEVMKLYEEE 1604

                          170       180
                   ....*....|....*....|....*...
gi 2462616488  245 RKM-IEQLKRGSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121  1605 KKMkAEEAKKAEEAKIKAEELKKAEEEK 1632
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
112-251 6.93e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 6.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  112 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNEL 191
Cdd:PRK02224   469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERREDLEEL 524

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  192 EEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN---------REEAHT-----TDLKEEIDKMRKMIEQL 251
Cdd:PRK02224   525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeeeaeeaREEVAElnsklAELKERIESLERIRTLL 598
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 296-433 7.69e-05

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 46.87  E-value: 7.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  296 ENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIgasVPAFPPPSANKIE--ENGPSTGST 373
Cdd:PHA03291   151 EGATNASLFPLGLAAFPAEGTLAAPPLGEGSADGSCDPALPLSAPRLGPADVF---VPATPRPTPRTTAspETTPTPSTT 227

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  374 PDPTSSTPPLPS-NAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSlhpglnPRIQAARFR 433
Cdd:PHA03291   228 TSPPSTTIPAPStTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANAT------PAPEASRYE 282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-251 7.79e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 7.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196    664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  184 EKKKTNELEEE-------LSAEKRRSTEMEAQMEK-------QLSEFDTEREQLRAkLNREEAhttDLKEEIDKMRKMIE 249
Cdd:COG1196    744 EEELLEEEALEelpeppdLEELERELERLEREIEAlgpvnllAIEEYEELEERYDF-LSEQRE---DLEEARETLEEAIE 819


                   ..
gi 2462616488  250 QL 251
Cdd:COG1196    820 EI 821
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 149-250 8.09e-05

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: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 8.09e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   149 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 224
Cdd:smart00935    5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82

                            90       100
                    ....*....|....*....|....*.
gi 2462616488   225 AKLNREEAhttdlkEEIDKMRKMIEQ 250
Cdd:smart00935   83 QDLQKRQQ------EELQKILDKINK 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-208 8.44e-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: 47.37  E-value: 8.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    8 LKKKEFDVDTLSKS--ELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRfnLNDPFLALQRDYEagaGDKEKKpv 85
Cdd:TIGR02169  331 IDKLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAELEEV--DKEFAE--TRDELKDYREKLE---KLKREI-- 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   86 ctNPLsileavmahcKKMQERMSAQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkqvvlmlvKECKQLSG 165
Cdd:TIGR02169  402 --NEL----------KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEW 455

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462616488  166 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQ 208
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 22-252 8.45e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.20  E-value: 8.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGAGDKEKKPVCTNPLSilEAV 96
Cdd:pfam07888    5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDR--EQW 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   97 MAHCKKMQERMS-AQLAAAESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:pfam07888   72 ERQRRELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  174 LEDV---------MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:pfam07888  152 LERMkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNsLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231


                   ....*....
gi 2462616488  244 MRKMIEQLK 252
Cdd:pfam07888  232 NEALLEELR 240
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 104-207 8.66e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 47.25  E-value: 8.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGkvIEEAQKLEDVMAKLEE 183
Cdd:pfam15709  409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME--MAEEERLEYQRQKQEA 486

                           90       100
                   ....*....|....*....|....
gi 2462616488  184 EKKKtneleeELSAEKRRSTEMEA 207
Cdd:pfam15709  487 EEKA------RLEAEERRQKEEEA 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
103-253 8.96e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 8.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  103 MQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLE 182
Cdd:COG3206    162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  183 EEKKKTNELEEELSAEKRRSTEMEA-----QMEKQLSEFDTEREQLRAKLNreEAHTT--DLKEEIDKMRKMIEQLKR 253
Cdd:COG3206    237 EAEARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYT--PNHPDviALRAQIAALRAQLQQEAQ 312
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 118-252 9.44e-05

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 45.44  E-value: 9.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIEEAqklEDVMAKLEEEKKKTNELEE 193
Cdd:pfam05010    3 QKDMDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEKQKQKELEH 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  194 elsaekrrstemeAQMEKQLSEfdteREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:pfam05010   68 -------------AEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 93-208 9.76e-05

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 44.23  E-value: 9.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAES-RQKKLEMEKLQLQALE-QEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEE 170
Cdd:TIGR02473   22 LAKAQAEFERLETQLQQLIKYREEyEQQALEKVGAGTSALElSNYQRFIRQLDQRIQQQQQELALLQQEVEAKRERLLEA 101

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462616488  171 AQKLEdVMAKLEEeKKKTNELEEELSAEKRRSTEMEAQ 208
Cdd:TIGR02473  102 RRELK-ALEKLKE-KKQKEYRAEEAKREQKEMDELATQ 137
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 81-248 1.02e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.09  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   81 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEklqLQALEQ--EHKKLAA-RLEEERGKNKQV---VL 154
Cdd:pfam01576  510 EAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQqlEEKAAAYdKLEKTKNRLQQElddLL 586

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  155 MLVKECKQLSGKvIEEAQKLEDVMakLEEEKKKTNELeeelsAEKRRSTEMEAQmekqlsefdtEREQLRAKLNREEAHT 234
Cdd:pfam01576  587 VDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARY-----AEERDRAEAEAR----------EKETRALSLARALEEA 648

                          170
                   ....*....|....
gi 2462616488  235 TDLKEEIDKMRKMI 248
Cdd:pfam01576  649 LEAKEELERTNKQL 662
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 725-757 1.03e-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: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 1.03e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2462616488  725 DGHSALYSAA-KNGHTDCVRLLLSAEAQVNAADK 757
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
LUC7 pfam03194
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
 114-256 1.19e-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: 460842 [Multi-domain]  Cd Length: 246  Bit Score: 45.67  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  114 AESRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKnkqvvlmlvkeckqlsgkvIEEAQKLedvMAKLEEEKKKTNEL 191
Cdd:pfam03194  111 QEEIEQTDELKQEQISVLEEKIKKLLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEEL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  192 EEEL-SAEKRRSTEMEAQME------KQLSEFDTERE--------------QLRAKLNReeahttdLKEEIDKmRKMIEQ 250
Cdd:pfam03194  169 EQQYeSLTKESAASQEKKMEvcevcgAFLIVNDADRRladhltgkqhlgyaKIRDTLEE-------LKEKIEE-RREERE 240


                   ....*.
gi 2462616488  251 LKRGSD 256
Cdd:pfam03194  241 ERREKR 246
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 91-232 1.19e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   91 SILEAVMA-------HCKKMQERMSAQLAAAESRQKKLEM---EKLQLQALEQEHKKlaaRLEEERGKNKQVVLMLVKEC 160
Cdd:PRK09510    48 SVIDAVMVdpgavveQYNRQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAA 124

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  161 KQ--LSGKVIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNREEA 232
Cdd:PRK09510   125 KQaaLKQKQAEEAAAkaAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
PHA02946 PHA02946
ankyin-like protein; Provisional
 695-837 1.22e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  695 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFT 761
Cdd:PHA02946    28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  762 PL--CAAAAQGHFECVELLISYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGN 837
Cdd:PHA02946   108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 27-250 1.25e-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: 46.74  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   27 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGAGD-KE----------K 82
Cdd:pfam10174  438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   83 KPVCTNPLSI-LEAVMAHCKKMQERMSAQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKQVV---LMLVK 158
Cdd:pfam10174  515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVerlLGILR 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  159 EC---KQLSGKVIEEAQKLEDVMAKLE------------EEKKKTNELEEElsAEKRRSTEMEAQMEKQLSEFDTEREQL 223
Cdd:pfam10174  590 EVeneKNDKDKKIAELESLTLRQMKEQnkkvanikhgqqEMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALEKT 667

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2462616488  224 RAKLN--------------REEAHTTDLKEEidkMRKMIEQ 250
Cdd:pfam10174  668 RQELDatkarlsstqqslaEKDGHLTNLRAE---RRKQLEE 705
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 247-626 1.30e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  247 MIEQLKRGSDSKPSlslPRKTKDRRLVSISVGTEGTVTRSVACQTDlVTENADHMKKLPLTMPVKPSTGSP-LVSANAK- 324
Cdd:PHA03307    10 LIEAAAEGGEFFPR---PPATPGDAADDLLSGSQGQLVSDSAELAA-VTVVAGAAACDRFEPPTGPPPGPGtEAPANESr 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  325 ------GSVCTSATMARPGIDRQASYGDLIG---ASVPAFPPPSANKI---------EENGPSTGSTPDPTSSTPPLPSN 386
Cdd:PHA03307    86 stptwsLSTLAPASPAREGSPTPPGPSSPDPpppTPPPASPPPSPAPDlsemlrpvgSPGPPPAASPPAAGASPAAVASD 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  387 AA--------------------PPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPG-LNPRIQAARFRF--------QGN 437
Cdd:PHA03307   166 AAssrqaalplsspeetarapsSPPAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGAsssdssssESS 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  438 ANDPDQNGNTTQSPPSRDVSPTSRDNLVAkqlARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSLKTHGVA 517
Cdd:PHA03307   246 GCGWGPENECPLPRPAPITLPTRIWEASG---WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  518 RVDRGNPPPIPPKKPGLSQTPSPPH--------PQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR-VINEENLPKS 588
Cdd:PHA03307   323 ESSSSSTSSSSESSRGAAVSPGPSPsrspspsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaAVAGRARRRD 402

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2462616488  589 SSPQLP-----PKPSIDLTVAPAGCAVSALATSQVGAWPAATP 626
Cdd:PHA03307   403 ATGRFPagrprPSPLDAGAASGAFYARYPLLTPSGEPWPGSPP 445
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 152-253 1.39e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  152 VVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLN 228
Cdd:COG4942      7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELA 86

                           90       100
                   ....*....|....*....|....*
gi 2462616488  229 REEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4942     87 ELEKEIAELRAELEAQKEELAELLR 111
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 118-229 1.54e-04

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 42.94  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEE-AQKLEDVMAKLEEEKKKTNELEEE 194
Cdd:pfam13863    3 EKKREMFLVQlaLDAKREEIERLEELLKQREEELEKKEQEL-KEDLIKFDKFLKEnDAKRRRALKKAEEETKLKKEKEKE 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462616488  195 LsaekrrstemeAQMEKQLSEFDTEREQLRAKLNR 229
Cdd:pfam13863   82 I-----------KKLTAQIEELKSEISKLEEKLEE 105
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 169-252 1.73e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.98  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  169 EEAQK----LEDVMAKLEEEKKKTNEleeelsaEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEidKM 244
Cdd:pfam20492    2 EEAERekqeLEERLKQYEEETKKAQE-------ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES--AE 72


                   ....*...
gi 2462616488  245 RKMIEQLK 252
Cdd:pfam20492   73 MEAEEKEQ 80
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 111-276 1.77e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  111 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE 190
Cdd:COG4942     12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  191 LEEELSAEKRRSTEMEAQMEKQL----------------------------------SEFDTER-EQLRAKLNREEAHTT 235
Cdd:COG4942     88 LEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylAPARREQaEELRADLAELAALRA 167

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462616488  236 DLKEEIDKMRKMIEQLKRgsdSKPSLSLPRKTKDRRLVSIS 276
Cdd:COG4942    168 ELEAERAELEALLAELEE---ERAALEALKAERQKLLARLE 205
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 118-253 1.88e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.51  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEMEKLQLQALEQEHKKLAARLEEErgkNKQvvlmLVKECKQLSGKVIEEAQKLE----DVMAkLEEEKKKTNELEE 193
Cdd:pfam13851   28 IKSLKEEIAELKKKEERNEKLMSEIQQE---NKR----LTEPLQKAQEEVEELRKQLEnyekDKQS-LKNLKARLKVLEK 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  194 ELSAEKRRSTEMEAQMEKqLSEfdtEREQLRAKLNR--EEAHT-TDLKEEI--DKMRKMIEQLKR 253
Cdd:pfam13851  100 ELKDLKWEHEVLEQRFEK-VER---ERDELYDKFEAaiQDVQQkTGLKNLLleKKLQALGETLEK 160
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 108-253 1.89e-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: 46.50  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  108 SAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKledVMAKLEEEKKK 187
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEEEK---EKKLQEEELKL 290

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  188 TNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 699-823 2.33e-04

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: 45.84  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  699 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLSAEAQVNAADKngftpLCAAAAQGHFEC 774
Cdd:TIGR00870   24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  775 VELLISY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTT 823
Cdd:TIGR00870   97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAC 159
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 9-230 2.76e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.72  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    9 KKKEFDvdtlskSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfnlndpflalQRDYEAGAgDKEKKPVCTN 88
Cdd:COG5185    330 SKRETE------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-------------LSKSSEEL-DSFKDTIEST 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   89 PLSILEAVMAHCKKMQErmsaqLAAAESRQKKlemeklqlqALEQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVI 168
Cdd:COG5185    390 KESLDEIPQNQRGYAQE-----ILATLEDTLK---------AADRQIEELQRQIEQATSSNEEV------------SKLL 443

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  169 EEAQK-LEDVMAKLEEEKK-----KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE 230
Cdd:COG5185    444 NELISeLNKVMREADEESQsrleeAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 117-232 2.79e-04

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 42.69  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  117 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE----KKKTNELE 192
Cdd:TIGR02473   11 REKEEEQAKLELAKAQAEFERLETQLQQLIKYREE--YEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqQQELALLQ 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462616488  193 EELsaEKRRSTEMEAQMEKQLseFDTEREQLRAKLNREEA 232
Cdd:TIGR02473   89 QEV--EAKRERLLEARRELKA--LEKLKEKKQKEYRAEEA 124
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 763-845 2.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  763 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 842
Cdd:PHA02875     6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85


                   ...
gi 2462616488  843 LLM 845
Cdd:PHA02875    86 ELL 88
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
116-263 2.92e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  116 SRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKQVVLMLVKECKQLS------GKVIEEAQKLEDVMAKLEEEKKK 187
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  188 TNELEEELsaekrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSL 263
Cdd:COG4913    687 LAALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
101-263 2.98e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVlmlvkecKQLSGKVIEEAQKLEDV 177
Cdd:COG4372     83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQI-------AELQSEIAEREEELKEL 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAKLEEEKKKTNELEEELSAEKRRSTemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:COG4372    156 EEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233


                   ....*.
gi 2462616488  258 KPSLSL 263
Cdd:COG4372    234 ALSALL 239
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-272 3.13e-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: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  123 MEKLQLQA-LEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEaqkLEDVMAKLEEEKKKTNELEEELSAEKRR 201
Cdd:TIGR02168  202 LKSLERQAeKAERYKELKAELRELE--------------LALLVLRLEE---LREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  202 StemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI----EQLKRGSDSKPSLSLPRKTKDRRL 272
Cdd:TIGR02168  265 L-------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
109-246 3.23e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.42  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkvIEEAQKLEDVMA----KLEEE 184
Cdd:COG3064      6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK---AEAEQRAAELAAeaakKLAEA 82

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  185 KKKTNELEEELSAEKRRStemEAQMEKQLSEfdtEREQLRAklnrEEAHTTDLKEEIDKMRK 246
Cdd:COG3064     83 EKAAAEAEKKAAAEKAKA---AKEAEAAAAA---EKAAAAA----EKEKAEEAKRKAEEEAK 134
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 76-232 3.26e-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: 44.84  E-value: 3.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   76 GAGDKEKKPVCTNPLSILEAVMAHCKKMQERMsAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLM 155
Cdd:TIGR02794   21 GSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQA-NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  156 LVKECKQlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:TIGR02794  100 AEKAAKQ-----AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA 171
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 149-250 3.26e-04

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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.56  E-value: 3.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  149 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKL 227
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKElQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85

                           90       100
                   ....*....|....*....|....
gi 2462616488  228 NREEAhttDLKEEI-DKMRKMIEQ 250
Cdd:pfam03938   86 QKKQQ---ELLQPIqDKINKAIKE 106
mukB PRK04863
chromosome partition protein MukB;
35-257 3.30e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   35 EARDLVIEALRARRkevFIQERYGRFNLNDPFLA-----------LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCK-- 101
Cdd:PRK04863   898 EIREQLDEAEEAKR---FVQQHGNALAQLEPIVSvlqsdpeqfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSye 974

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  102 KMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergkNKQVVLMLVKECKQLSGKVIEEAQKLED--VMA 179
Cdd:PRK04863   975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ----YNQVLASLKSSYDAKRQMLQELKQELQDlgVPA 1050

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  180 KLEEEKKkTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEahttdlkEEIDKMRKMIEQLKRGSDS 257
Cdd:PRK04863  1051 DSGAEER-ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE-------RDYHEMREQVVNAKAGWCA 1120
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 104-228 3.71e-04

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: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 42.24  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLeMEKLQLQAleqehkKLAARLEE--ERgknkQVVlmlvkeckqlsgKVIEEAQKLEDVMAKL 181
Cdd:pfam07926   10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyER----ELV------------LHAEDIKALQALREEL 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462616488  182 EEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 228
Cdd:pfam07926   67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIE 113
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 792-822 3.78e-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: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 3.78e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462616488  792 GQTPLYLAC-KNGNKECIKLLLEAGTNRSVKT 822
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 107-253 3.85e-04

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: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 43.35  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  107 MSAQLAA--AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKEcKQLSGKviEEAQ-KLEDVMAKL 181
Cdd:pfam15619   58 LPQLIARhnEEVRvlRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLE-KLSED-KNLAER--EELQkKLEQLEAKL 133

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  182 EEEKKKTNELEEELS-AEKRRSTEMEAQMEKQLsefdtereQLRAKLNreeahttDLKEEIDKMRKMIEQLKR 253
Cdd:pfam15619  134 EDKDEKIQDLERKLElENKSFRRQLAAEKKKHK--------EAQEEVK-------ILQEEIERLQQKLKEKER 191
MFAP1 pfam06991
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ...
 169-270 3.88e-04

Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with microfibrils which are an important component of the extracellular matrix (ECM) of many tissues. For example, MFAP1 has been shown to be associated with elastin-like fibres at the base of Schlemm's canal endothelium cells, in the juxtacanalicular tissue, and in the uveal region. Based on its role in the ECM and the proximity of the MFAP1 gene to FBN1 it was hypothesized that mutations in MFAP1 contributed to heritable diseases affecting microfibrils, Marfan syndrome but this has now been shown not to be the case. MFAP1 has also been shown to interact directly with certain pre-mRNA processing factor proteins, Prps, which are also spliceosome components and is thus required for pre-mRNA processing. MAFP1 bound to Pr38 of yeast is necessary for cells in vivo to progress from G2 to M phase.


Pssm-ID: 462060 [Multi-domain]  Cd Length: 215  Bit Score: 43.70  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  169 EEAQKLEDVMAKLEEEKKKTNEL-EEELsaeKRRSTEMEAQMEKQ-LSEFDTE--------------REQLRAKLNREEA 232
Cdd:pfam06991   34 EEEEEEEEAKKEAEERKKEADKLvEEEI---RREAAAKEAGDEDEnEEDVDDTdgldpeaeyeawklRELKRIKRDREER 110

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462616488  233 HTTD-LKEEIDKMRKMIEQLKRGSDSKpslsLPRKTKDR 270
Cdd:pfam06991  111 EAREkEREEIERRRNMTEEERLAEDRE----NPKKQREK 145
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 151-246 3.92e-04

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: 42.75  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  151 QVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTE---MEAQMEKQLSEfdTEREQLRAKL 227
Cdd:pfam11600    1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEearRKKEEEKELKE--KERREKKEKD 78

                           90
                   ....*....|....*....
gi 2462616488  228 NREEAHTTDLKEEIDKMRK 246
Cdd:pfam11600   79 EKEKAEKLRLKEEKRKEKQ 97
Ank_4 pfam13637
Ankyrin repeats (many copies);
825-914 4.01e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  825 GWTPVHAAVDTGNVDSLKLLMYHRIPahgnsfneeesessvfdldggeespegiskpvvpadlINHANREGWTAAHIAAS 904
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD-------------------------------------INAVDGNGETALHFAAS 43

                           90
                   ....*....|
gi 2462616488  905 KGFKNCLEIL 914
Cdd:pfam13637   44 NGNVEVLKLL 53
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 109-228 4.07e-04

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 41.44  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkqvvLMLVKE---CKQLSGKVIEEaQKLEDVMAKLEEEK 185
Cdd:pfam01920    2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERK 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2462616488  186 KKtneLEEELSAekrrstemeaqMEKQLSEFDTEREQLRAKLN 228
Cdd:pfam01920   69 ET---LEKEIKT-----------LEKQLEKLEKELEELKEELY 97
PRK11637 PRK11637
AmiB activator; Provisional
 101-260 4.16e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.68  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERM-SAQLAAAeSRQKKLEMEKLQLQALE-QEHKKLAAR---LEEERGKNkqvvlmlVKECKQLSGKVIEEAQKLE 175
Cdd:PRK11637   119 QAAQERLlAAQLDAA-FRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELE 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  176 DVMAK----LEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKE----EIDKM 244
Cdd:PRK11637   191 EKQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAEREAKARAErearEAARV 270

                          170
                   ....*....|....*..
gi 2462616488  245 RKMIEQLKR-GSDSKPS 260
Cdd:PRK11637   271 RDKQKQAKRkGSTYKPT 287
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 139-269 4.18e-04

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: 42.48  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  139 AARLEE-ERGKNKQVvlmlvkECKQLSGKVIEEAQKLEdvmaKLEEEKKKTNELEEELsaEKRRSTEMeaqMEKQLsefd 217
Cdd:pfam15236   41 PAQLEErERKRQKAL------EHQNAIKKQLEEKERQK----KLEEERRRQEEQEEEE--RLRREREE---EQKQF---- 101

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  218 tEREQLRAKlNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 269
Cdd:pfam15236  102 -EEERRKQK-EKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIRELAEKGHD 151
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
305-497 4.22e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  305 PLTMPVKP-STGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPS----ANKIEENGPSTGSTPDPTSS 379
Cdd:PRK12323   374 PATAAAAPvAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealAAARQASARGPGGAPAPAPA 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  380 TPPLPSNAAPPTAQTPGIAPQNSQAPPmhSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGnttqsPPSRDVSPT 459
Cdd:PRK12323   454 PAAAPAAAARPAAAGPRPVAAAAAAAP--ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA-----PAGWVAESI 526

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462616488  460 SRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPT 497
Cdd:PRK12323   527 PDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPR 564
growth_prot_Scy NF041483
polarized growth protein Scy;
94-252 4.28e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.20  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   94 EAVMAHCKkmqERMSAQLAAAES------RQKKLEMEKL------QLQALEQEHKKLA--ARLEEERgknkqvvlmLVKE 159
Cdd:NF041483   282 EKVVAEAK---EAAAKQLASAESaneqrtRTAKEEIARLvgeatkEAEALKAEAEQALadARAEAEK---------LVAE 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  160 CKQLSGKVIEE---------AQKLEDVMAKLEEEKKKTNELEEElSAEKRRsTEMEAQMEKQLSEFDTEREQLR--AKLN 228
Cdd:NF041483   350 AAEKARTVAAEdtaaqlakaARTAEEVLTKASEDAKATTRAAAE-EAERIR-REAEAEADRLRGEAADQAEQLKgaAKDD 427

                          170       180
                   ....*....|....*....|....*.
gi 2462616488  229 REE--AHTTDLKEEIDKMRKMIEQLK 252
Cdd:NF041483   428 TKEyrAKTVELQEEARRLRGEAEQLR 453
PRK00106 PRK00106
ribonuclease Y;
122-253 4.48e-04

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 44.86  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  122 EMEKLQLQALEQEHKKLaarleeeRGKNKQVVLMLVKECKQLSgkvieEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 201
Cdd:PRK00106    31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  202 STEMEAQMEKQLSEFDTEREQLRAK---LNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:PRK00106    99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
103-229 4.88e-04

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


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 41.41  E-value: 4.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  103 MQERMSAQLaaaesrQKKLEmeklQLQALEQEHKKLAARleeergknKQVVLMLVKECKqlsgKVIEEAQKLED------ 176
Cdd:COG1382      1 MMQNLPPEV------QNQLA----QLQQLQQQLQAVAAQ--------KQQVESELKEAE----KALEELEKLPDdaevyk 58

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  177 ----VMAKLEEEKKKtNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR 229
Cdd:COG1382     59 svgnLLVKTDKEEVI-KELEEKKETLELRLKTLEKQEERLQKQLEELQEKLQEALSG 114
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 117-229 4.99e-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: 44.11  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  117 RQKKLEMEKLQLQALEQEhkklAARLEEERGKNKQVvlmlvkeckqlsgkvIEEAQK-----LEDVMAKLEEEKKKTNEL 191
Cdd:cd16269    196 KEKEIEAERAKAEAAEQE----RKLLEEQQRELEQK---------------LEDQERsyeehLRQLKEKMEEERENLLKE 256

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462616488  192 EEELSAEKRRstEMEAQMEKqlsEFDTEREQLRAKLNR 229
Cdd:cd16269    257 QERALESKLK--EQEALLEE---GFKEQAELLQEEIRS 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-230 5.01e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196    685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  184 EKKKTNELE--------------EELSAEKRRSTEMEAQMEKqLSEfdtEREQLR---AKLNRE 230
Cdd:COG1196    765 LERELERLEreiealgpvnllaiEEYEELEERYDFLSEQRED-LEE---ARETLEeaiEEIDRE 824
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 18-252 5.03e-04

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: 45.04  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   18 LSKSElRMLLSVMEGELEARDL-----VIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSI 92
Cdd:TIGR00606  767 IEEQE-TLLGTIMPEEESAKVCltdvtIMERFQMELKDV--ERKIAQQAAKLQGSDLDRTVQQVNQEKQEK---QHELDT 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergKNKQVvLMLVKECKQLSGKVIEEAQ 172
Cdd:TIGR00606  841 VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE---LSTEV-QSLIREIKDAKEQDSPLET 916

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 KLED-------VMAKLEEEKK----KTNELEEELSAE--KRRSTEMEAQ--MEKQLSEFDTEREQLRAKLNREEAHTTDL 237
Cdd:TIGR00606  917 FLEKdqqekeeLISSKETSNKkaqdKVNDIKEKVKNIhgYMKDIENKIQdgKDDYLKQKETELNTVNAQLEECEKHQEKI 996

                          250
                   ....*....|....*
gi 2462616488  238 KEEIDKMRKMIEQLK 252
Cdd:TIGR00606  997 NEDMRLMRQDIDTQK 1011
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
98-281 5.05e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   98 AHCKKMQERMSAQLAAAESRQKKLEmeklqlqaLEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL--- 174
Cdd:COG3064     39 AEEERLAELEAKRQAEEEAREAKAE--------AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAaaa 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 --EDVMAKLE--EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:COG3064    111 ekAAAAAEKEkaEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462616488  251 LKRGSDSKPSLSLPRKTKDRRLVSISVGTEG 281
Cdd:COG3064    191 EAADTAAAAAAALAAAAAAAAADAALLALAV 221
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 105-244 5.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 184
Cdd:COG1196    654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  185 KKKTNELEEELSAEkrrstEMEAQMEKQLSEFDteREQLRAKLNReeahttdLKEEIDKM 244
Cdd:COG1196    734 REELLEELLEEEEL-----LEEEALEELPEPPD--LEELERELER-------LEREIEAL 779
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 312-693 5.24e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  312 PSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPT 391
Cdd:PHA03307    49 ELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPP 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  392 AQTPGIAPqnsQAPPMHSLHSPCANTSLHPGLNPRIQAArfrfqgNANDPDQNGNTTQSPPS--RDVSPTSRDNLVAKQL 469
Cdd:PHA03307   129 SPAPDLSE---MLRPVGSPGPPPAASPPAAGASPAAVAS------DAASSRQAALPLSSPEEtaRAPSSPPAEPPPSTPP 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  470 ARntvtqalsrfTSPQAGAPSRPGVPPTGDVGTHPpvGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQlkviI 549
Cdd:PHA03307   200 AA----------ASPRPPRRSSPISASASSPAPAP--GRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP----I 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  550 DSSRASNTGAKVDNKTVASTPSSLPQGNRVINEENLP-KSSSPQLPPKPSIDLTVAPAGCAVSA--LATSQVGAWPAATP 626
Cdd:PHA03307   264 TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPsSPGSGPAPSSPRASSSSSSSRESSSSstSSSSESSRGAAVSP 343

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462616488  627 GlnQPACSDSSLVIPTTIAFCSS----INPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRP 693
Cdd:PHA03307   344 G--PSPSRSPSPSRPPPPADPSSprkrPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
Rootletin pfam15035
Ciliary rootlet component, centrosome cohesion;
114-252 5.78e-04

Ciliary rootlet component, centrosome cohesion;


Pssm-ID: 464459 [Multi-domain]  Cd Length: 190  Bit Score: 42.72  E-value: 5.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  114 AESRQKKLeMEKLQLQALEQ-------EHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEaqkLEDVMAKLEEEKK 186
Cdd:pfam15035   10 AQQRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHSAD---LEEALIRLEEERQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  187 KTNEL-----------EEELSAEKRRSTEMEA----------QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:pfam15035   86 RSESLsqvnsllreqlEQASRANEALREDLQKltndwerareELEQKESEWRKEEEAFNEYLSSEHSRLLSLWREVVAVR 165


                   ....*..
gi 2462616488  246 KMIEQLK 252
Cdd:pfam15035  166 RQFTELK 172
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
305-499 6.08e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 6.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  305 PLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPDPTSSTPPLP 384
Cdd:PRK12323   402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA-------PAAAARPAAAGPRPVAA 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  385 SNAAPPTAQTPGI--APQNSQAPPMHSLHSPCANTSLHPglnpriQAARFRFQGNANDPDQngNTTQSPPSRdvsPTSRD 462
Cdd:PRK12323   475 AAAAAPARAAPAAapAPADDDPPPWEELPPEFASPAPAQ------PDAAPAGWVAESIPDP--ATADPDDAF---ETLAP 543

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462616488  463 NLVAKQLARntVTQALSRFTSPQAGAPSRPGVPPTGD 499
Cdd:PRK12323   544 APAAAPAPR--AAAATEPVVAPRPPRASASGLPDMFD 578
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 109-198 6.24e-04

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 41.23  E-value: 6.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECKQLSGKVIEEAQK-------LEDVM 178
Cdd:pfam04871    1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELeaeVKKLEEALKKLKAELSEEKQKekekqseLDDLL 80

                           90       100
                   ....*....|....*....|....*..
gi 2462616488  179 -------AKLEEEKKKTNELEEELSAE 198
Cdd:pfam04871   81 lllgdleEKVEKYKARLKELGEEVLSD 107
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 105-245 6.71e-04

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 44.51  E-value: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 184
Cdd:pfam15964  548 NEAKAQALQAQQREQELTQ---KMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQE 624

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  185 KKKTNELEEELsaeKRRSTEMEAQ----------MEKQLSEFD----TEREQLRAKLNREEA---HTTDLKEEIDKMR 245
Cdd:pfam15964  625 KEYLQDRLEKL---QKRNEELEEQcvqhgrmherMKQRLRQLDkhcqATAQQLVQLLSKQNQlfkERQNLTEEVQSLR 699
PHA02795 PHA02795
ankyrin-like protein; Provisional
 772-838 7.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 44.22  E-value: 7.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  772 FECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNV 838
Cdd:PHA02795   201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 22-253 7.24e-04

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: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.35  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARDlviEALRARRKEVFIQERYgrfnlNDPFLALQRDYEAGAGD-KEKKPVCTNPLSILeAVMAHC 100
Cdd:pfam05557   52 ELQKRIRLLEKREAEAE---EALREQAELNRLKKKY-----LEALNKKLNEKESQLADaREVISCLKNELSEL-RRQIQR 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQerMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK------- 173
Cdd:pfam05557  123 AELE--LQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKselarip 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  174 -LEDVMAKLEEEKKKTNE-------LEEELSAEKRRSTEMEAQMEKqLSEFDTEREQLRAKLNR----EEAHTTDLKEEI 241
Cdd:pfam05557  201 eLEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQELQSwvklAQDTGLNLRSPE 279

                          250
                   ....*....|..
gi 2462616488  242 DKMRKMIEQLKR 253
Cdd:pfam05557  280 DLSRRIEQLQQR 291
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 725-754 7.41e-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: 7.41e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2462616488   725 DGHSALYSAAKNGHTDCVRLLLSAEAQVNA 754
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 107-233 7.50e-04

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 44.07  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  107 MSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkeckqlSGKVIEEAQ-KLEDVMAKLEEEK 185
Cdd:pfam05917  115 LAACSAGDTDEQIELEQEKKEAENAEDRANKNGIELEQEKQKTNK------------SGIELANNQiKAEQEQQKTEQEK 182

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462616488  186 KKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQlraklNREEAH 233
Cdd:pfam05917  183 QKAEKEAIELEQEKQKTIKTQRDLIKEQKDFIKETEQ-----NCQENH 225
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 257-508 7.54e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 7.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  257 SKPSLSLPRKTKDRRLVSISVGTEgtvTRSVACQTDLVTENADHMKKlPLTMPVKPSTGSPlvsANAKGSVCTSATMARP 336
Cdd:PHA03307   218 SSPAPAPGRSAADDAGASSSDSSS---SESSGCGWGPENECPLPRPA-PITLPTRIWEASG---WNGPSSRPGPASSSSS 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  337 GIDRQASYGDlIGASVPAFPPPSANKiEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCAN 416
Cdd:PHA03307   291 PRERSPSPSP-SSPGSGPAPSSPRAS-SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKR 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  417 TSLHPGL-NPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTvtqalsrFTSPQAGAPSR---P 492
Cdd:PHA03307   369 PRPSRAPsSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAF-------YARYPLLTPSGepwP 441

                          250
                   ....*....|....*.
gi 2462616488  493 GVPPtgdvgthPPVGR 508
Cdd:PHA03307   442 GSPP-------PPPGR 450
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 699-938 8.01e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  699 AAAQGNVTLLSMLLNeegldINYSCEDGHSALYSAAKNghTDCVRLLLSAEaqVNAADKNGFTPLCAAAAQGHFECVELL 778
Cdd:cd22194     90 ASDTGKTCLMKALLN-----INENTKEIVRILLAFAEE--NGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLL 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  779 ISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAG-TNRSVKTTDGWTPVHAAV----DTGNVD 839
Cdd:cd22194    161 IAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaeDSKTQN 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  840 SLKLLMYHRIPahgnsfneeesessvfdLDGGEESPEGISkpvvpadlinhaNREGWTAAHIAASKGfknCLEILcrHGG 919
Cdd:cd22194    241 DFVKRMYDMIL-----------------LKSENKNLETIR------------NNEGLTPLQLAAKMG---KAEIL--KYI 286

                          250
                   ....*....|....*....
gi 2462616488  920 LEPERRDKCNRTVHDVATD 938
Cdd:cd22194    287 LSREIKEKPNRSLSRKFTD 305
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
127-254 8.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 8.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  127 QLQALEQEHKKLAARLEEERgknkqvvlmLVKECKQLSGKV----IEEAQKLEDVMAKLEEEKKKTNELEEEL-SAEKRR 201
Cdd:COG4717    348 ELQELLREAEELEEELQLEE---------LEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLeELLGEL 418

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  202 STEMEAQMEKQLSEfdtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:COG4717    419 EELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLEED 468
PRK12704 PRK12704
phosphodiesterase; Provisional
 33-210 8.72e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   33 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvctnpLSILEAVMahcKKMQERMSAQLA 112
Cdd:PRK12704    37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  113 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKT--NE 190
Cdd:PRK12704   104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162

                          170       180
                   ....*....|....*....|...
gi 2462616488  191 LEEELSAEKR---RSTEMEAQME 210
Cdd:PRK12704   163 VEEEARHEAAvliKEIEEEAKEE 185
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
124-250 8.89e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  124 EKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSgkvieEAQKLEDVMAKLE-EEKKKTNELEEElsaekRRS 202
Cdd:COG3064      3 EALEEKAAEAAAQERLEQAEAEKRAAAE----AEQKAKEEA-----EEERLAELEAKRQaEEEAREAKAEAE-----QRA 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462616488  203 TEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:COG3064     69 AELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAA 116
PRK00106 PRK00106
ribonuclease Y;
94-248 8.95e-04

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 43.70  E-value: 8.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   94 EAVMAHCKKMQERMSAQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGK 166
Cdd:PRK00106    52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  167 --VIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:PRK00106   124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203


                   ....*
gi 2462616488  244 MRKMI 248
Cdd:PRK00106   204 MAKDL 208
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 94-250 9.12e-04

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: 42.43  E-value: 9.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   94 EAVMAHCKKMQERMSAQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkqvvlmlvKECKQLSGKVIEEAQK 173
Cdd:cd00176     75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER-EQLRAKLNReeahttdLKEEIDKMRKMIEQ 250
Cdd:cd00176    141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 104-194 1.01e-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: 41.32  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAEsRQKKLEMEK------LQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEAQKLEDV 177
Cdd:pfam15236   58 QNAIKKQLEEKE-RQKKLEEERrrqeeqEEEERLRREREEEQKQFEEERRKQKE-----KEEAMTRKTQALLQAMQKAQE 131

                           90
                   ....*....|....*..
gi 2462616488  178 MAKLEEEKKKTNELEEE 194
Cdd:pfam15236  132 LAQRLKQEQRIRELAEK 148
COG5022 COG5022
Myosin heavy chain [General function prediction only];
105-324 1.01e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECkqlsgKVIEEAQKLEDVMAKL 181
Cdd:COG5022    810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAkkrFSLLKKET-----IYLQSAQRVELAERQL 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  182 EEEKK----------KTNELEEELSaEKRRS------------TEMEAQMEKQLSEFDTEREQLR--------AKLNREE 231
Cdd:COG5022    885 QELKIdvksisslklVNLELESEII-ELKKSlssdlienlefkTELIARLKKLLNNIDLEEGPSIeyvklpelNKLHEVE 963

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  232 AHTTDLKEEIDKMRKMIEQLKRgsDSKPSLSLPRKTKdRRLVSISvgtegtvtrsvaCQTDLVTENADHMKKLPLTMPVK 311
Cdd:COG5022    964 SKLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAEL 1028

                          250
                   ....*....|...
gi 2462616488  312 PSTGSPLVSANAK 324
Cdd:COG5022   1029 QSASKIISSESTE 1041
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 730-802 1.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.05  E-value: 1.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  730 LYSAAKNGHtDCVRLLLSAEAQVNA-ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA---CKN 802
Cdd:PHA02884    75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNN 150
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 172-258 1.01e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  172 QKLEDVMAKLEEEKKKTNELEEELSAEKrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRkmiEQL 251
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDEL-------AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQL 82


                   ....*..
gi 2462616488  252 KRGSDSK 258
Cdd:COG1579     83 GNVRNNK 89
PHA03378 PHA03378
EBNA-3B; Provisional
 305-504 1.03e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  305 PLTMPVKPSTGS--PLVSANAKGSVCTSATMARPGIDRQASYGDLIGASvPAFPPPSANKIEE----NGPSTGSTPDPTS 378
Cdd:PHA03378   602 PSQTPEPPTTQShiPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPT-PHQPPQVEITPYKptwtQIGHIPYQPSPTG 680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  379 STPPLPSNAAPPTAQTPGIAPqnSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPdqngntTQSPPSRDVSP 458
Cdd:PHA03378   681 ANTMLPIQWAPGTMQPPPRAP--TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP------GRARPPAAAPG 752

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462616488  459 TSRDNLVAKQLARntvtqalsrftsPQAGAPSRPGVPPTGDVGTHP 504
Cdd:PHA03378   753 RARPPAAAPGRAR------------PPAAAPGAPTPQPPPQAPPAP 786
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 103-253 1.03e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.92  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  103 MQERMSAQLAAAESRQKKLEMEKLQLQAlEQE--HKKLAARLEEERGKNKqvvlmlvkeckqlsgkvieeaQKLEDVMAK 180
Cdd:COG0542    405 EIDSKPEELDELERRLEQLEIEKEALKK-EQDeaSFERLAELRDELAELE---------------------EELEALKAR 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  181 LEEEKKKTNE---LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE-----AHTTD------LKEEIDKMRK 246
Cdd:COG0542    463 WEAEKELIEEiqeLKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvSRWTGipvgklLEGEREKLLN 542


                   ....*..
gi 2462616488  247 MIEQLKR 253
Cdd:COG0542    543 LEEELHE 549
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 117-461 1.04e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.88  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  117 RQKKLEMEKLQLQALEQEHKKLAARLEEE---RGKNKQVvlmLVKECKQLSGKVIEEAQ--KLEDVMAKLEEEKKKTNEL 191
Cdd:PTZ00108   997 KEYLLGKLERELARLSNKVRFIKHVINGElviTNAKKKD---LVKELKKLGYVRFKDIIkkKSEKITAEEEEGAEEDDEA 1073

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  192 EEELSAEKRRST----------------EMEAQMEKQLSEFDTEREQLRAKlNREEAHTTDLK---EEIDKMRKMIEQLK 252
Cdd:PTZ00108  1074 DDEDDEEELGAAvsydyllsmpiwsltkEKVEKLNAELEKKEKELEKLKNT-TPKDMWLEDLDkfeEALEEQEEVEEKEI 1152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  253 RGSDSKPSlslPRKTKDRRLVSisvgtegtvtrsvacQTDLVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSAT 332
Cdd:PTZ00108  1153 AKEQRLKS---KTKGKASKLRK---------------PKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPD 1214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  333 MARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSL-- 410
Cdd:PTZ00108  1215 NKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPdg 1294

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  411 ---HSPCANTSLHPGLNPRIQ----AARFRFQGNANDPDQNGNTTQSPPSRDVSPTSR 461
Cdd:PTZ00108  1295 esnGGSKPSSPTKKKVKKRLEgslaALKKKKKSEKKTARKKKSKTRVKQASASQSSRL 1352
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 101-228 1.11e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 41.13  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESR-----QKKLEMEK-LQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:pfam10473    2 EKKQLHVLEKLKESERKadslkDKVENLEReLEMSEENQELAILEAENSkAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 228
Cdd:pfam10473   82 KENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 761-845 1.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  761 TPL--CAAAAQGHFECVELLISYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVD 834
Cdd:PHA02859    53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132

                           90
                   ....*....|...
gi 2462616488  835 TGNV--DSLKLLM 845
Cdd:PHA02859   133 NFNVriNVIKLLI 145
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 101-232 1.12e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.40  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMS--AQLAAAESRQKKLEMEKLQLQALEQEHKK-LAARLEEERGKNKQVVLMlvKECKQLS-GKVIEEAQKLE- 175
Cdd:pfam15709  372 EKMREELEleQQRRFEEIRLRKQRLEEERQRQEEEERKQrLQLQAAQERARQQQEEFR--RKLQELQrKKQQEEAERAEa 449

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  176 ------DVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:pfam15709  450 ekqrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 124-254 1.17e-03

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 tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 43.05  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  124 EKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKT-----NELEEElsaE 198
Cdd:pfam07767  198 QELLQKAVEAEKKRLKEEEKLER---------------------VLEKIAESAATAEAREEKRKTkaqrnKEKRRK---E 253

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  199 KRRSTEMEAQMEKQLSEFDTEREqLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:pfam07767  254 EEREAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 177-253 1.18e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.31  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  177 VMAKLEEEKKK-TNELEEelsAEKRRS--TEMEAQMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKM- 247
Cdd:COG0711     25 ILKALDERQEKiADGLAE---AERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEaeaiaEEAKAEAEAEAERIIAQa 101


                   ....*....
gi 2462616488  248 ---IEQLKR 253
Cdd:COG0711    102 eaeIEQERA 110
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 112-243 1.18e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  112 AAAesrQKKLEMEKL--QLQALEQEHkklaARLEEERGKnkqvvlmLVKECKQLSgkvIEEAQKLEDVMAKLEEEKkktN 189
Cdd:COG0542    398 AAA---RVRMEIDSKpeELDELERRL----EQLEIEKEA-------LKKEQDEAS---FERLAELRDELAELEEEL---E 457

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  190 ELEEELSAEK---RRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:COG0542    458 ALKARWEAEKeliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 105-230 1.21e-03

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: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 43.51  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvkECKQLSGKVIEEaqKLEDVMAKLEEE 184
Cdd:pfam05911  698 ENLEVELASCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 770

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  185 KKKTNELEEELSAEKR-------RSTEMEAQME----KQLSEFDTEREQLRAKLNRE 230
Cdd:pfam05911  771 RQKFEALEVELEEEKNcheeleaKCLELQEQLErnekKESSNCDADQEDKKLQQEKE 827
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
117-270 1.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  117 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELs 196
Cdd:PRK02224   183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI-ERYEEQREQARETRDEADEVLEEHEERREELETLEAEI- 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  197 aEKRRSTEMEAQMEK------------QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG-SDSKPSLSL 263
Cdd:PRK02224   261 -EDLRETIAETEREReelaeevrdlreRLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRlEECRVAAQA 339


                   ....*..
gi 2462616488  264 PRKTKDR 270
Cdd:PRK02224   340 HNEEAES 346
PRK01156 PRK01156
chromosome segregation protein; Provisional
 103-249 1.29e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  103 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLA-----ARLEEERG--KNKQVVLMLVKECKQLSGKVieeaQKLE 175
Cdd:PRK01156   250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyKNRNYINDyfKYKNDIENKKQILSNIDAEI----NKYH 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  176 DVMAKLEEEKKKTNELEEelsaEKRRSTEmeaqMEKQLSEFDT----------EREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:PRK01156   326 AIIKKLSVLQKDYNDYIK----KKSRYDD----LNNQILELEGyemdynsylkSIESLKKKIEEYSKNIERMSAFISEIL 397


                   ....
gi 2462616488  246 KMIE 249
Cdd:PRK01156   398 KIQE 401
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 91-253 1.31e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   91 SILEAVMAHCKKMQERMSA---------QLAAAESRQKkLEMEKlQLQALEQEHKKLAARLEEERGKNKQVVlmlvKECK 161
Cdd:pfam01576  447 SLLNEAEGKNIKLSKDVSSlesqlqdtqELLQEETRQK-LNLST-RLRQLEDERNSLQEQLEEEEEAKRNVE----RQLS 520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  162 QLSGKVIEEAQKLED---VMAKLEEEKKKtneLEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNreeahttDLK 238
Cdd:pfam01576  521 TLQAQLSDMKKKLEEdagTLEALEEGKKR---LQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELD-------DLL 586

                          170
                   ....*....|....*
gi 2462616488  239 EEIDKMRKMIEQLKR 253
Cdd:pfam01576  587 VDLDHQRQLVSNLEK 601
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 90-249 1.36e-03

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: 43.50  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKL---EMEKLQLQALEQEHKKLAARLEEERGKN---KQVVLMLVKE---C 160
Cdd:TIGR00606  600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDEnqsC 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  161 KQLSGKVIEEAQKLEDVMAKLEEEKK----KTNELEEELSAEKRRSTEMEAQMEKQLSEFD---TEREQLRAKLNREEAH 233
Cdd:TIGR00606  680 CPVCQRVFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRD 759

                          170
                   ....*....|....*.
gi 2462616488  234 TTDLKEEIDKMRKMIE 249
Cdd:TIGR00606  760 IQRLKNDIEEQETLLG 775
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 8-256 1.42e-03

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: 43.50  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    8 LKKKEFDVDtlsksELRMLLSVMEGELEARDLVIEALRARRKEVF--IQERYGRFNLNDPFLalqrdyEAGAGDKEKKPV 85
Cdd:TIGR00606  718 LKKKEKRRD-----EMLGLAPGRQSIIDLKEKEIPELRNKLQKVNrdIQRLKNDIEEQETLL------GTIMPEEESAKV 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   86 CTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK--------KLAARLEEERGKNKQVVLMLV 157
Cdd:TIGR00606  787 CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldtvvskiELNRKLIQDQQEQIQHLKSKT 866

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  158 KECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNRE----EAH 233
Cdd:TIGR00606  867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK----DQQEKEELISSKETSnkkaQDK 942

                          250       260
                   ....*....|....*....|....*..
gi 2462616488  234 TTDLKEEIDK----MRKMIEQLKRGSD 256
Cdd:TIGR00606  943 VNDIKEKVKNihgyMKDIENKIQDGKD 969
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 169-250 1.44e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 41.73  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  169 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam06785   87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVL 166


                   ..
gi 2462616488  249 EQ 250
Cdd:pfam06785  167 EK 168
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 166-253 1.52e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  166 KVIEEAQKLEDVMAKLEEEKKKtneleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:pfam03938    9 KILEESPEGKAAQAQLEKKFKK-----------------RQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71


                   ....*...
gi 2462616488  246 KMIEQLKR 253
Cdd:pfam03938   72 QELQQLQQ 79
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 101-226 1.63e-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: 42.53  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK-KLAARLEEERGKNKQVVLMLVKECKQLSGK-------VIEEAQ 172
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeakakaeAEAERK 143

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  173 KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 226
Cdd:TIGR02794  144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 695-906 1.63e-03

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: 42.94  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  695 LLQQAAAQGNvtlLSMLLNEEGLDINYsceDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAdkngftpLCAAAAQGHfec 774
Cdd:cd21882     48 LLEAAPDSGN---PKELVNAPCTDEFY---QGQTALHIAIENRNLNLVRLLVENGADVSAR-------ATGRFFRKS--- 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  775 VELLISYdaninhaadgGQTPLYLACKNGNKECIKLLLEAGTN-RSVKTTD--GWTPVHAAVDTGN--VDSLKLL--MYH 847
Cdd:cd21882    112 PGNLFYF----------GELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYN 181

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  848 RIPAHGNSfneeesessvfdldggeespegiSKPVVPADLInhANREGWTAAHIAASKG 906
Cdd:cd21882    182 LLLSYGAH-----------------------LDPTQQLEEI--PNHQGLTPLKLAAVEG 215
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 116-248 1.66e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 40.62  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  116 SRQKKLEMEKLQlQALEQEHKKLAARLEEERGKNkqvvLMLVKEckqlsgkvieeAQKLEDVMAKLEEEKKKTNELEEEL 195
Cdd:pfam12474   31 ERQQKQQIEKLE-QRQTQELRRLPKRIRAEQKKR----LKMFRE-----------SLKQEKKELKQEVEKLPKFQRKEAK 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  196 saeKRRSTEMEAQMEKQlsefdtEREQLRAKLnreEAHTTDLKEEIDKMRKMI 248
Cdd:pfam12474   95 ---RQRKEELELEQKHE------ELEFLQAQS---EALERELQQLQNEKRKEL 135
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 104-253 1.67e-03

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: 43.29  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKQVVlMLVKECKQLSGKV 167
Cdd:pfam12128  620 QAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN-SLEAQLKQLDKKH 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 ---IEE--AQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEID 242
Cdd:pfam12128  699 qawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778

                          170
                   ....*....|.
gi 2462616488  243 KMRKMIEQLKR 253
Cdd:pfam12128  779 TLERKIERIAV 789
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 119-250 1.69e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 41.18  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  119 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----LEE 193
Cdd:pfam09756    1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQeeyekLKS 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  194 ELSAEKRRSTEMEAQMEKQLSE----FDTER-----EQLRAKLNreeahtTDLKEEIDKMRKMIEQ 250
Cdd:pfam09756   81 QFVVEEEGTDKLSAEDESQLLEdfinYIKLKkvvllEELAAEFG------LKTQDVIDRIQDLEEQ 140
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
80-231 1.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   80 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLML- 156
Cdd:PRK03918   618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreEYLELSRELAGLRAELEELEKRREEIKKTLe 697

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462616488  157 -VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELsaeKRRSTEMEAQMEKQL-SEFdTEREQLRAKLNREE 231
Cdd:PRK03918   698 kLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL---KERALSKVGEIASEIfEEL-TEGKYSGVRVKAEE 770
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 792-817 1.80e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.80e-03
                           10        20
                   ....*....|....*....|....*.
gi 2462616488  792 GQTPLYLACKNGNKECIKLLLEAGTN 817
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGAD 27
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 97-215 1.80e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 41.61  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   97 MAHCKKMQERMSAQ------LAA-AESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKQVVLM 155
Cdd:pfam13904   41 ARKLEGLKLERQPLeayenwLAAkQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKA 120

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  156 LVKECKQLSGKVIEEAQklEDVMAKLEE-EKKKTNEL----EEELSAEKRRstEMEAQMEKQLSE 215
Cdd:pfam13904  121 AESASKSLAKPERKVSQ--EEAKEVLQEwERKKLEQQqrkrEEEQREQLKK--EEEEQERKQLAE 181
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 102-252 1.93e-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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  102 KMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkqvvLMLVKECKQLSgkviEEAQKLEDvm 178
Cdd:pfam01576  437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  179 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTeREQLRAKLNRE-EAHTTDLKE---EIDKMRKMIEQLK 252
Cdd:pfam01576  504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEEkaaAYDKLEKTKNRLQ 579
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 101-150 2.00e-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: 2.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462616488  101 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 150
Cdd:cd14686      4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 166-246 2.04e-03

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 39.51  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  166 KVIEEA-QKLEDVMAKLEEEKKKT-NELEEElSAEKRRSTEMEAQMEKQ--LSEFDTEREQLRAKLnREEAhttdlKEEI 241
Cdd:COG2811      8 KEIKEAeEEADEIIEEAKEEREERiAEAREE-AEEIIEQAEEEAEEEAQerLEEAREEAEAEAEEI-IEEG-----EKEA 80


                   ....*
gi 2462616488  242 DKMRK 246
Cdd:COG2811     81 EALKK 85
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 99-257 2.05e-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: 42.89  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   99 HCKkmqERMSAQLAAAESRQ-KKLEMEKLQLQALEQEHKKLAARLEEErGKNKQVVLMLVKECKQLSgkviEEAQKLEDV 177
Cdd:pfam10174  596 NDK---DKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEE-ARRREDNLADNSQQLQLE----ELMGALEKT 667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ---LKR 253
Cdd:pfam10174  668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEALLAAISEKDANIALLELSSSKKKKTQEEvmaLKR 747


                   ....
gi 2462616488  254 GSDS 257
Cdd:pfam10174  748 EKDR 751
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-254 2.05e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  122 EMEKlQLQALEQE------HKKLAARLEEergknKQVVLMLVKeckqlsgkvieeaqkLEDVMAKLEEEKKKTNELEEEL 195
Cdd:COG1196    197 ELER-QLEPLERQaekaerYRELKEELKE-----LEAELLLLK---------------LRELEAELEELEAELEELEAEL 255

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  196 SAEkrrstemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:COG1196    256 EEL-----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 93-252 2.24e-03

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: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 172
Cdd:pfam04012   45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQ------AALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 KLEDVMAKLEEEKKKTNELEEELSAEKrrsteMEAQMEKQLSEFDTER-----EQLRAKLNREEAhTTDLKEEIDKMRKM 247
Cdd:pfam04012  119 QLAALETKIQQLKAKKNLLKARLKAAK-----AQEAVQTSLGSLSTSSatdsfERIEEKIEEREA-RADAAAELASAVDL 192


                   ....*
gi 2462616488  248 IEQLK 252
Cdd:pfam04012  193 DAKLE 197
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 95-252 2.54e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 41.18  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   95 AVMAHCKKMQERMSAQlAAAESRQKKLEMEKLQLqALEQEHKklaarleeergknkQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:pfam15665   56 QTLEESLEQHERMKRQ-ALTEFEQYKRRVEEREL-KAEAEHR--------------QRVVELSREVEEAKRAFEEKLESF 119

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  175 EDVMAKLEEEKKKTneLEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHttdlKEEIDKMRKMIEQLK 252
Cdd:pfam15665  120 EQLQAQFEQEKRKA--LEELRAKHRQEIQELLTTQRAQSASSLAEQEKL------EELH----KAELESLRKEVEDLR 185
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
172-252 2.69e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  172 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqmekQLSEFDTEREQLRAKL--NREEAHTtdLKEEIDKMRKMIE 249
Cdd:COG1340      1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE----ELKELAEKRDELNAQVkeLREEAQE--LREKRDELNEKVK 74


                   ...
gi 2462616488  250 QLK 252
Cdd:COG1340     75 ELK 77
DUF4355 pfam14265
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ...
 177-252 2.69e-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: 39.21  E-value: 2.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462616488  177 VMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQlsefDTEREQLRAKLNREEAHTTdLKEEIDKMRKMIEQLK 252
Cdd:pfam14265    8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 67-250 2.83e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   67 LALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERmsAQLAAAESRQKKLEMEKLQlQALEQEHKKLAARLEEER 146
Cdd:cd22656     97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDK--AAKVVDKLTDFENQTEKDQ-TALETLEKALKDLLTDEG 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  147 GKNKQvvlmlvKECKQLSGKvIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqMEKQLSEFDTEREQLR 224
Cdd:cd22656    174 GAIAR------KEIKDLQKE-LEKLNEeyAAKLKAKIDELKALIADDEAKLAAALRLIADLTA-ADTDLDNLLALIGPAI 245

                          170       180
                   ....*....|....*....|....*.
gi 2462616488  225 AKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:cd22656    246 PALEKLQGAWQAIATDLDSLKDLLED 271
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 112-252 2.86e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. 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 this 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. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 42.37  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  112 AAAESRQKKLEMEKL--------QLQALEQEHKKlaaRLEEERGKNKQVvlmlvkecKQLSGKVIEEAQKledvMAKLEE 183
Cdd:pfam05622  109 LAEEAQALKDEMDILressdkvkKLEATVETYKK---KLEDLGDLRRQV--------KLLEERNAEYMQR----TLQLEE 173

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  184 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT---EREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:pfam05622  174 ELKKANALRGQLETYKRQVQELHGKLSEESKKADKlefEYKKLEEKLEALQKEKERLIIERDTLRETNEELR 245
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 101-256 3.01e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 40.81  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQ-ERMSAQLAAAESRQK--KLEMEKLQLQALEQEHKKLAARLEEERGKNKQVV---LMLVKECKQLSGKVIEEAQK- 173
Cdd:pfam05010   11 EKARnEIEEKELEINELKAKyeELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEhaeIQKVLEEKDQALADLNSVEKs 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  174 LEDVMAKLE------------EE--KKKTNELEEELSAEKRRSTEMEAQMEKQL-----------SEFDTEREQLRAKLN 228
Cdd:pfam05010   91 FSDLFKRYEkqkevisgykknEEslKKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLR 170

                          170       180
                   ....*....|....*....|....*...
gi 2462616488  229 REEAHTTDLKEEIDKMRKMIEQLKRGSD 256
Cdd:pfam05010  171 KEQMKVQSLERQLEQKTKENEELTKICD 198
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 118-275 3.02e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.72  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  118 QKKLEMEKlQLQALEQEHKKLAARLeeergknkqvvLMLVKECKQLSGKVIE-EAQKLEDVMA------KLEEE--KKKT 188
Cdd:pfam15905   87 QERGEQDK-RLQALEEELEKVEAKL-----------NAAVREKTSLSASVASlEKQLLELTRVnellkaKFSEDgtQKKM 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  189 NELEEEL-SAEKRRSTEMEA------QMEKQLSEFDTEREQLRAKL--------------NREEAHTTDLKEEIDKMRKM 247
Cdd:pfam15905  155 SSLSMELmKLRNKLEAKMKEvmakqeGMEGKLQVTQKNLEHSKGKVaqleeklvstekekIEEKSETEKLLEYITELSCV 234

                          170       180
                   ....*....|....*....|....*...
gi 2462616488  248 IEQLKRGSDSKPSLSLPRKTKDRRLVSI 275
Cdd:pfam15905  235 SEQVEKYKLDIAQLEELLKEKNDEIESL 262
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
8-311 3.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488    8 LKKKEFDVDTLsKSELRML---LSVMEGELEArdlVIEALRARRKEV-FIQERYGRFNLNdpflaLQRDYEAGAGDKEKk 83
Cdd:COG4372     33 LRKALFELDKL-QEELEQLreeLEQAREELEQ---LEEELEQARSELeQLEEELEELNEQ-----LQAAQAELAQAQEE- 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   84 pvctnplsiLEAVMAHCKKMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKEC 160
Cdd:COG4372    103 ---------LESLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  161 KQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 240
Cdd:COG4372    174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462616488  241 IDKM---RKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVK 311
Cdd:COG4372    254 EVILkeiEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 115-218 3.12e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 40.09  E-value: 3.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   115 ESRQK-KLEMEKLQLQ-----ALEQEHKKLAARLEEERGK-NKQVVLMLVKEC-KQLSGKVIEEAQKLEDVMAKLEEEKK 186
Cdd:smart01071   39 QARVErMEEIKNLKYElimndHLNKRIDKLLKGLREEELSpETPTYNEMLAELqDQLKKELEEANGDSEGLLEELKKHRD 118

                            90       100       110
                    ....*....|....*....|....*....|..
gi 2462616488   187 KTNELEEELsaeKRRSTEMEAQMEKQLSEFDT 218
Cdd:smart01071  119 KLKKEQKEL---RKKLDELEKEEKKKIWSVDT 147
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 105-252 3.38e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKL-----AARLEEergkNKQVvlmlvkecKQLSGKVIEEAQKLEDvma 179
Cdd:pfam10368    4 EKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELyeeiiELGMDE----FDEI--------KKLSDEALENVEEREE--- 68

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  180 KLEEEKKKTNELEEELSaekrrstEMEAQMEK-QLSEFDTEREQLRAKLN-REEAH---TTDLKEEIDKMRKMIEQLK 252
Cdd:pfam10368   69 LLEKEKESIEEAKEEFK-------KIKEIIEEiEDEELKKEAEELIDAMEeRYEAYdelYDAYKKALELDKELYEMLK 139
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 133-258 3.54e-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: 41.41  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  133 QEHKKLAARLEEERGKN---KQVVLMLVKEcKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE-ELSAEKRRSTEMEAQ 208
Cdd:cd16269    149 EDREKLVEKYRQVPRKGvkaEEVLQEFLQS-KEAEAEAILQADQALTEKEKEIEAERAKAEAAEqERKLLEEQQRELEQK 227

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  209 MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI--DKMRKMIEQLKRGSDSK 258
Cdd:cd16269    228 LEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSKLKEQEALLEEGFKEQ 279
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 156-252 3.60e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.54  E-value: 3.60e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   156 LVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE----ELSA--EKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLN 228
Cdd:smart00787  163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRakEKLKKLLQEIMIKVKkLEELEEELQELESKIE 242

                            90       100
                    ....*....|....*....|....
gi 2462616488   229 REEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:smart00787  243 DLTNKKSELNTEIAEAEKKLEQCR 266
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 110-250 3.76e-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: 41.93  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  110 QLAAAESRQKKLEMEKLQ----LQALEQEHKKLAARL------EEERGKNKQVVLM----------------LVKECKQL 163
Cdd:TIGR04523  518 KISSLKEKIEKLESEKKEkeskISDLEDELNKDDFELkkenleKEIDEKNKEIEELkqtqkslkkkqeekqeLIDQKEKE 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  164 SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:TIGR04523  598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677


                   ....*..
gi 2462616488  244 MRKMIEQ 250
Cdd:TIGR04523  678 IIELMKD 684
PHA02798 PHA02798
ankyrin-like protein; Provisional
 740-845 3.86e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  740 DCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF---ECVELLISYDANINHAADGGQTPLYLACKNGNK---ECIKLLLE 813
Cdd:PHA02798    90 DIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462616488  814 AGTN-RSVKTTDGWTPVHA----AVDTGNVDSLKLLM 845
Cdd:PHA02798   170 KGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFV 206
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
317-570 4.16e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.76  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  317 PLVSANAKGSVCTSATMARP-GIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPlPSNAAPP----- 390
Cdd:PRK07003   360 PAVTGGGAPGGGVPARVAGAvPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP-PAAPAPPatadr 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  391 -TAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAarfrfqgnANDPDQNGNTTQSPPSRDVSPTSRdnlVAKQL 469
Cdd:PRK07003   439 gDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSAS--------APASDAPPDAAFEPAPRAAAPSAA---TPAAV 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  470 ARNTVTQALSRFTSPQAGAPSRPGVPPTGdvgthPPVGRTSLKTHGVA-----------RV--DRG-NPPPIPPKKPGLS 535
Cdd:PRK07003   508 PDARAPAAASREDAPAAAAPPAPEARPPT-----PAAAAPAARAGGAAaaldvlrnagmRVssDRGaRAAAAAKPAAAPA 582

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462616488  536 QTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTP 570
Cdd:PRK07003   583 AAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAE 617
fliH PRK06669
flagellar assembly protein H; Validated
 101-277 4.38e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 41.16  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAK 180
Cdd:PRK06669    28 KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEE 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  181 LEEEKKktnELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRA---KLNRE-EAHTTDLKEEIDKMRKMI--EQLKRG 254
Cdd:PRK06669   108 WEEELE---RLIEEAKAEGYEEGYEKGR-EEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELALDIakKVIKEI 183

                          170       180
                   ....*....|....*....|....*....
gi 2462616488  255 SDSKPSLSLP------RKTKDRRLVSISV 277
Cdd:PRK06669   184 SENSKEIALAlvkellKEVKDATDITIRV 212
PRK12705 PRK12705
hypothetical protein; Provisional
 101-262 4.55e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.62  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEER-----GKNKQVVLMLVKECKQL---SGKVIEEAQ 172
Cdd:PRK12705    33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREElqreeERLVQKEEQLDARAEKLdnlENQLEEREK 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  173 KLEDVMAKLEEEKKKT-NELEEelsAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:PRK12705   113 ALSARELELEELEKQLdNELYR---VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRI 189

                          170
                   ....*....|.
gi 2462616488  252 KRGSDSKPSLS 262
Cdd:PRK12705   190 ASETASDLSVS 200
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
368-665 4.56e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.76  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  368 PSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMhslhspcANTSLHPGLNPRIQAARFRFQGNAndpdqngnt 447
Cdd:PRK07003   360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAV-------TAVTGAAGAALAPKAAAAAAATRA--------- 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  448 tQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSlkthgvarvdrgnpppi 527
Cdd:PRK07003   424 -EAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAP----------------- 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  528 ppkkpglsqTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQgnrvineenlPKSSSPQL-PPKPSIDLTVAPA 606
Cdd:PRK07003   486 ---------PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAA----------AAPPAPEArPPTPAAAAPAARA 546

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462616488  607 GCAVSAL-------------------ATSQVGAWPAATPglnQPACSDSSLVIPTTIAFCSSINPVSASSCR-PGASDS 665
Cdd:PRK07003   547 GGAAAALdvlrnagmrvssdrgaraaAAAKPAAAPAAAP---KPAAPRVAVQVPTPRARAATGDAPPNGAARaEQAAES 622
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 112-277 4.63e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  112 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEA--------------QKLEDV 177
Cdd:PRK00409   523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAkkeadeiikelrqlQKGGYA 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  178 MAK---LEEEKKKTNE----LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLrAKLNREEAhttDLKEEIDKMRKMIEQ 250
Cdd:PRK00409   603 SVKaheLIEARKRLNKanekKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL-SIPDDKEA---IVQAGIMKMKVPLSD 678

                          170       180
                   ....*....|....*....|....*..
gi 2462616488  251 LKRGSDSKPSLSLPRKTKDRRLVSISV 277
Cdd:PRK00409   679 LEKIQKPKKKKKKKPKTVKPKPRTVSL 705
PHA02791 PHA02791
ankyrin-like protein; Provisional
 726-826 4.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  726 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADkNGFtPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNK 805
Cdd:PHA02791    30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107

                           90       100
                   ....*....|....*....|.
gi 2462616488  806 ECIKLLLEAGTNRSVKTTDGW 826
Cdd:PHA02791   108 QTVKLFVKKNWRLMFYGKTGW 128
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 760-848 4.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  760 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTdgWTPVHAAVDTGNVD 839
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVE 115


                   ....*....
gi 2462616488  840 SLKLLMYHR 848
Cdd:PHA02878   116 IFKIILTNR 124
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 309-496 5.01e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 5.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  309 PVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAA 388
Cdd:PRK07764   601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  389 PPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAARfrfQGNANDPDQNGNTTQSPPsrdvsPTSRDNLVAKQ 468
Cdd:PRK07764   681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQ---AAQGASAPSPAADDPVPL-----PPEPDDPPDPA 752

                          170       180
                   ....*....|....*....|....*...
gi 2462616488  469 LARNTVTQALSRFTSPQAGAPSRPGVPP 496
Cdd:PRK07764   753 GAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
PRK10905 PRK10905
cell division protein DamX; Validated
 307-406 5.63e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 40.69  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  307 TMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLI-------GASVPAFPPPSANKIEENGPSTGSTPDPTSS 379
Cdd:PRK10905   122 TLPTEPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIepkkpqaTAKTEPKPVAQTPKRTEPAAPVASTKAPAAT 201

                           90       100
                   ....*....|....*....|....*..
gi 2462616488  380 TPPLPSNAApPTAQTPGIAPQNSQAPP 406
Cdd:PRK10905   202 STPAPKETA-TTAPVQTASPAQTTATP 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
22-250 5.81e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   22 ELRMLLSVMEGELEARDLVIEALRARRkEVFIQERYGRFNLNDpFLALQRDYEA--------GAGDKEkkpvctnpLSIL 93
Cdd:COG4913    621 ELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID-VASAEREIAEleaelerlDASSDD--------LAAL 690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   94 EAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEE-ERGKNKQVVLMLVKECKQLSGKVIEE-- 170
Cdd:COG4913    691 EEQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVERel 767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  171 AQKLEDVMAKLEEEK-KKTNELEEELSAEKRR----STEMEAQMEkQLSEFDTEREQL-------------RAKLNREEA 232
Cdd:COG4913    768 RENLEERIDALRARLnRAEEELERAMRAFNREwpaeTADLDADLE-SLPEYLALLDRLeedglpeyeerfkELLNENSIE 846

                          250
                   ....*....|....*...
gi 2462616488  233 HTTDLKEEIDKMRKMIEQ 250
Cdd:COG4913    847 FVADLLSKLRRAIREIKE 864
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 101-256 5.85e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 41.43  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAaesRQKKLEMEKLQLQALEQehKKLAARLEEERGKNKQVVLMlvkECKQLSGKVIEEAQKLEDVMAK 180
Cdd:pfam15964  307 KERDDLMSALVSV---RSSLAEAQQRESSAYEQ--VKQAVQMTEEANFEKTKALI---QCEQLKSELERQKERLEKELAS 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  181 ------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam15964  379 qqekraqekealRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458


                   ....*...
gi 2462616488  249 EQLKRGSD 256
Cdd:pfam15964  459 NQTKMKKD 466
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 102-211 5.90e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.82  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  102 KMQ----ERMSAQLAA--AESRQKKLEMEKLQ-----------LQALEQEHKKLAARLEE-----ERGKNKQV------- 152
Cdd:pfam12718    1 KMNslklEAENAQERAeeLEEKVKELEQENLEkeqeikslthkNQQLEEEVEKLEEQLKEakekaEESEKLKTnnenltr 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  153 -VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK 211
Cdd:pfam12718   81 kIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 169-251 6.08e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 39.80  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  169 EEAQKLEDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQMEKQL----SEFDTER----EQLRAK---LNREEAHT 234
Cdd:pfam06785   80 LDAEGFKILEETLEELQSEEERLEEELSqkeEELRRLTEENQQLQIQLqqisQDFAEFRleseEQLAEKqllINEYQQTI 159

                           90
                   ....*....|....*..
gi 2462616488  235 TDLKEEIDKMRKMIEQL 251
Cdd:pfam06785  160 EEQRSVLEKRQDQIENL 176
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 168-252 6.43e-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: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.84  E-value: 6.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  168 IEEAQKLEDVMAKLEEEK----KKTNELEEELSAekrrstemeAQMEKQLSEFDtEReQLRAKLNREEAHTTDLKEEIDK 243
Cdd:pfam11559   51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLED---------LERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119


                   ....*....
gi 2462616488  244 MRKMIEQLK 252
Cdd:pfam11559  120 LKNALQQIK 128
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
93-236 6.59e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 38.73  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   93 LEAVMAHCKKMQERMSAQLAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkecKQLSGKVIEEAQ 172
Cdd:COG2882      7 LQTLLDLAEKEEDEAARELGQA---QQALEQAEEQLEQLEQYREEYEQRLQQ----------------KLQQGLSAAQLR 67

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  173 KLEDVMAKLEEE----KKKTNELEEELsaEKRRSTEMEAQMEKQLseFDT----EREQLRAKLNREEAHTTD 236
Cdd:COG2882     68 NYQQFIARLDEAieqqQQQVAQAEQQV--EQARQAWLEARQERKA--LEKlkerRREEERQEENRREQKELD 135
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
 81-253 6.75e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 40.32  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   81 EKKPVCTNPLSILEAvmAHCKKMQErMSAQLaaaesrQKKLEMEKLQLQALEQEHKKLAARLEEERGK------------ 148
Cdd:pfam15397   45 QQYEKFGTIISILEY--SNKKQLQQ-AKAEL------QEWEEKEESKLNKLEQQLEQLNAKIQKTQEElnflstykdkey 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  149 -NKQV-VLMLVKECKQLSGKVIEEAQKLED----VMAKLEEEK-KKTNELEEELSAEKRRSTEmEAQMEKQLSEFDTERE 221
Cdd:pfam15397  116 pVKAVqIANLVRQLQQLKDSQQDELDELEEmrrmVLESLSRKIqKKKEKILSSLAEKTLSPYQ-ESLLQKTRDNQVMLKE 194

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462616488  222 QLRAKLNREEahttdLKEEIDKMRKMIEQLKR 253
Cdd:pfam15397  195 IEQFREFIDE-----LEEEIPKLKAEVQQLQA 221
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 127-252 6.76e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  127 QLQALEQEHKKLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEE-------AQKLEDVMAKLEEEKKKTNELEEE-- 194
Cdd:PRK04778   113 LLDLIEEDIEQILEELQELLEseeKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEEFSQFVELTESgd 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  195 -------LSAEKRRSTEMEAQMEK---QLSEFDTE-REQLR------AKLNRE---------EAHTTDLKEEIDKMRKMI 248
Cdd:PRK04778   193 yveareiLDQLEEELAALEQIMEEipeLLKELQTElPDQLQelkagyRELVEEgyhldhldiEKEIQDLKEQIDENLALL 272


                   ....
gi 2462616488  249 EQLK 252
Cdd:PRK04778   273 EELD 276
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 167-272 6.79e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  167 VIEEAQKLEdvmAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 246
Cdd:pfam07888   25 VVPRAELLQ---NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE 101

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462616488  247 MIEQLKRGSDS----KPSLSLPRKTKDRRL 272
Cdd:pfam07888  102 KYKELSASSEElseeKDALLAQRAAHEARI 131
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 101-253 7.32e-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: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  101 KKMQERMSAQLAAAESRQKKL----EMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLsgkviEEAQKL 174
Cdd:pfam05557  359 RAILESYDKELTMSNYSPQLLerieEAEDMtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-----RQQESL 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  175 EDVMAKLEEE---KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam05557  434 ADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKtkvLHLSMNPAAEAYQQRKNQLEKLQAEI 513


                   ....*
gi 2462616488  249 EQLKR 253
Cdd:pfam05557  514 ERLKR 518
PHA02917 PHA02917
ankyrin-like protein; Provisional
 775-848 7.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.14  E-value: 7.38e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  775 VELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV-DTGNVDSLKLLMYHR 848
Cdd:PHA02917   435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 114-258 7.39e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  114 AESRQKKLEMEKLQLQALEqehkkLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEEAQKLEdvmAKLEEEKKKTNE 190
Cdd:pfam07888  272 AELHQARLQAAQLTLQLAD-----ASLALREGRArwaQERETLQQSAEADKDRIEKLSAELQRLE---ERLQEERMEREK 343

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462616488  191 LEEELSAEKRRStemeaqmEKQLSEFDTEREQLRAKL----NREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 258
Cdd:pfam07888  344 LEVELGREKDCN-------RVQLSESRRELQELKASLrvaqKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-251 7.48e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  170 EAQKLEDVMAKLEEE-----------KKKTNELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTT 235
Cdd:TIGR02168  678 EIEELEEKIEELEEKiaelekalaelRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKELT 757

                           90
                   ....*....|....*.
gi 2462616488  236 DLKEEIDKMRKMIEQL 251
Cdd:TIGR02168  758 ELEAEIEELEERLEEA 773
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 694-849 7.48e-03

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: 40.83  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSC-------EDGHSALY------SAAKN-GHTDCVRLLLSAEAQVNAADKNG 759
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLL-ERGASVPARAcgdffvkSQGVDSFYhgesplNAAAClGSPSIVALLSEDPADILTADSLG 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  760 FTPLCAAAAQGHF---------ECVELLISYDANI----------NHAadgGQTPLYLACKNGNKECIKLLLEagTNRSV 820
Cdd:TIGR00870  209 NTLLHLLVMENEFkaeyeelscQMYNFALSLLDKLrdskelevilNHQ---GLTPLKLAAKEGRIVLFRLKLA--IKYKQ 283

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462616488  821 KTTDGWT--PVH-AAVDTGNVDS-------LKLLMYHRI 849
Cdd:TIGR00870  284 KKFVAWPngQQLlSLYWLEELDGwrrkqsvLELIVVFVI 322
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
 150-241 7.66e-03

Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.


Pssm-ID: 461118  Cd Length: 103  Bit Score: 37.61  E-value: 7.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  150 KQVVLMLVKECKQLSGKVIEEaqklEDVMAKLeeekkktNELEE-ELSAEKRRSTEMEAQMEKQL-----------SEFD 217
Cdd:pfam03980    8 RQMVEFLQESCREEFEEILEE----RDVVAKL-------NELDElIEEAKERREEGEGPAWRPSVppeelirahlaPYKQ 76

                           90       100
                   ....*....|....*....|....
gi 2462616488  218 TEREQLRAKLNREEAHTTDLKEEI 241
Cdd:pfam03980   77 KQLEQLNARLQKLEAENAALAEEV 100
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 164-237 7.80e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 38.15  E-value: 7.80e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462616488  164 SGKVIEEAQKLEDVMAKLEEE----KKKTNELEEELSAEKrrstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL 237
Cdd:pfam04871    3 KSELESEASSLKNENTELKAElqelSKQYNSLEQKESQAK----ELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 122-276 8.78e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.68  E-value: 8.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  122 EMEKLQLQALEQEHKKLAARLEEErGknkqvvLMLVKECKQLS-----GKVIEEAQKLEDVMAKLEEEKKKTNELEEELS 196
Cdd:PRK05771     5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  197 AEKRRSTEmEAQmEKQLSEFDTEREQLRAKLNREeahtTDLKEEIDKMRKMIEQLK--RGSDSKPSLSLPRKTKDRRLVS 274
Cdd:PRK05771    78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151


                   ..
gi 2462616488  275 IS 276
Cdd:PRK05771   152 VP 153
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 104-195 8.92e-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: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 38.10  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAR--LEEERGKNKQVVLMLVKecKQLSGKVIEEAQkLEDVMAKL 181
Cdd:pfam00836   44 LEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQkaDEENNNFSKMAEEKLKQ--KMEAYKENREAQ-IAALKEKL 120

                           90
                   ....*....|....
gi 2462616488  182 EEEKKKTNELEEEL 195
Cdd:pfam00836  121 KEKEKHVEEVRKNK 134
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 119-260 9.27e-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: 39.65  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488  119 KKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKECKQLsGKVIEE-AQKLEDvMAKLEEEKKKT-NELEEELS 196
Cdd:cd07596      4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElGEALSKLG 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462616488  197 -AEKRRSTEMEAQMEKQLSEF-DTEREQLR----AKL---NREEA--HTTDLKEEIDKMRKMIEQLKRGSDSKPS 260
Cdd:cd07596     71 kAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 164-253 9.70e-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: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 9.70e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462616488   164 SGKVIEEAQKLEDVMAKLEEEKKKtneLEEELsaekrrsTEMEAQMEKQLSEFDTEreqlRAKLNREEAhtTDLKEEIDK 243
Cdd:smart00935    6 VQKILQESPAGKAAQKQLEKEFKK---RQAEL-------EKLEKELQKLKEKLQKD----AATLSEAAR--EKKEKELQK 69

                            90
                    ....*....|
gi 2462616488   244 MRKMIEQLKR 253
Cdd:smart00935   70 KVQEFQRKQQ 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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