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Conserved domains on  [gi|1822435973|ref|XP_032804765|]
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liprin-alpha-2 isoform X6 [Petromyzon marinus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 1028-1093 2.40e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188964  Cd Length: 66  Bit Score: 154.17  E-value: 2.40e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973 1028 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLKRL 1093
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 920-990 6.51e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188961  Cd Length: 71  Bit Score: 150.41  E-value: 6.51e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  920 FALWDGQTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 990
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1113-1184 9.66e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


:

Pssm-ID: 188967  Cd Length: 72  Bit Score: 149.78  E-value: 9.66e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1113 DVMVWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIALALSLQIPTQNTQARQVLEREFNNLL 1184
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 256-520 1.18e-13

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 76.25  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQ 335
Cdd:TIGR02168  716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 REATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTkydpsspDDS 415
Cdd:TIGR02168  796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELI 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  416 TILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQ-----REKMNEEHNK--RLSDTVDKLLSESNER 488
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRReleelREKLAQLELRleGLEVRIDNLQERLSEE 948

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1822435973  489 LQLHLKERMSSLEEKNALTHELDNTRKQLEEA 520
Cdd:TIGR02168  949 YSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-480 1.17e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   21 QDDASFERLMVGMLDERDRLLDALRDAQETIAHTQSRlhdvchdRDSLQRQLNSALpqefAALTKELNACREQLLEREEE 100
Cdd:COG1196    400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEE-------EEEEEEALEEAA----EEEAELEEEEEALLELLAEL 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  101 IAELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALER 178
Cdd:COG1196    469 LEEAALLEAALAELLEELAEAAARLLLLLEA------EADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEA 542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  179 VAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKArvtNGTGLRDIEGPGRLLELQ 258
Cdd:COG1196    543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV---DLVASDLREADARYYVLG 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  259 DLLDKRSMEVAQ-------MKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRY 331
Cdd:COG1196    620 DTLLGRTLVAARleaalrrAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  332 LGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpss 411
Cdd:COG1196    700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER----- 774

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  412 pddstilevKLQDM-SILLRkAEERHGDIEERLRQLETQLEeknqEVLRARQR-----EKMNEEHNKRLSDTVDK 480
Cdd:COG1196    775 ---------EIEALgPVNLL-AIEEYEELEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 429-695 1.02e-03

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  429 LRKAEERHGDIEERLRQLETQLEEKNQevlrarQREKMNEEHNKRLSdtVDKLLSESNE-RLQLHLKERMSSLEEKNALT 507
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQ------QLERLRREREKAER--YQALLKEKREyEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  508 HELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSMVDPVIPR--SHLGSTSDIRYSLGSSVileapgdpfgsSA 585
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLERSI-----------AE 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  586 VLRRQK---GRLSALRDEPGKVQ-TLNEQEWQRMQQAGVLASVaqafesETEASDQEDDRETIFSSADLLSPSG------ 655
Cdd:TIGR02169  313 KERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKL------TEEYAELKEELEDLRAELEEVDKEFaetrde 386

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1822435973  656 HSDAQTLALMLQEQLDAINNEIRLIQEEKESTEQRAEEIE 695
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 1028-1093 2.40e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 154.17  E-value: 2.40e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973 1028 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLKRL 1093
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 920-990 6.51e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 150.41  E-value: 6.51e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  920 FALWDGQTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 990
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1113-1184 9.66e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 149.78  E-value: 9.66e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1113 DVMVWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIALALSLQIPTQNTQARQVLEREFNNLL 1184
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1027-1091 1.59e-14

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.22  E-value: 1.59e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973 1027 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 256-520 1.18e-13

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: 76.25  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQ 335
Cdd:TIGR02168  716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 REATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTkydpsspDDS 415
Cdd:TIGR02168  796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELI 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  416 TILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQ-----REKMNEEHNK--RLSDTVDKLLSESNER 488
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRReleelREKLAQLELRleGLEVRIDNLQERLSEE 948

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1822435973  489 LQLHLKERMSSLEEKNALTHELDNTRKQLEEA 520
Cdd:TIGR02168  949 YSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 253-518 1.43e-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: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYL 332
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  333 GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpssp 412
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA------ 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  413 dDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESnERLQLH 492
Cdd:COG1196    401 -QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA-ALLEAA 478

                          250       260
                   ....*....|....*....|....*.
gi 1822435973  493 LKERMSSLEEKNALTHELDNTRKQLE 518
Cdd:COG1196    479 LAELLEELAEAAARLLLLLEAEADYE 504
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-531 3.29e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 68.14  E-value: 3.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  151 LKALKSLFEHHKALDEKVRERLRVALERVAALEE---ELQATSQELMLLREQAAHAQRRAGDGSEDATEMEtpptQNSAE 227
Cdd:PRK02224   215 LAELDEEIERYEEQREQARETRDEADEVLEEHEErreELETLEAEIEDLRETIAETEREREELAEEVRDLR----ERLEE 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  228 LRPLTSHAKARvtngTGLRDIEgPGRLLELQDLLDKRSMEVaqmKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQ 307
Cdd:PRK02224   291 LEEERDDLLAE----AGLDDAD-AEAVEARREELEDRDEEL---RDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  308 --------------RDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERL 373
Cdd:PRK02224   363 eeaaeleseleearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  374 ELAEQklqqtMRKAETLPEVEAELAQrvaaltkydpsSPDDSTILEvklqdmsillrkAEERHGDIEERLRQLETQLEEK 453
Cdd:PRK02224   443 EEAEA-----LLEAGKCPECGQPVEG-----------SPHVETIEE------------DRERVEELEAELEDLEEEVEEV 494

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  454 NQEVLRARQREKMNEEHNKRLS--DTVDKLLSESNERLQlHLKERMSSL-EEKNALTHELDNTRKQLEEAHMDKERMADE 530
Cdd:PRK02224   495 EERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREE 573


                   .
gi 1822435973  531 V 531
Cdd:PRK02224   574 V 574
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 28-503 9.16e-11

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: 66.28  E-value: 9.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   28 RLMVGMLDERDRLLDA-LRDAQETIAHTQSRLHDVchdRDSLQRQLNS--ALPQEFAALTK-----------ELNACREQ 93
Cdd:pfam05483  267 RDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKticqlteekeaQMEELNKA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   94 LLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagvsSEVEVLKALKS-----LFEHHKALDEKv 168
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED- 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  169 rERLRVALERVAALEEELQATSQELMLL---REQAAH---AQRRAGDGSED---------ATEMETPPTQNSAelrpLTS 233
Cdd:pfam05483  418 -EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQLTAIKTSEEhylkevedlKTELEKEKLKNIE----LTA 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  234 HAKARVTNGTGLRDiEGPGRLLEL----QDLLDKRSMEvAQMKERLGTLSARVGELEDDVDTARRDLI-----------K 298
Cdd:pfam05483  493 HCDKLLLENKELTQ-EASDMTLELkkhqEDIINCKKQE-ERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkckldK 570

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  299 SEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLN---------------------DKLENELANTED 357
Cdd:pfam05483  571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASAKQ 650

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  358 LLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYdpsspddstilevKLQDMSILLRKAEERHG 437
Cdd:pfam05483  651 KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH-------------KIAEMVALMEKHKHQYD 717

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  438 DI-EERLRQLET-QLEEKNQEVLRARQREKMNEEHNKRLSdtVDKLLS---ESNERLQLHLKERMSSLEEK 503
Cdd:pfam05483  718 KIiEERDSELGLyKNKEQEQSSAKAALEIELSNIKAELLS--LKKQLEiekEEKEKLKMEAKENTAILKDK 786
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 920-986 2.95e-08

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 51.53  E-value: 2.95e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973   920 FALWDGQTVVAWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 986
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1036-1091 5.91e-08

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.76  E-value: 5.91e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973  1036 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-480 1.17e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   21 QDDASFERLMVGMLDERDRLLDALRDAQETIAHTQSRlhdvchdRDSLQRQLNSALpqefAALTKELNACREQLLEREEE 100
Cdd:COG1196    400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEE-------EEEEEEALEEAA----EEEAELEEEEEALLELLAEL 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  101 IAELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALER 178
Cdd:COG1196    469 LEEAALLEAALAELLEELAEAAARLLLLLEA------EADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEA 542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  179 VAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKArvtNGTGLRDIEGPGRLLELQ 258
Cdd:COG1196    543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV---DLVASDLREADARYYVLG 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  259 DLLDKRSMEVAQ-------MKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRY 331
Cdd:COG1196    620 DTLLGRTLVAARleaalrrAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  332 LGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpss 411
Cdd:COG1196    700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER----- 774

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  412 pddstilevKLQDM-SILLRkAEERHGDIEERLRQLETQLEeknqEVLRARQR-----EKMNEEHNKRLSDTVDK 480
Cdd:COG1196    775 ---------EIEALgPVNLL-AIEEYEELEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1116-1185 4.95e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.06  E-value: 4.95e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  1116 VWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIalalsLQIPTQNTQARQVLEREFNNLLA 1185
Cdd:smart00454    3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDL-----KELGITKLGHRKKILKAIQKLKE 67
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1116-1184 2.37e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 43.41  E-value: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822435973 1116 VWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIAlalslQIPTQNTQARQVLEREFNNLL 1184
Cdd:pfam07647    3 SWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLK-----RLGITSVGHRRKILKKIQELK 66
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 923-986 2.92e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 40.33  E-value: 2.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  923 WDGQTVVAWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 986
Cdd:pfam00536    3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 32-423 3.52e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   32 GMLDERDRLLDALRDAQETIAHTQSRLHDVCHDRDSLQRQLNsALPQEFAALTKELNACREQLLEREEEIAELKAErnnt 111
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  112 rllLEHLECLVSRHERSLrmtvvkrqaqspAGVSSEVEVLKA--LKSLFEHHKALDEKVRERLRVALERVAALEEELQAT 189
Cdd:TIGR02169  760 ---LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  190 SQELMLLREQAAHAQRRAGD----GSEDATEMETPPTQNSAELRPLTSHAKARVTNGTGLRDIEGPGR-----LLELQDL 260
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDeleaqLRELERK 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  261 LDKRSMEVAQMKERLGTLSARVGELEDDVDTArRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEkrylgaqreats 340
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE------------ 971

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  341 lhDLNDKLENELANTEDLLKQSEDK-------TRQLQERLELAEQKLQQTMRKA-----ETLPEVEAELAQRVAALTKYD 408
Cdd:TIGR02169  972 --PVNMLAIQEYEEVLKRLDELKEKrakleeeRKAILERIEEYEKKKREVFMEAfeainENFNEIFAELSGGTGELILEN 1049

                          410
                   ....*....|....*
gi 1822435973  409 PSSPDDSTiLEVKLQ 423
Cdd:TIGR02169 1050 PDDPFAGG-LELSAK 1063
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 33-466 5.06e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.90  E-value: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   33 MLDERDRLLDALRDAQETIAHTQSRLhdvchdrdSLQRQLNSALPQEFAALTKELNACREQLLEREEEIAELKAERNNTR 112
Cdd:pfam19220   32 LIEPIEAILRELPQAKSRLLELEALL--------AQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  113 LLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLRVALERVAALEEELQATSQE 192
Cdd:pfam19220  104 AAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQAAEKALQRAEGELATARER 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  193 LMLLREQAAHAQRRAGDGSEDATEMetppTQNSAELRPLTSHAKARvtngtgLRDIEGpgRLLELQDLldkRSMEVAQMK 272
Cdd:pfam19220  169 LALLEQENRRLQALSEEQAAELAEL----TRRLAELETQLDATRAR------LRALEG--QLAAEQAE---RERAEAQLE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  273 ERLGTLSARVGELEDDVDTARRDLIKSEEMNTkyqrdirEAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENEL 352
Cdd:pfam19220  234 EAVEAHRAERASLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  353 antedllkqsEDKTRQLQErlelaeqklQQTMRkaetlpeveAELAQRVAALTKydpsspddstilevKLQDMSILLRKA 432
Cdd:pfam19220  307 ----------ERRTQQFQE---------MQRAR---------AELEERAEMLTK--------------ALAAKDAALERA 344

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1822435973  433 EERHGDIEERLRQLE-------TQLEEKNQEVLRARQREKM 466
Cdd:pfam19220  345 EERIASLSDRIAELTkrfeverAALEQANRRLKEELQRERA 385
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 429-695 1.02e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  429 LRKAEERHGDIEERLRQLETQLEEKNQevlrarQREKMNEEHNKRLSdtVDKLLSESNE-RLQLHLKERMSSLEEKNALT 507
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQ------QLERLRREREKAER--YQALLKEKREyEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  508 HELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSMVDPVIPR--SHLGSTSDIRYSLGSSVileapgdpfgsSA 585
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLERSI-----------AE 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  586 VLRRQK---GRLSALRDEPGKVQ-TLNEQEWQRMQQAGVLASVaqafesETEASDQEDDRETIFSSADLLSPSG------ 655
Cdd:TIGR02169  313 KERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKL------TEEYAELKEELEDLRAELEEVDKEFaetrde 386

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1822435973  656 HSDAQTLALMLQEQLDAINNEIRLIQEEKESTEQRAEEIE 695
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 442-548 9.04e-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: 38.17  E-value: 9.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   442 RLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDN--TRKQLEE 519
Cdd:smart01071   33 KQRDIHQARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLREEELSPETPTYNEMLAELQDQLKKELEEANgdSEGLLEE 112

                            90       100
                    ....*....|....*....|....*....
gi 1822435973   520 AHMDKERMADEVEKVRLEMEQWRLKTSSM 548
Cdd:smart01071  113 LKKHRDKLKKEQKELRKKLDELEKEEKKK 141
 
Name Accession Description Interval E-value
SAM_liprin-alpha1,2,3,4_repeat2 cd09565
SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 ...
 1028-1093 2.40e-44

SAM domain of liprin-alpha1,2,3,4 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188964  Cd Length: 66  Bit Score: 154.17  E-value: 2.40e-44
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973 1028 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLKRL 1093
Cdd:cd09565      1 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRTHLKMVDSFHRTSLQYGILCLKRL 66
SAM_liprin-alpha1,2,3,4_repeat1 cd09562
SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 ...
 920-990 6.51e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188961  Cd Length: 71  Bit Score: 150.41  E-value: 6.51e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  920 FALWDGQTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 990
Cdd:cd09562      1 FALWNGPTVVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLT 71
SAM_liprin-alpha1,2,3,4_repeat3 cd09568
SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 ...
 1113-1184 9.66e-43

SAM domain of liprin-alpha1,2,3,4 proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin-alpha1,2,3,4 proteins is a protein-protein interaction domain. Liprin-alpha proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-beta proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance; in particular, liprin-alpha is involved in formation of the presynaptic active zone.


Pssm-ID: 188967  Cd Length: 72  Bit Score: 149.78  E-value: 9.66e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1113 DVMVWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIALALSLQIPTQNTQARQVLEREFNNLL 1184
Cdd:cd09568      1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
SAM_liprin-kazrin_repeat2 cd09495
SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1032-1091 4.20e-30

SAM domain of liprin/kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adheren junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188894  Cd Length: 60  Bit Score: 113.40  E-value: 4.20e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973 1032 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:cd09495      1 WWVTRWLDDIGLPQYKDQFHESLVDRRMLQYLTVNDLLVHLKVTSQLHHLSLKCGIHVLH 60
SAM_liprin-kazrin_repeat1 cd09494
SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 927-985 2.55e-27

SAM domain of liprin/kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of the SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188893  Cd Length: 58  Bit Score: 105.39  E-value: 2.55e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822435973  927 TVVAWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 985
Cdd:cd09494      1 RVCAWLEDFGLMP-MYVIFCRQNVKSGHTLLTLSDQEMEKELGIKNPLHRKKLRLAIKE 58
SAM_liprin-kazrin_repeat3 cd09496
SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of ...
 1121-1182 5.02e-25

SAM domain of liprin/kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of liprin/kazrin proteins is a protein-protein interaction domain. The long form of liprin/kazrin proteins contains three copies (repeats) of SAM domain. Liprin-alpha may form heterodimers with liprin-beta through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development and in axon guidance. In particular, liprin-alpha is involved in formation of the presynaptic active zone; liprin-beta is involved in the maintenance of lymphatic vessel integrity. Kazrins are involved in interplay between desmosomes and in adherens junctions; additionally they play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188895  Cd Length: 62  Bit Score: 99.15  E-value: 5.02e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1121 RVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIALALSLQIPTQNTQARQVLEREFNN 1182
Cdd:cd09496      1 RVIHWIRSIDLREYANNLVESGVHGGLLVLEPNFDHNTMALVLQIPPQKTQARRHLETEFNN 62
SAM_kazrin_repeat3 cd09570
SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin ...
 1113-1184 4.91e-20

SAM domain of kazrin proteins repeat 3; SAM (sterile alpha motif) domain repeat 3 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188969  Cd Length: 72  Bit Score: 85.19  E-value: 4.91e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1113 DVMVWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIALALSLQIPTQNTQARQVLEREFNNLL 1184
Cdd:cd09570      1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 923-985 1.79e-16

SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrin contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved into interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188963  Cd Length: 70  Bit Score: 75.18  E-value: 1.79e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822435973  923 WDGQTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 985
Cdd:cd09564      4 WKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 1027-1091 1.15e-15

SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin proteins is a protein-protein interaction domain. The long isoform of kazrins contains three copies (repeats) of SAM domain. Kazrin can interact with periplakin. It is involved in interplay between desmosomes and in adheren junctions. Additionally kazrins play a role in regulation of intercellular differentiation, junction assembly, and cytoskeletal organization.


Pssm-ID: 188966  Cd Length: 65  Bit Score: 72.44  E-value: 1.15e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973 1027 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:cd09567      1 QLDHTWVAREWLRDLGLPQYSEAFREHLVDGRVLDTLSRKDLEKHLGVSKKFHQASLLRGIELLR 65
SAM_liprin-beta1,2_repeat2 cd09566
SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 1027-1091 1.74e-15

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188965  Cd Length: 63  Bit Score: 71.96  E-value: 1.74e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973 1027 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:cd09566      1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1113-1184 1.24e-14

SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188968  Cd Length: 72  Bit Score: 69.79  E-value: 1.24e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1113 DVMVWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIALALSLQIPTQNTQARQVLEREFNNLL 1184
Cdd:cd09569      1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1027-1091 1.59e-14

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 69.22  E-value: 1.59e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973 1027 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 256-520 1.18e-13

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: 76.25  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQ 335
Cdd:TIGR02168  716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 REATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTkydpsspDDS 415
Cdd:TIGR02168  796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELI 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  416 TILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQ-----REKMNEEHNK--RLSDTVDKLLSESNER 488
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRReleelREKLAQLELRleGLEVRIDNLQERLSEE 948

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1822435973  489 LQLHLKERMSSLEEKNALTHELDNTRKQLEEA 520
Cdd:TIGR02168  949 YSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 254-542 2.30e-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: 72.01  E-value: 2.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  254 LLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLG 333
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  334 AQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPD 413
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  414 DSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEV-----LRARQREKMnEEHNKRLSDTVDKLLSESNER 488
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallnERASLEEAL-ALLRSELEELSEELRELESKR 910

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  489 LQL-----HLKERMSSLEEK-NALTHELDNTRKQLEEAHMDKERMADE-VEKVRLEMEQWR 542
Cdd:TIGR02168  911 SELrreleELREKLAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEAlENKIEDDEEEAR 971
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 920-984 3.55e-12

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 62.63  E-value: 3.55e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973  920 FALWDGQTVVAWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 984
Cdd:cd09563      1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 253-518 1.43e-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: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYL 332
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  333 GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpssp 412
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA------ 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  413 dDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESnERLQLH 492
Cdd:COG1196    401 -QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA-ALLEAA 478

                          250       260
                   ....*....|....*....|....*.
gi 1822435973  493 LKERMSSLEEKNALTHELDNTRKQLE 518
Cdd:COG1196    479 LAELLEELAEAAARLLLLLEAEADYE 504
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-531 3.29e-11

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 68.14  E-value: 3.29e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  151 LKALKSLFEHHKALDEKVRERLRVALERVAALEE---ELQATSQELMLLREQAAHAQRRAGDGSEDATEMEtpptQNSAE 227
Cdd:PRK02224   215 LAELDEEIERYEEQREQARETRDEADEVLEEHEErreELETLEAEIEDLRETIAETEREREELAEEVRDLR----ERLEE 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  228 LRPLTSHAKARvtngTGLRDIEgPGRLLELQDLLDKRSMEVaqmKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQ 307
Cdd:PRK02224   291 LEEERDDLLAE----AGLDDAD-AEAVEARREELEDRDEEL---RDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  308 --------------RDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERL 373
Cdd:PRK02224   363 eeaaeleseleearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  374 ELAEQklqqtMRKAETLPEVEAELAQrvaaltkydpsSPDDSTILEvklqdmsillrkAEERHGDIEERLRQLETQLEEK 453
Cdd:PRK02224   443 EEAEA-----LLEAGKCPECGQPVEG-----------SPHVETIEE------------DRERVEELEAELEDLEEEVEEV 494

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  454 NQEVLRARQREKMNEEHNKRLS--DTVDKLLSESNERLQlHLKERMSSL-EEKNALTHELDNTRKQLEEAHMDKERMADE 530
Cdd:PRK02224   495 EERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIE-EKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAREE 573


                   .
gi 1822435973  531 V 531
Cdd:PRK02224   574 V 574
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 267-545 3.78e-11

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: 67.79  E-value: 3.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  267 EVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNtKYQRDIREA-----MAQKDDMEERITTLEKRYLGAQREATSL 341
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREYegyelLKEKEALERQKEAIERQLASLEEELEKL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  342 HDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQklqqtmrkaETLPEVEAELAQRVAALTKYdpsspddstilEVK 421
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK---------EKIGELEAEIASLERSIAEK-----------ERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  422 LQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEV---------LRARQREKMN--EEHNKRLSDTVDKL------LSE 484
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdklteeyaeLKEELEDLRAelEEVDKEFAETRDELkdyrekLEK 396

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822435973  485 SNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ--WRLKT 545
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqeWKLEQ 459
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 253-406 5.81e-11

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: 64.18  E-value: 5.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLdkrsMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRyl 332
Cdd:COG1579      8 ALLDLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-- 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822435973  333 gaQREATSLHDLNDkLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRK----AETLPEVEAELAQRVAALTK 406
Cdd:COG1579     82 --LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAElaelEAELEEKKAELDEELAELEA 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 177-465 8.42e-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: 66.62  E-value: 8.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  177 ERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMEtpptQNSAELRPLTSHAKarvtngtglrdiegpgrLLE 256
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEE----LEELTAELQELEEK-----------------LEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  257 LQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQR 336
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  337 EATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDST 416
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  417 ILEVKLQDMSI-----LLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREK 465
Cdd:TIGR02168  432 EAELKELQAELeeleeELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 28-503 9.16e-11

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: 66.28  E-value: 9.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   28 RLMVGMLDERDRLLDA-LRDAQETIAHTQSRLHDVchdRDSLQRQLNS--ALPQEFAALTK-----------ELNACREQ 93
Cdd:pfam05483  267 RDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDI---KMSLQRSMSTqkALEEDLQIATKticqlteekeaQMEELNKA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   94 LLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSpagvsSEVEVLKALKS-----LFEHHKALDEKv 168
Cdd:pfam05483  344 KAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-----SELEEMTKFKNnkeveLEELKKILAED- 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  169 rERLRVALERVAALEEELQATSQELMLL---REQAAH---AQRRAGDGSED---------ATEMETPPTQNSAelrpLTS 233
Cdd:pfam05483  418 -EKLLDEKKQFEKIAEELKGKEQELIFLlqaREKEIHdleIQLTAIKTSEEhylkevedlKTELEKEKLKNIE----LTA 492

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  234 HAKARVTNGTGLRDiEGPGRLLEL----QDLLDKRSMEvAQMKERLGTLSARVGELEDDVDTARRDLI-----------K 298
Cdd:pfam05483  493 HCDKLLLENKELTQ-EASDMTLELkkhqEDIINCKKQE-ERMLKQIENLEEKEMNLRDELESVREEFIqkgdevkckldK 570

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  299 SEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLN---------------------DKLENELANTED 357
Cdd:pfam05483  571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENkalkkkgsaenkqlnayeikvNKLELELASAKQ 650

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  358 LLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYdpsspddstilevKLQDMSILLRKAEERHG 437
Cdd:pfam05483  651 KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH-------------KIAEMVALMEKHKHQYD 717

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  438 DI-EERLRQLET-QLEEKNQEVLRARQREKMNEEHNKRLSdtVDKLLS---ESNERLQLHLKERMSSLEEK 503
Cdd:pfam05483  718 KIiEERDSELGLyKNKEQEQSSAKAALEIELSNIKAELLS--LKKQLEiekEEKEKLKMEAKENTAILKDK 786
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
287-548 1.31e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.86  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  287 DDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLK------ 360
Cdd:PRK03918   158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKeleelk 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  361 ----QSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSIlLRKAEERH 436
Cdd:PRK03918   238 eeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  437 GDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDtvdkllsesnerlqlhLKERMSSLEEKNALTHELDNTRKQ 516
Cdd:PRK03918   317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE----------------LEERHELYEEAKAKKEELERLKKR 380

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1822435973  517 LEEAHMDK-ERMADEVEKVRLEMEQWRLKTSSM 548
Cdd:PRK03918   381 LTGLTPEKlEKELEELEKAKEEIEEEISKITAR 413
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 307-520 3.51e-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: 63.63  E-value: 3.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  307 QRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRK 386
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  387 AETLpevEAELAQRVAALTKYDPS-------SPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLR 459
Cdd:COG4942     99 LEAQ---KEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  460 ARQREKMNEEHNKRLSDTVD---KLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEA 520
Cdd:COG4942    176 LEALLAELEEERAALEALKAerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 177-590 3.98e-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: 3.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  177 ERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKARVtngtglrdiegpGRLLE 256
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK------------ERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  257 LQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARrdliksEEMNTKYQRD----IREAMAQKDDMEERITTLEKRYL 332
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE------EALNDLEARLshsrIPEIQAELSKLEEEVSRIEARLR 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  333 GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQrvaaltkydpssp 412
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRD------------- 879

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  413 ddstiLEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQL- 491
Cdd:TIGR02169  880 -----LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLe 954

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  492 -------HLKERMSSLEEKNALT-HELDNTRKQLEEAHMDKERMADEVEKVRLEMEQW-RLKTSSMVDPVIPRSHLGSTS 562
Cdd:TIGR02169  955 dvqaelqRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYeKKKREVFMEAFEAINENFNEI 1034

                          410       420
                   ....*....|....*....|....*....
gi 1822435973  563 DIRYSLGS-SVILEAPGDPFGSSAVLRRQ 590
Cdd:TIGR02169 1035 FAELSGGTgELILENPDDPFAGGLELSAK 1063
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-540 4.27e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 4.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  275 LGTLSARVGELEDDVDTARRdlikseemntkYqrdiREAMAQKDDMEERITTLEKRYLGAQREatslhdlndKLENELAN 354
Cdd:COG1196    195 LGELERQLEPLERQAEKAER-----------Y----RELKEELKELEAELLLLKLRELEAELE---------ELEAELEE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  355 TEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpsspdDSTILEVKLQDMSILLRKAEE 434
Cdd:COG1196    251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-------DIARLEERRRELEERLEELEE 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  435 RHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQL---HLKERMSSLEEKNALTHELD 511
Cdd:COG1196    324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEleeLAEELLEALRAAAELAAQLE 403

                          250       260
                   ....*....|....*....|....*....
gi 1822435973  512 NTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAE 432
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 170-483 4.56e-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: 64.32  E-value: 4.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  170 ERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKARVtngtgLRDIE 249
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL-----LEELN 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  250 gpgrllelQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEK 329
Cdd:TIGR02169  279 --------KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  330 RYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLE---------------LAEQKLQQTMRKAE------ 388
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkreinelkreldrLQEELQRLSEELADlnaaia 430

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  389 ----TLPEVEAEL---AQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRAR 461
Cdd:TIGR02169  431 gieaKINELEEEKedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510

                          330       340
                   ....*....|....*....|..
gi 1822435973  462 QREKMNEEHNKRLSDTVDKLLS 483
Cdd:TIGR02169  511 AVEEVLKASIQGVHGTVAQLGS 532
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-490 5.80e-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: 63.92  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  100 EIAELKAERNNTRLLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEkVRERLRVALERV 179
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELE--------------ELEEELEQLRKELEELSRQISA-LRKDLARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  180 AALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMEtpptQNSAELRPLTSHAKARVTNGTglrdiegpGRLLELQD 259
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE----AEIEELEAQIEQLKEELKALR--------EALDELRA 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  260 LLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREAT 339
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  340 SLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQT----MRKAETLPE---VEAELAQRVAALTKYDPSSP 412
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEeysLTLEEAEALENKIEDDEEEA 970

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  413 DDSTI-LEVKLQDMSILLRKAEERHGDIEERLRQLETQLEeknqEVLRARQR-----EKMNEEHNKRLSDTVDKLlsesN 486
Cdd:TIGR02168  971 RRRLKrLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKDTFDQV----N 1042


                   ....
gi 1822435973  487 ERLQ 490
Cdd:TIGR02168 1043 ENFQ 1046
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
165-542 9.03e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.14  E-value: 9.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  165 DEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSH---AKARVTN 241
Cdd:PRK02224   323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieeLRERFGD 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  242 GtglrdiegPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRdLIKSEEMNTKYQrDIREA--MAQKDD 319
Cdd:PRK02224   403 A--------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-LLEAGKCPECGQ-PVEGSphVETIEE 472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  320 MEERITTLEKRYLGAQREATSLHDLNDKLEnELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAEL-- 397
Cdd:PRK02224   473 DRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELea 551

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  398 ---AQRVAALTKYDPSspddstilevklQDMSILLRKAEERHGDIEERLRQLET------QLEEKNQEVLRARQREKMNE 468
Cdd:PRK02224   552 eaeEKREAAAEAEEEA------------EEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALA 619

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  469 EHNkrlsdtvdkllSESNERLQlHLKERMSSLEEknalthELDNTRkqLEEAHMDKERMADEVEKVRLEMEQWR 542
Cdd:PRK02224   620 ELN-----------DERRERLA-EKRERKRELEA------EFDEAR--IEEAREDKERAEEYLEQVEEKLDELR 673
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
78-545 2.61e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 2.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   78 QEFAALTKELNACREQLLEREEEIAELKAERNNTRLLLEHLEclvsRHERSLRMTVvkRQAQSPAGVSSEVEVLKALKSL 157
Cdd:PRK03918   231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK----KEIEELEEKV--KELKELKEKAEEYIKLSEFYEE 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  158 FEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPpTQNSAELRPLtshaKA 237
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERL----KK 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  238 RVTNGTglrdiegPGRLLELQDLLDKRSMEV----AQMKERLGTLSARVGELEDDVD----------TARRDLIKSEEMN 303
Cdd:PRK03918   380 RLTGLT-------PEKLEKELEELEKAKEEIeeeiSKITARIGELKKEIKELKKAIEelkkakgkcpVCGRELTEEHRKE 452

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  304 --TKYQRDIREAMAQKDDMEERITTLEKRYLgaqreatslhdlndKLENELANTEDLLKQSE--DKTRQLQERLE-LAEQ 378
Cdd:PRK03918   453 llEEYTAELKRIEKELKEIEEKERKLRKELR--------------ELEKVLKKESELIKLKElaEQLKELEEKLKkYNLE 518

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  379 KLQQTMRKAETLPEVEAELAQRVAALTKYdpsspddstiLEvKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVL 458
Cdd:PRK03918   519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKE----------LE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESV 587

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  459 -----RARQREKMNEEHNkRLSDTVDKL--LSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEV 531
Cdd:PRK03918   588 eeleeRLKELEPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666

                          490
                   ....*....|....
gi 1822435973  532 EKVRLEMEQWRLKT 545
Cdd:PRK03918   667 EYLELSRELAGLRA 680
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-469 2.83e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  177 ERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETppTQNSAELRpltSHAKARVTNGTGLRDIEGpgRLLE 256
Cdd:COG1196    213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL--EELEAELA---ELEAELEELRLELEELEL--ELEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  257 LQDLLDKRSMEVAQM-------KERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEK 329
Cdd:COG1196    286 AQAEEYELLAELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  330 RYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydp 409
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--- 442

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  410 sspdDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEE 469
Cdd:COG1196    443 ----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 269-540 5.50e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 5.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  269 AQMKERLGTLSARVGELEDDVDTARRDLikseemnTKYQRDIREAMAQKDDMEERITTLEKRYlgaqreatslhdlnDKL 348
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSEL-------RRIENRLDELSQELSDASRKIGEIEKEI--------------EQL 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  349 ENELANTEDLLKQSEDKTRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRVAALTKYDPSSPD-DSTILEVKLQDMSI 427
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELK----------ELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQA 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  428 LLRKAEERHGDIEERLRQLETQLEEKNQEvlRARQREKMNEEHNKRLSDTVDKllsESNERLQLHLKERmssLEEKNALT 507
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLE--KEYLEKEIQELQEQRIDLKEQI---KSIEKEIENLNGK---KEELEEEL 870

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1822435973  508 HELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELER 903
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
261-462 7.35e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.31  E-value: 7.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  261 LDKRSME--VAQMKERLGTLSarvgELEDDVDTARRDLIKSEEMNTKYQRdIREAMAQKDDMEERITTLekRYLGAQREA 338
Cdd:COG4913    218 LEEPDTFeaADALVEHFDDLE----RAHEALEDAREQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  339 TSLHDLNDKLENELANTEDLLKQSEDKTRQLQE---------------RLELAEQKLQQTMRKAETLPEVEAELAQRVAA 403
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREeldeleaqirgnggdRLEQLEREIERLERELEERERRRARLEALLAA 370

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  404 LTKYDPSSPDD--STILEVK--LQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEV--LRARQ 462
Cdd:COG4913    371 LGLPLPASAEEfaALRAEAAalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIasLERRK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 42-539 1.05e-08

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: 60.08  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   42 DALRDAQETIAHTQSRLHDVCHDRDSLQRQLNS------ALPQEFAALTKELNACREQLLEREEEIAELKAERNNTRlll 115
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR--- 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  116 EHLECLVSRHERSLRMtvVKRQAQSPAGVSSEVEVLKA-LKSLFEHHKALDE------------------------KVRE 170
Cdd:TIGR02169  392 EKLEKLKREINELKRE--LDRLQEELQRLSEELADLNAaIAGIEAKINELEEekedkaleikkqewkleqlaadlsKYEQ 469

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  171 RLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGS-------------------------EDATEMET------ 219
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkasiqgvhgtvaqlgsvgeRYATAIEVaagnrl 549

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  220 -----------------------------PPTQNSAELRPLTSHAKARVTN---------------------GTGL---- 245
Cdd:TIGR02169  550 nnvvveddavakeaiellkrrkagratflPLNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgDTLVvedi 629

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  246 ---RDIEGPGRLLELQ-DLLDK-------------RSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQR 308
Cdd:TIGR02169  630 eaaRRLMGKYRMVTLEgELFEKsgamtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  309 DIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERL------------ELA 376
Cdd:TIGR02169  710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndleaRLS 789

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  377 EQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQE 456
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  457 VLRARQREKMNEEHNKRLSDTVDKL-------------LSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEE---A 520
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELeaqlrelerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeE 949

                          650
                   ....*....|....*....
gi 1822435973  521 HMDKERMADEVEKVRLEME 539
Cdd:TIGR02169  950 ELSLEDVQAELQRVEEEIR 968
PTZ00121 PTZ00121
MAEBL; Provisional
 135-540 2.40e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  135 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERVAALEE-----ELQATSQElmllREQAAHAQRRA 207
Cdd:PTZ00121  1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEakkadEAKKKAEE----AKKADEAKKKA 1492

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  208 GDGSEDATEME--TPPTQNSAELRPLTSHAKARvtngtGLRDIEGPGRLLELQDLLDKRSMEVAQMKERLgtlsaRVGEL 285
Cdd:PTZ00121  1493 EEAKKKADEAKkaAEAKKKADEAKKAEEAKKAD-----EAKKAEEAKKADEAKKAEEKKKADELKKAEEL-----KKAEE 1562

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  286 EDDVDTARRdlikSEEMNTKYQRDIREA-MAQKDDMEERITTLEKRYLGAQREATslhdlndKLENELANTEDLLKQSED 364
Cdd:PTZ00121  1563 KKKAEEAKK----AEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAK-------KAEEAKIKAEELKKAEEE 1631

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  365 KTRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMsillRKAEERHGDIEERLR 444
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEK-----KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAK 1702

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  445 QLEtQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERmsslEEKNALTHELDNTRKQLEEAHMDK 524
Cdd:PTZ00121  1703 KAE-ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE----EEKKKIAHLKKEEEKKAEEIRKEK 1777

                          410       420
                   ....*....|....*....|.
gi 1822435973  525 ERMADEV-----EKVRLEMEQ 540
Cdd:PTZ00121  1778 EAVIEEEldeedEKRRMEVDK 1798
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 253-539 2.52e-08

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 57.77  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYL 332
Cdd:pfam19220   49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLA 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  333 GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSP 412
Cdd:pfam19220  129 AETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATR 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  413 DDSTILEVKLQDMSILLRKAEerhgdieerlRQLETQLEEKNQEvlRARQREKMnEEHNKRLSDTvDKLLSESNERLQ-- 490
Cdd:pfam19220  209 ARLRALEGQLAAEQAERERAE----------AQLEEAVEAHRAE--RASLRMKL-EALTARAAAT-EQLLAEARNQLRdr 274

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1822435973  491 ---LHLKERMssLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEME 539
Cdd:pfam19220  275 deaIRAAERR--LKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELE 324
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 920-986 2.95e-08

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 51.53  E-value: 2.95e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973   920 FALWDGQTVVAWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEM 986
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
37-500 3.56e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 3.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   37 RDRLLDALRDAQETIAHTQSRLHDVCHDR-DSLQRQLNSA--LPQEFAALTKELNACREQLLEREEEIAELKAERNNTRL 113
Cdd:COG4717     44 RAMLLERLEKEADELFKPQGRKPELNLKElKELEEELKEAeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  114 LLEHLECLVSRHE------------RSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERVAA 181
Cdd:COG4717    124 LLQLLPLYQELEAleaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  182 LEEELQATSQELMLLREQAAHAQRRAgDGSEDATEMETPPTQNSAELRPLTSHAKARVTNGTGLRDIEGPGRLLELQDL- 260
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEEL-EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLv 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  261 ----------LDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKR 330
Cdd:COG4717    283 lgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  331 YLGAQREATSLHDLNDKLENELANTEDLLKQSEDKtRQLQERLELAEQKLQQ------TMRKAETLPEVEAELAQrvaal 404
Cdd:COG4717    363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEE----- 436

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  405 tkydpsspddstiLEVKLQDMSILLRKAEERHGDIEERLRQLETQ--LEEKNQEVLRARQREKMNEEHNKRL---SDTVD 479
Cdd:COG4717    437 -------------LEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALklaLELLE 503

                          490       500
                   ....*....|....*....|.
gi 1822435973  480 KLLSESNERLQLHLKERMSSL 500
Cdd:COG4717    504 EAREEYREERLPPVLERASEY 524
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 249-408 4.04e-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: 55.70  E-value: 4.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  249 EGPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEE--MNTKYQRDIREAMAQKDDMEERITT 326
Cdd:COG1579     28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISD 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  327 LEKRYLGAQREAtslhdlnDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQtmrKAETLPEVEAELAQRVAA--L 404
Cdd:COG1579    108 LEDEILELMERI-------EELEEELAELEAELAELEAELEEKKAELDEELAELEA---ELEELEAEREELAAKIPPelL 177


                   ....
gi 1822435973  405 TKYD 408
Cdd:COG1579    178 ALYE 181
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 256-540 4.56e-08

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: 57.72  E-value: 4.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAmaqkddmEERITTLEKrylgaq 335
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK-------QNEIEKLKK------ 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 rEATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDpsspdds 415
Cdd:TIGR04523  378 -ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD------- 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  416 TILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNErlqlhLKE 495
Cdd:TIGR04523  450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-----LKE 524

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1822435973  496 RMSSLE-EKNALTHELDNTRKQLEEahMDKERMADEVEKVRLEMEQ 540
Cdd:TIGR04523  525 KIEKLEsEKKEKESKISDLEDELNK--DDFELKKENLEKEIDEKNK 568
mukB PRK04863
chromosome partition protein MukB;
169-519 5.11e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 57.66  E-value: 5.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  169 RERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELrpltshakARVTNGtgLRDI 248
Cdd:PRK04863   278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL--------NLVQTA--LRQQ 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  249 EGPGR----LLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARrdlikseemntkyqrdireamAQKDDMEERI 324
Cdd:PRK04863   348 EKIERyqadLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELK---------------------SQLADYQQAL 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  325 TTLEKR---YLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTmRKAETLPEVEAELAQRV 401
Cdd:PRK04863   407 DVQQTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRKI 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  402 AALTkyDPSSPDDSTIlevklqdmSILLRKAEERHGDieERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLS------ 475
Cdd:PRK04863   486 AGEV--SRSEAWDVAR--------ELLRRLREQRHLA--EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGknldde 553

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1822435973  476 DTVDKLLSESNERLQlHLKERMSSL-EEKNALTHELDNTRKQLEE 519
Cdd:PRK04863   554 DELEQLQEELEARLE-SLSESVSEArERRMALRQQLEQLQARIQR 597
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1036-1091 5.91e-08

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 50.76  E-value: 5.91e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973  1036 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 35-540 6.09e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 6.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   35 DERDRLLDALRDAQETIAHTQSRLHDVCHDRDSLQRQLNSALpQEFAALTKELNACREQLLEREEEIAELKAERNNTRLL 114
Cdd:COG1196    274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  115 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEkVRERLRVALERVAALEEELQATSQELM 194
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALA 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  195 LLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSME------- 267
Cdd:COG1196    432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvk 511

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  268 VAQMKERLGTLSARVGELEDDVDTARRDLIKSEEmntkyQRDIREAMAQKDDMEERITTLEKRYLG----------AQRE 337
Cdd:COG1196    512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIEYLKAAKAGratflpldkiRARA 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  338 ATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRVAALTKYDPSSPDDSTI 417
Cdd:COG1196    587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA----ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  418 LEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLsdtvdklLSESNERLQLHLKERM 497
Cdd:COG1196    663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE-------ELEEEALEEQLEAERE 735

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1822435973  498 SSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:COG1196    736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-480 1.17e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   21 QDDASFERLMVGMLDERDRLLDALRDAQETIAHTQSRlhdvchdRDSLQRQLNSALpqefAALTKELNACREQLLEREEE 100
Cdd:COG1196    400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEE-------EEEEEEALEEAA----EEEAELEEEEEALLELLAEL 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  101 IAELKAERNNTRLLLEHLECLVSRHERSLRMtvvkrqAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALER 178
Cdd:COG1196    469 LEEAALLEAALAELLEELAEAAARLLLLLEA------EADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEA 542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  179 VAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKArvtNGTGLRDIEGPGRLLELQ 258
Cdd:COG1196    543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV---DLVASDLREADARYYVLG 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  259 DLLDKRSMEVAQ-------MKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRY 331
Cdd:COG1196    620 DTLLGRTLVAARleaalrrAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  332 LGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpss 411
Cdd:COG1196    700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER----- 774

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  412 pddstilevKLQDM-SILLRkAEERHGDIEERLRQLETQLEeknqEVLRARQR-----EKMNEEHNKRLSDTVDK 480
Cdd:COG1196    775 ---------EIEALgPVNLL-AIEEYEELEERYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
PTZ00121 PTZ00121
MAEBL; Provisional
 135-512 2.04e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  135 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE---KVRERLRVALERVAALEEELQAtsQELMLLREQAAHAQRRAGDGS 211
Cdd:PTZ00121  1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkKAEEAKKKADEAKKAAEAKKKA--DEAKKAEEAKKADEAKKAEEA 1533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  212 EDATEMETPPTQNSA-------ELRPLTSHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGE 284
Cdd:PTZ00121  1534 KKADEAKKAEEKKKAdelkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  285 LEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATslhdlndKLENELANTEDLLKQSED 364
Cdd:PTZ00121  1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK-------KAEEDKKKAEEAKKAEED 1686

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  365 KTRQLQERLELAEQKlqqtmRKAETLPEVEAELAQRVAALTKYDpsspddstilEVKLQDMSILLRKAEERHGDIEErlr 444
Cdd:PTZ00121  1687 EKKAAEALKKEAEEA-----KKAEELKKKEAEEKKKAEELKKAE----------EENKIKAEEAKKEAEEDKKKAEE--- 1748

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822435973  445 qLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDN 512
Cdd:PTZ00121  1749 -AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
323-540 2.29e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  323 RITTLEKRYLGAQREATSLHDLNDKLENELANTEDLlkqsEDKTRQLQERLelaEQKLQQTMRKAETLPEVEAELAQRVA 402
Cdd:PRK03918   156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENI----EELIKEKEKEL---EEVLREINEISSELPELREELEKLEK 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  403 ALTKYDPsspddstiLEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEV--LRARQRE---------------K 465
Cdd:PRK03918   229 EVKELEE--------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKElkelkekaeeyiklsE 300

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  466 MNEEHNKRLSDtVDKLLSESNERLQlHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:PRK03918   301 FYEEYLDELRE-IEKRLSRLEEEIN-GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 144-469 2.77e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 2.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  144 VSSEVEVLKALKSLFEHHKALDEKVRE-RLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPT 222
Cdd:TIGR02169  196 KRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  223 QNSAELRPLTSHAKARVTngTGLRDIEGPGRLLELQDLLDKRSME-----VAQMKERLGTLSARVGELEDDVDTARRDLI 297
Cdd:TIGR02169  276 ELNKKIKDLGEEEQLRVK--EKIGELEAEIASLERSIAEKERELEdaeerLAKLEAEIDKLLAEIEELEREIEEERKRRD 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  298 K--------SEEMNTKYQR------DIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDK-------LENELANTE 356
Cdd:TIGR02169  354 KlteeyaelKEELEDLRAEleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlseeladLNAAIAGIE 433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  357 DLLKQSEDKTRQLQERLELAEQKLQQTMRKaetlpeveaelaqrvaaltkydpsspddstilevklqdmsilLRKAEERH 436
Cdd:TIGR02169  434 AKINELEEEKEDKALEIKKQEWKLEQLAAD------------------------------------------LSKYEQEL 471

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1822435973  437 GDIEERLRQLETQLEEKNQEVLRARQREKMNEE 469
Cdd:TIGR02169  472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
PTZ00121 PTZ00121
MAEBL; Provisional
 148-533 4.75e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 4.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  148 VEVLKALkslfEHHKALDEKVRERLRVAlERVAALEEELQATSqelmllrEQAAHAQRRAGDGSEDATEME-TPPTQNSA 226
Cdd:PTZ00121  1185 EEVRKAE----ELRKAEDARKAEAARKA-EEERKAEEARKAED-------AKKAEAVKKAEEAKKDAEEAKkAEEERNNE 1252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  227 ELRPLTSHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSMEVAQMKERLgtlsARVGELEDDVDTARrdliKSEEMNTKY 306
Cdd:PTZ00121  1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK----KKADEAKKKAEEAK----KADEAKKKA 1324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  307 QRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQE--RLELAEQKLQQTM 384
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDK 1404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  385 RKAETLPEVEAELAQRVAALTKYDPSSPDDStiLEVKLQDMsillRKAEERHGDIEERLR--QLETQLEEKNQ-EVLRAR 461
Cdd:PTZ00121  1405 KKADELKKAAAAKKKADEAKKKAEEKKKADE--AKKKAEEA----KKADEAKKKAEEAKKaeEAKKKAEEAKKaDEAKKK 1478

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822435973  462 QREKMNEEHNKRLSDTVDKLLSESNERLQLHLK-ERMSSLEEKNalthELDNTRKQLEEAHMDKERMADEVEK 533
Cdd:PTZ00121  1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKaDEAKKAEEAK----KADEAKKAEEAKKADEAKKAEEKKK 1547
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-540 4.76e-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: 54.68  E-value: 4.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   35 DERDRLLDALRDAQETIAHTQSRLhDVCHDRDSLQRQLNSALPQEFAALTKELNACREQLLEREEEIAELKAERNNTRLL 114
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAEL-QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  115 LEHLECLVSRHERSLRMT------VVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERVAALEEELQA 188
Cdd:TIGR02168  318 LEELEAQLEELESKLDELaeelaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  189 TSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSMEV 268
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  269 AQMKERLGTLSARVGELEDD------------------------------------------------------------ 288
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLqenlegfsegvkallknqsglsgilgvlselisvdegyeaaieaalggrlqavvvenlna 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  289 --------------------VDTARRDLIKSEEMN-------------------TKYQR-------------DIREAMAQ 316
Cdd:TIGR02168  558 akkaiaflkqnelgrvtflpLDSIKGTEIQGNDREilkniegflgvakdlvkfdPKLRKalsyllggvlvvdDLDNALEL 637

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  317 --KDDMEERITTLEKRYLGA------QREATSLHDLNdkLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAE 388
Cdd:TIGR02168  638 akKLRPGYRIVTLDGDLVRPggvitgGSAKTNSSILE--RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  389 TLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQR-EKMN 467
Cdd:TIGR02168  716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLK 795

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822435973  468 EEHNkrlsdTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:TIGR02168  796 EELK-----ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1116-1185 4.95e-07

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 48.06  E-value: 4.95e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  1116 VWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIalalsLQIPTQNTQARQVLEREFNNLLA 1185
Cdd:smart00454    3 QWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDL-----KELGITKLGHRKKILKAIQKLKE 67
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
314-540 5.95e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 5.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  314 MAQKDDmeeRITTLEKRYLG----AQREAtsLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAEt 389
Cdd:COG4913    589 RHEKDD---RRRIRSRYVLGfdnrAKLAA--LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID- 662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  390 LPEVEAELAQRVAALTKYDPSSPDdstilevklqdmsilLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEE 469
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDD---------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  470 HNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAhmdKERMADEVEKVRLEMEQ 540
Cdd:COG4913    728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL---RARLNRAEEELERAMRA 795
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
317-535 8.69e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 8.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  317 KDDMEERITTLEKRYlgAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAE 396
Cdd:PRK02224   182 LSDQRGSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  397 LAQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGD----------IEERLRQLETQLEEKNQEVLRARQREKM 466
Cdd:PRK02224   260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQA 339

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822435973  467 NEEHNKRLSDTVDKLLSESNErlqlhLKERMSSLEEknalthELDNTRKQLEEAHMDKERMADEVEKVR 535
Cdd:PRK02224   340 HNEEAESLREDADDLEERAEE-----LREEAAELES------ELEEAREAVEDRREEIEELEEEIEELR 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-399 9.86e-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: 53.52  E-value: 9.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   45 RDAQETIAHTQ---SRLHDVCHDR----DSLQRQLNSAlpQEFAALTKELNAcrEQLLEREEEIAELKAERNNTRLLLEH 117
Cdd:TIGR02168  175 KETERKLERTRenlDRLEDILNELerqlKSLERQAEKA--ERYKELKAELRE--LELALLVLRLEELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  118 LECLVSRHERSLRMTvvkrqaqspagvSSEVEVLKALKSlfEHHKALDEkVRERLRVALERVAALEEELQATSQELMLLR 197
Cdd:TIGR02168  251 AEEELEELTAELQEL------------EEKLEELRLEVS--ELEEEIEE-LQKELYALANEISRLEQQKQILRERLANLE 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  198 -------EQAAHAQRRAGDGSEDATEMEtpptQNSAELRPLTSHAKARVTNGTGLRDiEGPGRLLELQDLLDKRSMEVAQ 270
Cdd:TIGR02168  316 rqleeleAQLEELESKLDELAEELAELE----EKLEELKEELESLEAELEELEAELE-ELESRLEELEEQLETLRSKVAQ 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  271 MKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAmaQKDDMEERITTLEKRYLGAQREATSLHDLNDKLEN 350
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELRE 468

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1822435973  351 ELANTEDLLKQSEDKTRQLQERLELaeqkLQQTMRKAETLPEVEAELAQ 399
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDS----LERLQENLEGFSEGVKALLK 513
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1036-1087 1.44e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 46.46  E-value: 1.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1822435973 1036 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRTSLQYGI 1087
Cdd:cd09487      4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-544 2.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   78 QEFAALTKELNACREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMtVVKRQAQSPAGVSSEVEVLKALKSL 157
Cdd:COG1196    239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEER 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  158 FEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAgdgSEDATEMEtpptqnsAELRPLTSHAKA 237
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELA-------EAEEELEELAEE 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  238 RVTNGTglrdiegpgRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQK 317
Cdd:COG1196    388 LLEALR---------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  318 DDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKL----------------- 380
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayea 538

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  381 -----------QQTMRKAETLPEVEAELAQRVAA------LTKYDPSSPDDSTILEVKLQDMSILLRKAEERHgdiEERL 443
Cdd:COG1196    539 aleaalaaalqNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREA---DARY 615

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  444 RQLETQLEEKNQEVLRARQREKMNEEHNKRlsdtvdkLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMD 523
Cdd:COG1196    616 YVLGDTLLGRTLVAARLEAALRRAVTLAGR-------LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688

                          490       500
                   ....*....|....*....|.
gi 1822435973  524 KERMADEVEKVRLEMEQWRLK 544
Cdd:COG1196    689 AEEELELEEALLAEEEEEREL 709
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 185-540 3.04e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.04  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  185 ELQATSQELMLLREQAAHAQRRAGDGSEDATEMetppTQNSaelrpltshakarvtngtgLRDIEGPGRLLElqDLLDKR 264
Cdd:pfam15921  114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ----LQNT-------------------VHELEAAKCLKE--DMLEDS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  265 SMEVAQMKERL----GTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQK-DDMEERITTLEKRYLGAQREat 339
Cdd:pfam15921  169 NTQIEQLRKMMlsheGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKIlRELDTEISYLKGRIFPVEDQ-- 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  340 sLHDLNDKLENELantEDLLKQSEDKTRQLQERLELAEQKLQQTMRKA-------ETLPEVEAELAQRVAALTKYDPSSp 412
Cdd:pfam15921  247 -LEALKSESQNKI---ELLLQQHQDRIEQLISEHEVEITGLTEKASSArsqansiQSQLEIIQEQARNQNSMYMRQLSD- 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  413 ddstiLEVKLQDMSILLRKAEERHgdiEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSEsnerlqLH 492
Cdd:pfam15921  322 -----LESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD------LH 387

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822435973  493 LKERMSSLEEK-----------NALTheLDNTRKQLEEAHMDKERMADEVEKVRLE----MEQ 540
Cdd:pfam15921  388 KREKELSLEKEqnkrlwdrdtgNSIT--IDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMER 448
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 253-548 3.47e-06

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: 51.36  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDtarrdlIKSEEMNTkYQRDIREAMAQKDDMEERITTLEKRYL 332
Cdd:pfam10174  353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD------VKERKINV-LQKKIENLQEQLRDKDKQLAGLKERVK 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  333 GAQREATSLHDLNDKLENELANTEDLLKQ-SEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALT--KYDP 409
Cdd:pfam10174  426 SLQTDSSNTDTALTTLEEALSEKERIIERlKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEHA 505

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  410 SSPDDSTI------------LEVKLQDMSIL---LRKAEE------RHGDIEERLRQLETQLEEKNQEVLRARQ------ 462
Cdd:pfam10174  506 SSLASSGLkkdsklksleiaVEQKKEECSKLenqLKKAHNaeeavrTNPEINDRIRLLEQEVARYKEESGKAQAeverll 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  463 ---REKMNEEHNKrlsdtvDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQ-LEEAHMDKERMAD--------- 529
Cdd:pfam10174  586 gilREVENEKNDK------DKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlLEEARRREDNLADnsqqlqlee 659

                          330       340
                   ....*....|....*....|..
gi 1822435973  530 ---EVEKVRLEMEQWRLKTSSM 548
Cdd:pfam10174  660 lmgALEKTRQELDATKARLSST 681
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-545 3.69e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYL 332
Cdd:COG4372     46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  333 GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQtMRKAETLPEVEAELAQ-RVAALTKYDPSS 411
Cdd:COG4372    126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEaNRNAEKEEELAE 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  412 PDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQL 491
Cdd:COG4372    205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  492 HLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKT 545
Cdd:COG4372    285 LEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
169-408 3.74e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  169 RERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDAtemETPPTQnsAELRPLTSHakarvtngtgLRDI 248
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI---DVASAE--REIAELEAE----------LERL 680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  249 E-GPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEmntkyqrdiREAMAQKDDMEERITTL 327
Cdd:COG4913    681 DaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---------RLEAAEDLARLELRALL 751

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  328 EKRYLGAQREatslhdlndklenelANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKA-ETLPEVEAELAQRVAALTK 406
Cdd:COG4913    752 EERFAAALGD---------------AVERELRENLEERIDALRARLNRAEEELERAMRAFnREWPAETADLDADLESLPE 816


                   ..
gi 1822435973  407 YD 408
Cdd:COG4913    817 YL 818
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 304-540 4.33e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  304 TKYQRDIREAMAQKDDMEERITTLE---------KRYLGAQRE-ATSLHDLNDKLEN-ELANTEDLLKQSEDKTRQLQER 372
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLEdilnelerqLKSLERQAEkAERYKELKAELRElELALLVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  373 LELAEQKLQQTMRKAEtlpEVEAELAQRVAALTKYDpsspDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEE 452
Cdd:TIGR02168  248 LKEAEEELEELTAELQ---ELEEKLEELRLEVSELE----EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  453 KNQEVLRARQRekmNEEHNKRLSDTVDKLLSESNERLQLHLKermssLEEKNALTHELDNTRKQLEEAHmdkERMADEVE 532
Cdd:TIGR02168  321 LEAQLEELESK---LDELAEELAELEEKLEELKEELESLEAE-----LEELEAELEELESRLEELEEQL---ETLRSKVA 389


                   ....*...
gi 1822435973  533 KVRLEMEQ 540
Cdd:TIGR02168  390 QLELQIAS 397
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 256-542 4.40e-06

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: 51.20  E-value: 4.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDdmeerittlekrylgaq 335
Cdd:TIGR00606  574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD----------------- 636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 reatslhdlndkLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEV-------EAELAQRVAALTKYD 408
Cdd:TIGR00606  637 ------------EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVcqrvfqtEAELQEFISDLQSKL 704

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  409 PSSPDDSTILEVKL----QDMSILLRKAEERHGDIEERLRQLEtQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSE 484
Cdd:TIGR00606  705 RLAPDKLKSTESELkkkeKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973  485 SN---------ERLQLHLKERMSSLEEKNALTHELDNTRkQLEEAHMDKERMADEVEKVRLEMEQWR 542
Cdd:TIGR00606  784 AKvcltdvtimERFQMELKDVERKIAQQAAKLQGSDLDR-TVQQVNQEKQEKQHELDTVVSKIELNR 849
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 256-540 4.44e-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: 51.17  E-value: 4.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYlgaQ 335
Cdd:TIGR04523  215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL---N 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 REATSLHDLNDKLENELANT-EDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLP-----------EVEAELAQR--- 400
Cdd:TIGR04523  292 QLKSEISDLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKkeltnsesensEKQRELEEKqne 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  401 VAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLS--DTV 478
Cdd:TIGR04523  372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqDSV 451

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822435973  479 DKLLSESNERLQLHLKERMSSLE-EKNALTHELDNTRKQLEEahmdKERMADEVEKVRLEMEQ 540
Cdd:TIGR04523  452 KELIIKNLDNTRESLETQLKVLSrSINKIKQNLEQKQKELKS----KEKELKKLNEEKKELEE 510
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 256-548 4.68e-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: 51.33  E-value: 4.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKE---RLGTLSARVGELEDDVDTARRDLIKSEemntKYQRDIREAM-AQKDDMEERI-TTLEKR 330
Cdd:pfam01576  244 ELQAALARLEEETAQKNNalkKIRELEAQISELQEDLESERAARNKAE----KQRRDLGEELeALKTELEDTLdTTAAQQ 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  331 YLGAQREaTSLHDLNDKLENELANTEDLLKQSEDKTRQ----LQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTK 406
Cdd:pfam01576  320 ELRSKRE-QEVTELKKALEEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  407 YDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRArqrEKMNEEHNKRLSdTVDKLLSESN 486
Cdd:pfam01576  399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA---EGKNIKLSKDVS-SLESQLQDTQ 474

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973  487 ERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSM 548
Cdd:pfam01576  475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 258-488 5.60e-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: 50.15  E-value: 5.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  258 QDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRylgaqre 337
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE------- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  338 atsLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTI 417
Cdd:COG4942     92 ---IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822435973  418 LEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNER 488
Cdd:COG4942    169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
PTZ00121 PTZ00121
MAEBL; Provisional
 159-544 5.71e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 5.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  159 EHHKALDEKVRERLRVALERVAALE---EELQATSQELMLLREQ---AAHAQRRAGDGSEDATEMetpptQNSAELRPLT 232
Cdd:PTZ00121  1346 EAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADEL-----KKAAAAKKKA 1420

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  233 SHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSMEVAQMKE--RLGTLSARVGELEDDVDTARR--DLIKSEEMNTKYQR 308
Cdd:PTZ00121  1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKAD 1500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  309 DIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLND-------KLENELANTEDLLKQSEDKTRQLQERlelAEQKLQ 381
Cdd:PTZ00121  1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekKKADELKKAEELKKAEEKKKAEEAKK---AEEDKN 1577

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  382 QTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEErLRQLETQLEEKNQEVLRAR 461
Cdd:PTZ00121  1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAE 1656

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  462 QREKMNEEHNKRLSDTvDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQW 541
Cdd:PTZ00121  1657 EENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735


                   ...
gi 1822435973  542 RLK 544
Cdd:PTZ00121  1736 KKE 1738
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 357-540 5.75e-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: 50.15  E-value: 5.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  357 DLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKydpsspddstilevklqdmsiLLRKAEERH 436
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---------------------RIRALEQEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  437 GDIEERLRQLETQLE--EKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESN--------ERLQLHLKERMSSLEEKNAL 506
Cdd:COG4942     79 AALEAELAELEKEIAelRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRAD 158

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1822435973  507 THELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:COG4942    159 LAELAALRAELEAERAELEALLAELEEERAALEA 192
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 179-532 5.95e-06

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: 50.46  E-value: 5.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  179 VAALEEELQATSQELMLLREQAAHaqrragdgSEDATEMETPPTQNSAELRPLTSHAKA---RVTNGTG---LRDIEGPG 252
Cdd:pfam05622   23 VSLLQEEKNSLQQENKKLQERLDQ--------LESGDDSGTPGGKKYLLLQKQLEQLQEenfRLETARDdyrIKCEELEK 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQ---DLLDKRSMEVAQMKERLGTL---SARVGELEDDVDTARR------DLIK----SEEMNTKYqrdireaMAQ 316
Cdd:pfam05622   95 EVLELQhrnEELTSLAEEAQALKDEMDILresSDKVKKLEATVETYKKkledlgDLRRqvklLEERNAEY-------MQR 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  317 KDDMEERIttleKRY--LGAQREATS--LHDLNDKLENELANTEDLlkQSEDKtrQLQERLELAEQKLQQTMRKAETLPE 392
Cdd:pfam05622  168 TLQLEEEL----KKAnaLRGQLETYKrqVQELHGKLSEESKKADKL--EFEYK--KLEEKLEALQKEKERLIIERDTLRE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  393 VEAEL-------AQRVAALTKYDPSSPDDSTI------LEVK-----LQDMSILLRKAEErhGDIEERLRQLETQLEEKN 454
Cdd:pfam05622  240 TNEELrcaqlqqAELSQADALLSPSSDPGDNLaaeimpAEIReklirLQHENKMLRLGQE--GSYRERLTELQQLLEDAN 317

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822435973  455 qevlraRQREKMNEEHnkRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVE 532
Cdd:pfam05622  318 ------RRKNELETQN--RLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-469 9.42e-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: 50.07  E-value: 9.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  166 EKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPL---TSHAKARVTNG 242
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripEIQAELSKLEE 805

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  243 TgLRDIEGpgRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEE 322
Cdd:TIGR02169  806 E-VSRIEA--RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  323 RITTLEKrylgaQReatslhdlnDKLENElantedlLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVA 402
Cdd:TIGR02169  883 RLGDLKK-----ER---------DELEAQ-------LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973  403 ALTKYDPSSPDDSTI------LEVKLQDMSILLRKAEERHGDIEERLRQLETQL----EEKNQEVLRARQREKMNEE 469
Cdd:TIGR02169  942 EDEEIPEEELSLEDVqaelqrVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRakleEERKAILERIEEYEKKKRE 1018
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 284-530 1.88e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  284 ELEDDVDT-----ARRDLIKSEEMNTKYQRD---IREAMAQKDDMEE----RITTLEKRYLGAQRE----ATSLHDLNDK 347
Cdd:PRK04778    90 EAEELNDKfrfrkAKHEINEIESLLDLIEEDieqILEELQELLESEEknreEVEQLKDLYRELRKSllanRFSFGPALDE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  348 LENELANTEDLLKQSEDKT-----RQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAA-----------LTK--YD- 408
Cdd:PRK04778   170 LEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDqlqelkagyreLVEegYHl 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  409 PSSPDDSTI--LEVKLQDMSILLR-----KAEERHGDIEERLRQLETQLEeknQEVlRARQREkmnEEHNKRLSDTVDKl 481
Cdd:PRK04778   250 DHLDIEKEIqdLKEQIDENLALLEeldldEAEEKNEEIQERIDQLYDILE---REV-KARKYV---EKNSDTLPDFLEH- 321

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973  482 LSESNERLQL---HLKERM----SSLEEKNALTHELDNTRKQLEEahmDKERMADE 530
Cdd:PRK04778   322 AKEQNKELKEeidRVKQSYtlneSELESVRQLEKQLESLEKQYDE---ITERIAEQ 374
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
135-541 1.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  135 KRQAQSPAGVSSEVEVL-KALKSLFEHHKALDEKVRERLRVAlERVAALEEELQATSQELMLLrEQAAHAQRRAGDGSED 213
Cdd:COG4717     60 KPQGRKPELNLKELKELeEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKL-EKLLQLLPLYQELEAL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  214 ATEMETPPTQnsaeLRPLTSHAKARVTNGTGLRDIEGpgRLLELQDLLDKRSMEV-AQMKERLGTLSARVGELEDDVDTA 292
Cdd:COG4717    138 EAELAELPER----LEELEERLEELRELEEELEELEA--ELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAEL 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  293 RRDL--IKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYL--GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQ 368
Cdd:COG4717    212 EEELeeAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  369 LQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDStilevkLQDMSILLRKAEERHGDIEERLRQLET 448
Cdd:COG4717    292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE------LLELLDRIEELQELLREAEELEEELQL 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  449 QLEEKNQEVLRARQREKMNEEHNKRLSDTVD-----KLLSESNERLQLHLKERMSSLE--EKNALTHELDNTRKQLEEAH 521
Cdd:COG4717    366 EELEQEIAALLAEAGVEDEEELRAALEQAEEyqelkEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELE 445

                          410       420
                   ....*....|....*....|
gi 1822435973  522 MDKERMADEVEKVRLEMEQW 541
Cdd:COG4717    446 EELEELREELAELEAELEQL 465
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
327-706 1.91e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  327 LEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKaetlpevEAELAQRVAALTK 406
Cdd:COG4717     51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE-------LEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  407 ydpsspddstilEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESN 486
Cdd:COG4717    124 ------------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  487 ERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSMVDPVIprSHLGSTSDIRY 566
Cdd:COG4717    192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL--LALLGLGGSLL 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  567 SLGSSV---ILEAPGDPFGSSAVLRRQKGRLSALRDE---PGKVQTLNEQEWQRMQQA-------------GVLASVAQA 627
Cdd:COG4717    270 SLILTIagvLFLVLGLLALLFLLLAREKASLGKEAEElqaLPALEELEEEELEELLAAlglppdlspeellELLDRIEEL 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  628 FESETEASDQEDDRETIFSS---ADLLSPSGHSDAQTL--ALMLQEQLDAINNEIRLIQEEkesTEQRAEEIESRVGSGS 702
Cdd:COG4717    350 QELLREAEELEEELQLEELEqeiAALLAEAGVEDEEELraALEQAEEYQELKEELEELEEQ---LEELLGELEELLEALD 426


                   ....
gi 1822435973  703 LDSL 706
Cdd:COG4717    427 EEEL 430
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 923-981 1.96e-05

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.


Pssm-ID: 188903  Cd Length: 74  Bit Score: 43.86  E-value: 1.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822435973  923 WDGQTVVAWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 981
Cdd:cd09504      5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-534 1.99e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  144 VSSEVEVLKALKSLFEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDA--------- 214
Cdd:PRK03918   319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLekeleelek 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  215 --TEMETPPTQNSAELRPLTSHAKARVTNGTGLRDIEGP----GRLL---ELQDLLDKRSMEVAQMKERLGTLSARVGEL 285
Cdd:PRK03918   399 akEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELteeHRKELLEEYTAELKRIEKELKEIEEKERKL 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  286 EDDVDTARRDLIKSEEMntkyqRDIREAMAQKDDMEERITTLEKRYLGAQ-REATSLHDLNDKLENELANTEDLLKQSED 364
Cdd:PRK03918   479 RKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  365 ---KTRQLQERLELAEQKLQQTMRKAETLP-EVEAELAQRVAALTKYD------PSSPDDSTILEVKLQDMSILLRKAEE 434
Cdd:PRK03918   554 lkkKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYneylelKDAEKELEREEKELKKLEEELDKAFE 633

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  435 RHGDIEERLRQLETQLEEKNQ-------------------EVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQlhLKE 495
Cdd:PRK03918   634 ELAETEKRLEELRKELEELEKkyseeeyeelreeylelsrELAGLRAELEELEKRREEIKKTLEKLKEELEEREK--AKK 711

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1822435973  496 RMSSLEEKNALTHELdnTRKQLEEAHMDKERMADEVEKV 534
Cdd:PRK03918   712 ELEKLEKALERVEEL--REKVKKYKALLKERALSKVGEI 748
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 346-496 2.37e-05

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: 47.23  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  346 DKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRVAALTKYDpsspddSTILEVK---- 421
Cdd:COG1579     20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK---RLELEIEEVEARIKKYE------EQLGNVRnnke 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  422 LQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKER 496
Cdd:COG1579     91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1116-1184 2.37e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 43.41  E-value: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822435973 1116 VWSNERVIRWIQSIGLRDYANSLVESGVHGALIALDDTFDHIAlalslQIPTQNTQARQVLEREFNNLL 1184
Cdd:pfam07647    3 SWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLK-----RLGITSVGHRRKILKKIQELK 66
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 293-527 3.40e-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: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  293 RRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRY----LGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQ 368
Cdd:TIGR00618  165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  369 LQERLELAEQKLQQtmrkaetlpevEAELAQRVAALTKYDPSSPddstilEVKLQDMSILLRKAEERHGDIEERLRQLET 448
Cdd:TIGR00618  245 LTQKREAQEEQLKK-----------QQLLKQLRARIEELRAQEA------VLEETQERINRARKAAPLAAHIKAVTQIEQ 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  449 QLEEKNQEVlrarqREKMNEEhNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRK-QLEEAHMDKERM 527
Cdd:TIGR00618  308 QAQRIHTEL-----QSKMRSR-AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIReISCQQHTLTQHI 381
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
307-492 3.85e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 3.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  307 QRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRK 386
Cdd:COG4372     30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  387 AETLpevEAELAQRVAALTKydpsspddstiLEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVlrARQREKM 466
Cdd:COG4372    110 AEEL---QEELEELQKERQD-----------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL--AALEQEL 173

                          170       180
                   ....*....|....*....|....*.
gi 1822435973  467 NEEHNKRLSDTVDKLLSESNERLQLH 492
Cdd:COG4372    174 QALSEAEAEQALDELLKEANRNAEKE 199
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-463 4.21e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  272 KERLGTLSARVGELEDDVDTARRDLIKSEemntkyqrDIREAMAQKDDMEERITTL---EKRYLGAQREatsLHDLNDKL 348
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALE--------AELDALQERREALQRLAEYswdEIDVASAERE---IAELEAEL 677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  349 ENELANTEDL--LKQSEDKTRQLQERLELAEQKLQQTMRKAETlpEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDM- 425
Cdd:COG4913    678 ERLDASSDDLaaLEEQLEELEAELEELEEELDELKGEIGRLEK--ELEQAEEELDELQDRLEAAEDLARLELRALLEERf 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1822435973  426 -SILLRKAEERHGD-IEERLRQLETQLEEKNQEVLRARQR 463
Cdd:COG4913    756 aAALGDAVERELREnLEERIDALRARLNRAEEELERAMRA 795
PRK01156 PRK01156
chromosome segregation protein; Provisional
 275-552 4.47e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.97  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  275 LGTLSARVGELEDDV--DTARRDLIKSEEMNtkyqrdIREAMAQKDDMEERITTLekrylgaQREATSLHDLNDKLE--- 349
Cdd:PRK01156   130 LNSIFVGQGEMDSLIsgDPAQRKKILDEILE------INSLERNYDKLKDVIDML-------RAEISNIDYLEEKLKssn 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  350 NELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDpsspddSTILEVKlQDMSILL 429
Cdd:PRK01156   197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYE------SEIKTAE-SDLSMEL 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  430 RKAEERHGdIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLS--ESNERLQLHLKERMSSLEEKNALT 507
Cdd:PRK01156   270 EKNNYYKE-LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINkyHAIIKKLSVLQKDYNDYIKKKSRY 348

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1822435973  508 HELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSMVDPV 552
Cdd:PRK01156   349 DDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 63-548 4.51e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   63 HDRDSLQ----RQLNSALPQEFAALTKELNACREQLLEREEEIAELKAE-RNNTRLLLEH----LECLVSRHERSLR-MT 132
Cdd:pfam15921  205 YEHDSMStmhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQhqdrIEQLISEHEVEITgLT 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  133 VVKRQAQSPA-GVSSEVEV------------LKALKSLFEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLREQ 199
Cdd:pfam15921  285 EKASSARSQAnSIQSQLEIiqeqarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  200 AAHAQRRAGDGSEDATEMETPPTQNSAELRpLTSHAKARVTNgtglRDIEGPGRLLELQDLLDKRSMEVAQMKERLGTLS 279
Cdd:pfam15921  365 RDQFSQESGNLDDQLQKLLADLHKREKELS-LEKEQNKRLWD----RDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  280 ARV-GELE-------------DDVDTARRDLIKSEEMNTKYqrdIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLN 345
Cdd:pfam15921  440 SECqGQMErqmaaiqgkneslEKVSSLTAQLESTKEMLRKV---VEELTAKKMTLESSERTVSDLTASLQEKERAIEATN 516

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  346 DKLeNELANTEDL-------LKQSEDKTRQLQE-----RLELAEQ-KLQQTMRKA-ETLPEVEAELAQRVAALTKYDPSS 411
Cdd:pfam15921  517 AEI-TKLRSRVDLklqelqhLKNEGDHLRNVQTecealKLQMAEKdKVIEILRQQiENMTQLVGQHGRTAGAMQVEKAQL 595

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  412 PDDSTILEVKLQDMSIL-------LRKAEERHGDIE-----------ERLRQLETQLEEKNQ---EVLRARQR-EKMNEE 469
Cdd:pfam15921  596 EKEINDRRLELQEFKILkdkkdakIRELEARVSDLElekvklvnagsERLRAVKDIKQERDQllnEVKTSRNElNSLSED 675

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  470 HN--KRLSDTVDKLLSESNERLQLHLKERMSSLE---------------------------------------------- 501
Cdd:pfam15921  676 YEvlKRNFRNKSEEMETTTNKLKMQLKSAQSELEqtrntlksmegsdghamkvamgmqkqitakrgqidalqskiqflee 755

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  502 -------EKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSM 548
Cdd:pfam15921  756 amtnankEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANM 809
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 147-540 6.90e-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: 47.48  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  147 EVEVLKALKSLFEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAgdgSEDATEMETPPTQNSA 226
Cdd:pfam01576  171 EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI---AELRAQLAKKEEELQA 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  227 ELRPLTSHAKARVTNGTGLRDIEGpgRLLELQ-DLLDKRSMEVAQMKER--LGT-LSARVGELEDDVDT--ARRDL-IKS 299
Cdd:pfam01576  248 ALARLEEETAQKNNALKKIRELEA--QISELQeDLESERAARNKAEKQRrdLGEeLEALKTELEDTLDTtaAQQELrSKR 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  300 EEMNTKYQRDIREAM----AQKDDMEER----ITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQE 371
Cdd:pfam01576  326 EQEVTELKKALEEETrsheAQLQEMRQKhtqaLEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEH 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  372 RLELAEQKLQQTMRKAETLPEVEAELAQRVAALT---------------KYDPSSPDDSTiLEVKLQDMSILLRKAEERH 436
Cdd:pfam01576  406 KRKKLEGQLQELQARLSESERQRAELAEKLSKLQselesvssllneaegKNIKLSKDVSS-LESQLQDTQELLQEETRQK 484

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  437 GDIEERLRQLE---TQLEEKNQEVLRARQR-EKMNEEHNKRLSDTVDKLLSESnerlqlhlkERMSSLEE-KNALTHELD 511
Cdd:pfam01576  485 LNLSTRLRQLEderNSLQEQLEEEEEAKRNvERQLSTLQAQLSDMKKKLEEDA---------GTLEALEEgKKRLQRELE 555

                          410       420
                   ....*....|....*....|....*....
gi 1822435973  512 NTRKQLEEahmdKERMADEVEKVRLEMEQ 540
Cdd:pfam01576  556 ALTQQLEE----KAAAYDKLEKTKNRLQQ 580
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 63-532 7.16e-05

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: 47.53  E-value: 7.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   63 HDRDSLQRQLNSAlpQEFAALTKELNACREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPA 142
Cdd:pfam12128  228 RDIQAIAGIMKIR--PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLR-TLDDQWKEKRD 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  143 GVSSEVEVLKALKSLFEHH-KALDEKVRERLRVALERVAALEEELQATSQELMLLRE------------QAAHAQRRAGD 209
Cdd:pfam12128  305 ELNGELSAADAAVAKDRSElEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEErlkaltgkhqdvTAKYNRRRSKI 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  210 GSEDATEME--TPPTQNSAELRPLtSHAKARvtngTGLRDIEGPGRLlELQDLLDKRSMEVAQMKERLGTLSARVGEL-- 285
Cdd:pfam12128  385 KEQNNRDIAgiKDKLAKIREARDR-QLAVAE----DDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRLNQAta 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  286 -----------EDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLND----KLEN 350
Cdd:pfam12128  459 tpelllqlenfDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpqagTLLH 538

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  351 ELANTEDLLKQSEDK--TRQLQERLELAEQKLQQTMRKAETLPEVEAELaQRVAAltkydPSSPDDSTILEVKLQDMSIL 428
Cdd:pfam12128  539 FLRKEAPDWEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLYGVKLDL-KRIDV-----PEWAASEEELRERLDKAEEA 612

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  429 LRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLK---ERMSSLE-EKN 504
Cdd:pfam12128  613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDsanERLNSLEaQLK 692

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1822435973  505 ALTHE----LDNTRKQLEEAHMDKERMADEVE 532
Cdd:pfam12128  693 QLDKKhqawLEEQKEQKREARTEKQAYWQVVE 724
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 256-477 7.98e-05

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 46.94  E-value: 7.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDvdtarrdlIKSEEMNtkyqrdIREAMAQKDDMEERITTLEKRYLGAQ 335
Cdd:pfam05667  325 TEEELQQQREEELEELQEQLEDLESSIQELEKE--------IKKLESS------IKQVEEELEELKEQNEELEKQYKVKK 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  336 ReatslhdlndklenelanTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAEtlpEVEAELAQRVAALTKYDPSSPDDS 415
Cdd:pfam05667  391 K------------------TLDLLPDAEENIAKLQALVDASAQRLVELAGQWE---KHRVPLIEEYRALKEAKSNKEDES 449

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822435973  416 tilEVKLQDMSILLRKAEERHGDI---EERLRQLETQLEEKNQEVLRAR--QR--------EKMNEEHNKRLSDT 477
Cdd:pfam05667  450 ---QRKLEEIKELREKIKEVAEEAkqkEELYKQLVAEYERLPKDVSRSAytRRileivkniKKQKEEITKILSDT 521
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 309-520 8.15e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 8.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  309 DIREAMAQKDDMEERITTLEKRYLGAQREAtslhdlnDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTmrkae 388
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDALQAEL-------EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  389 tlpevEAELAQRVAALTKYDPSSPDDSTILEVK-LQDM---SILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQRE 464
Cdd:COG3883     85 -----REELGERARALYRSGGSVSYLDVLLGSEsFSDFldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973  465 KMNEEHNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDNTRKQLEEA 520
Cdd:COG3883    160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 175-412 1.01e-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: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  175 ALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKARVTNGTGLRDiegpgRL 254
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-----EI 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  255 LELQDLLDKRSmevAQMKERLGTL--SARVGELE-----DDVDtarrDLIKSEEMNTKYQRDIREAMAQkddMEERITTL 327
Cdd:COG4942     93 AELRAELEAQK---EELAELLRALyrLGRQPPLAlllspEDFL----DAVRRLQYLKYLAPARREQAEE---LRADLAEL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  328 EKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKY 407
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242


                   ....*
gi 1822435973  408 DPSSP 412
Cdd:COG4942    243 TPAAG 247
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 300-539 1.04e-04

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: 46.64  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  300 EEMNTKYQRDIREAMAQKDDMEERITTLEKRYL----GAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLEL 375
Cdd:pfam05483  200 EELRVQAENARLEMHFKLKEDHEKIQHLEEEYKkeinDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  376 AEQKLQQTMRKAETLPEveaelaqrvaaltkydpsspddstilevKLQDMSILLRKAEERHGDIEERLR-------QLET 448
Cdd:pfam05483  280 QDENLKELIEKKDHLTK----------------------------ELEDIKMSLQRSMSTQKALEEDLQiatkticQLTE 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  449 QLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQ----------LHLKERMSSLEEKNALTHELDNTRKQLE 518
Cdd:pfam05483  332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEknedqlkiitMELQKKSSELEEMTKFKNNKEVELEELK 411

                          250       260
                   ....*....|....*....|....
gi 1822435973  519 EAHMDKERMADE---VEKVRLEME 539
Cdd:pfam05483  412 KILAEDEKLLDEkkqFEKIAEELK 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 35-206 1.06e-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: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   35 DERDRLLDALRDAQETIAHTQSRLHDVCHDRDSLQRQLNsALPQEFAALTKELNACREQLLEREEEIAELKAERNNTRLL 114
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  115 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERVAALEEELQATSQ 191
Cdd:COG4942     99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174

                          170
                   ....*....|....*
gi 1822435973  192 ELMLLREQAAHAQRR 206
Cdd:COG4942    175 ELEALLAELEEERAA 189
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 129-540 1.17e-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: 46.27  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  129 LRMTVV-KRQAQSPAGVSSEVEVLKAL-KSLFEHHKALDEK------VRERLRVALERVAAL-------EEELQATSQEL 193
Cdd:pfam05557   55 KRIRLLeKREAEAEEALREQAELNRLKkKYLEALNKKLNEKesqladAREVISCLKNELSELrrqiqraELELQSTNSEL 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  194 MLLREQAAHAQRRAGDGSEDATEMETPPTQNS-AELRpltshakarvtngtgLRDIEgpgRLLELQdllDKRSMEVAQMK 272
Cdd:pfam05557  135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAeAEQR---------------IKELE---FEIQSQ---EQDSEIVKNSK 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  273 ERLgtlsARVGELEddvdtarRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEkRYLGAQREATSLHDLNDKLENEL 352
Cdd:pfam05557  194 SEL----ARIPELE-------KELERLREHNKHLNENIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQEL 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  353 ANTEDL-------LKQSEDKTRQ----LQERLELAEQK---LQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTIL 418
Cdd:pfam05557  262 QSWVKLaqdtglnLRSPEDLSRRieqlQQREIVLKEENsslTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  419 EvKLQDMSILLRKaeERHGdIEERLRQLETQLEEKN---QEVLRARQREKM-------NEEHNKRLSD-----TVDKLLS 483
Cdd:pfam05557  342 R-RLQRRVLLLTK--ERDG-YRAILESYDKELTMSNyspQLLERIEEAEDMtqkmqahNEEMEAQLSVaeeelGGYKQQA 417

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973  484 ESNERlQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:pfam05557  418 QTLER-ELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELER 473
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 316-540 1.41e-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: 46.58  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  316 QKDDMEERitTLEKRYLGAQRE-ATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVE 394
Cdd:TIGR00606  198 QGQKVQEH--QMELKYLKQYKEkACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  395 AELAQRvaaltkyDPSSPDDSTILEVKLQDMSILLRKAEERHG----DIEERLRQLETQLEEKNQEVLRARQREKMNEEH 470
Cdd:TIGR00606  276 SRKKQM-------EKDNSELELKMEKVFQGTDEQLNDLYHNHQrtvrEKERELVDCQRELEKLNKERRLLNQEKTELLVE 348

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822435973  471 NKRLSDTVDK----LLSESNERLQLHLKERMSSLEEKNALTHELDN-----TRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:TIGR00606  349 QGRLQLQADRhqehIRARDSLIQSLATRLELDGFERGPFSERQIKNfhtlvIERQEDEAKTAAQLCADLQSKERLKQEQ 427
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 272-519 2.02e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  272 KERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEK-------RYLGAQREATSLHDL 344
Cdd:TIGR04523   95 KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnKYNDLKKQKEELENE 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  345 NDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQqtmrKAETLPEVEAELAQRVAALTkydpsspDDSTILEVKLQD 424
Cdd:TIGR04523  175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLK-------DNIEKKQQEINE 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  425 MSILLRKAEERHGDIEERLRQLETQLEEKNQEVlraRQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKN 504
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL---EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE 320

                          250
                   ....*....|....*
gi 1822435973  505 altHELDNTRKQLEE 519
Cdd:TIGR04523  321 ---KKLEEIQNQISQ 332
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 146-491 2.16e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  146 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERVAALEEELqatSQELMLLREQAAHAQRRAGDGSEDAT---EMETP 220
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEK---AREVERRRKLEEAEKARQAEMDRQAAiyaEQERM 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  221 PTQNSAELRPLTSHAKARVTNGTGLRDIEGP-GRLLELQDLldkrSMEVAQMKERLgtlsarvgelEDDVDTARRDLIKS 299
Cdd:pfam17380  343 AMERERELERIRQEERKRELERIRQEEIAMEiSRMRELERL----QMERQQKNERV----------RQELEAARKVKILE 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  300 EEMNTKYQRDIREaMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENElANTEDLLKQSEDKTRQlqeRLELAEQK 379
Cdd:pfam17380  409 EERQRKIQQQKVE-MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQEEERKRK---KLELEKEK 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  380 LQQTMRKAETLPEVEAELAQRVAALTKYDpsspDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLR 459
Cdd:pfam17380  484 RDRKRAEEQRRKILEKELEERKQAMIEEE----RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMR 559

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1822435973  460 ARQREKMNEEHNKRLSDTVDKLLSESNERLQL 491
Cdd:pfam17380  560 KATEERSRLEAMEREREMMRQIVESEKARAEY 591
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 103-550 2.42e-04

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: 45.48  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  103 ELKAERNNTRLLLEHLECLVSRHERSLR-MTVVKRQAQSPAGVSSEVEVLKA--LKSLFEHHKALDEKVrERLRVALERV 179
Cdd:pfam05483  230 EYKKEINDKEKQVSLLLIQITEKENKMKdLTFLLEESRDKANQLEEKTKLQDenLKELIEKKDHLTKEL-EDIKMSLQRS 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  180 A----ALEEELQATSQELMLLRE----QAAHAQRRAGDGSEDATEMETpptqNSAELRPLTSHAKARVTNGtglrdiEGP 251
Cdd:pfam05483  309 MstqkALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEA----TTCSLEELLRTEQQRLEKN------EDQ 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  252 GRLLELQdlLDKRSMEVAQMKERLGTLSARVGELEDdvdtarrdlIKSEEMNTKYQRDIREAMAQkddmEERITTLEKRY 331
Cdd:pfam05483  379 LKIITME--LQKKSSELEEMTKFKNNKEVELEELKK---------ILAEDEKLLDEKKQFEKIAE----ELKGKEQELIF 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  332 LGAQREaTSLHDLNDKLENELANTEDLLKQSED-KTRQLQERLELAEQKLQQTMRKAETlpeveAELAQRVAALTkydps 410
Cdd:pfam05483  444 LLQARE-KEIHDLEIQLTAIKTSEEHYLKEVEDlKTELEKEKLKNIELTAHCDKLLLEN-----KELTQEASDMT----- 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  411 spddstiLEVKLQDMSILLRKAEErhgdiEERLRQLETqLEEKNQEVlraRQREKMNEEHNKRLSDTVDKLLSESNERLQ 490
Cdd:pfam05483  513 -------LELKKHQEDIINCKKQE-----ERMLKQIEN-LEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEENAR 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  491 LHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADE---------------------VEKVRLEMEQWRLKTSSMV 549
Cdd:pfam05483  577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgsaenkqlnayeikVNKLELELASAKQKFEEII 656


                   .
gi 1822435973  550 D 550
Cdd:pfam05483  657 D 657
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 923-986 2.92e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 40.33  E-value: 2.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  923 WDGQTVVAWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQEM 986
Cdd:pfam00536    3 WSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQRL 63
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 32-423 3.52e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   32 GMLDERDRLLDALRDAQETIAHTQSRLHDVCHDRDSLQRQLNsALPQEFAALTKELNACREQLLEREEEIAELKAErnnt 111
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIENVKSE---- 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  112 rllLEHLECLVSRHERSLrmtvvkrqaqspAGVSSEVEVLKA--LKSLFEHHKALDEKVRERLRVALERVAALEEELQAT 189
Cdd:TIGR02169  760 ---LKELEARIEELEEDL------------HKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  190 SQELMLLREQAAHAQRRAGD----GSEDATEMETPPTQNSAELRPLTSHAKARVTNGTGLRDIEGPGR-----LLELQDL 260
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDeleaqLRELERK 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  261 LDKRSMEVAQMKERLGTLSARVGELEDDVDTArRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEkrylgaqreats 340
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE------------ 971

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  341 lhDLNDKLENELANTEDLLKQSEDK-------TRQLQERLELAEQKLQQTMRKA-----ETLPEVEAELAQRVAALTKYD 408
Cdd:TIGR02169  972 --PVNMLAIQEYEEVLKRLDELKEKrakleeeRKAILERIEEYEKKKREVFMEAfeainENFNEIFAELSGGTGELILEN 1049

                          410
                   ....*....|....*
gi 1822435973  409 PSSPDDSTiLEVKLQ 423
Cdd:TIGR02169 1050 PDDPFAGG-LELSAK 1063
PRK09039 PRK09039
peptidoglycan -binding protein;
258-407 3.64e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  258 QDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYlgAQRE 337
Cdd:PRK09039    52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL--DSEK 129

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  338 ATSlhdlndklENELANTEDLLKQSEDKTRQL---QERLELAEQKLQQTMRKAETL-PEVEAELAQRVAALTKY 407
Cdd:PRK09039   130 QVS--------ARALAQVELLNQQIAALRRQLaalEAALDASEKRDRESQAKIADLgRRLNVALAQRVQELNRY 195
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 75-550 3.93e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   75 ALPQEFAALTKELNACREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkAL 154
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RG 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  155 KSLFEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLrEQAAHAQRRAGDGSEDATEMETPPTQNSAELR---PL 231
Cdd:TIGR00618  534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlAC 612

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  232 TSHAKARVTN------GTGLRDIEGPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEddvdTARRDLIKSEEMNTK 305
Cdd:TIGR00618  613 EQHALLRKLQpeqdlqDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE----LLASRQLALQKMQSE 688

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  306 YQR--DIREAMAQKDDMEERITTLEKRYlgaqreatslhdlnDKLENELANTEDLLKQsedktrQLQERLELAEQKLQQT 383
Cdd:TIGR00618  689 KEQltYWKEMLAQCQTLLRELETHIEEY--------------DREFNEIENASSSLGS------DLAAREDALNQSLKEL 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  384 MRKAETlpeveaelaqRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEvlrarqr 463
Cdd:TIGR00618  749 MHQART----------VLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE------- 811

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  464 ekmneehnkRLSDTVDKLLSEsnERLQLHLKERMSSLEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRL 543
Cdd:TIGR00618  812 ---------IPSDEDILNLQC--ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880


                   ....*..
gi 1822435973  544 KTSSMVD 550
Cdd:TIGR00618  881 INQIKIQ 887
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-412 4.52e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  164 LDEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGdgSEDATEMETPPTQNSAELRPLTSHAKARvtngt 243
Cdd:COG3206    162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAE----- 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  244 gLRDIEGpgRLLELQDLLDKRSMEVAQMKErlgtlSARVGELEDDVDTARRDLiksEEMNTKYQR---DIREAMAQKDDM 320
Cdd:COG3206    235 -LAEAEA--RLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAEL---AELSARYTPnhpDVIALRAQIAAL 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  321 EERI--------TTLEKRYLGAQREATSLHDLNDKLENELANtedlLKQSEDKTRQLQERLELAEQKLQQTMRKAEtlpE 392
Cdd:COG3206    304 RAQLqqeaqrilASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVARELYESLLQRLE---E 376

                          250       260
                   ....*....|....*....|....*..
gi 1822435973  393 VEAELAQRVA-------ALTKYDPSSP 412
Cdd:COG3206    377 ARLAEALTVGnvrvidpAVVPLKPVSP 403
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 33-466 5.06e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.90  E-value: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   33 MLDERDRLLDALRDAQETIAHTQSRLhdvchdrdSLQRQLNSALPQEFAALTKELNACREQLLEREEEIAELKAERNNTR 112
Cdd:pfam19220   32 LIEPIEAILRELPQAKSRLLELEALL--------AQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  113 LLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLRVALERVAALEEELQATSQE 192
Cdd:pfam19220  104 AAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQAAEKALQRAEGELATARER 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  193 LMLLREQAAHAQRRAGDGSEDATEMetppTQNSAELRPLTSHAKARvtngtgLRDIEGpgRLLELQDLldkRSMEVAQMK 272
Cdd:pfam19220  169 LALLEQENRRLQALSEEQAAELAEL----TRRLAELETQLDATRAR------LRALEG--QLAAEQAE---RERAEAQLE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  273 ERLGTLSARVGELEDDVDTARRDLIKSEEMNTkyqrdirEAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENEL 352
Cdd:pfam19220  234 EAVEAHRAERASLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADL 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  353 antedllkqsEDKTRQLQErlelaeqklQQTMRkaetlpeveAELAQRVAALTKydpsspddstilevKLQDMSILLRKA 432
Cdd:pfam19220  307 ----------ERRTQQFQE---------MQRAR---------AELEERAEMLTK--------------ALAAKDAALERA 344

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1822435973  433 EERHGDIEERLRQLE-------TQLEEKNQEVLRARQREKM 466
Cdd:pfam19220  345 EERIASLSDRIAELTkrfeverAALEQANRRLKEELQRERA 385
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 280-450 5.09e-04

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: 44.56  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  280 ARVGELEDDVDTARRDLIKSEEMNTKYQRdireAMAQKDDMEERITTLEkrYLGAQREATSLHD----------LNDKLE 349
Cdd:COG3096    917 KALAQLEPLVAVLQSDPEQFEQLQADYLQ----AKEQQRRLKQQIFALS--EVVQRRPHFSYEDavgllgensdLNEKLR 990

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  350 NELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDstilevklqdmsill 429
Cdd:COG3096    991 ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEE--------------- 1055

                          170       180
                   ....*....|....*....|....*...
gi 1822435973  430 rKAEERHGDIEERLR-------QLETQL 450
Cdd:COG3096   1056 -RARIRRDELHEELSqnrsrrsQLEKQL 1082
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
305-519 5.36e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 5.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  305 KYQRDIREAMAQK--DDMEERITTLEKRYLGAQREATSLhdlndKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQ 382
Cdd:COG3206    163 EQNLELRREEARKalEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  383 TMRKAETLpevEAELAQRVAALtkydPSSPDDSTILEVKLQ------DMSILLRKAEERHGDIEERLRQLETQLEEKNQE 456
Cdd:COG3206    238 AEARLAAL---RAQLGSGPDAL----PELLQSPVIQQLRAQlaeleaELAELSARYTPNHPDVIALRAQIAALRAQLQQE 310

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  457 VLRARQREKMNEEHNKRLSDTVDKLLSESNERLQlhlkeRMSSLEEK-NALTHELDNTRKQLEE 519
Cdd:COG3206    311 AQRILASLEAELEALQAREASLQAQLAQLEARLA-----ELPELEAElRRLEREVEVARELYES 369
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1036-1091 5.49e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 39.56  E-value: 5.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973 1036 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRTSLQYGIMCLK 1091
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 368-551 5.92e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 5.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  368 QLQERLELAE--QKLQQTMRKAETLPEVEAELAQRVAALTkydpsspDDSTILEVKLQDMSILLRKAEERHGDIEERLRQ 445
Cdd:COG1579      5 DLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  446 LETQLEE-KNQEVLRARQREKmnEEHNKRLSDTVDKLLsESNERLQlHLKERMSSLEEknalthELDNTRKQLEEAHMDK 524
Cdd:COG1579     78 YEEQLGNvRNNKEYEALQKEI--ESLKRRISDLEDEIL-ELMERIE-ELEEELAELEA------ELAELEAELEEKKAEL 147

                          170       180
                   ....*....|....*....|....*..
gi 1822435973  525 ERMADEVEKVRLEMEQWRLKTSSMVDP 551
Cdd:COG1579    148 DEELAELEAELEELEAEREELAAKIPP 174
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 168-543 6.56e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.04  E-value: 6.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  168 VRERLRVALER-------VAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAE----------LRP 230
Cdd:pfam10174   58 LKEQYRVTQEEnqhlqltIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqakelflLRK 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  231 LTSHAKARVT---NGTGLRDiEGPGRLLEL---QDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIK-SEEMN 303
Cdd:pfam10174  138 TLEEMELRIEtqkQTLGARD-ESIKKLLEMlqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHlREELH 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  304 TKYQ----RDIREAMAQKDDMEE-RITTLEKrylgaqreatSLHDLNDKLE----NELANTEDL---LKQSE-------- 363
Cdd:pfam10174  217 RRNQlqpdPAKTKALQTVIEMKDtKISSLER----------NIRDLEDEVQmlktNGLLHTEDReeeIKQMEvykshskf 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  364 --DKTRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSILLrkaEERHGDIEE 441
Cdd:pfam10174  287 mkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRL---EEKESFLNK 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  442 RLRQLETQLEEKN---------QEVLRARQReKMNEEHNK--RLSDTV---DKLLSEsnerlqlhLKERMSSLEEKNALT 507
Cdd:pfam10174  364 KTKQLQDLTEEKStlageirdlKDMLDVKER-KINVLQKKieNLQEQLrdkDKQLAG--------LKERVKSLQTDSSNT 434

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1822435973  508 helDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRL 543
Cdd:pfam10174  435 ---DTALTTLEEALSEKERIIERLKEQREREDRERL 467
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 256-513 8.22e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 42.78  E-value: 8.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREA---MAQKDDMEERITTLEKR-- 330
Cdd:pfam06008   27 QLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAkelAEAIKNLIDNIKEINEKva 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  331 YLGAQREATSlhdlNDKLENELANTEDLLKqsEDKTRQLQERLELAEQKLqqtmRKAETLPEVEAELAQRVAALTK-YDP 409
Cdd:pfam06008  107 TLGENDFALP----SSDLSRMLAEAQRMLG--EIRSRDFGTQLQNAEAEL----KAAQDLLSRIQTWFQSPQEENKaLAN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  410 SSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQletqleekNQEVLRARQREKmneehnkrlsdtvdKLLSESNERL 489
Cdd:pfam06008  177 ALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLA--------NQANLREFQRKK--------------EEVSEQKNQL 234

                          250       260
                   ....*....|....*....|....
gi 1822435973  490 QLHLKERMSSLEEKNALTHELDNT 513
Cdd:pfam06008  235 EETLKTARDSLDAANLLLQEIDDA 258
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 267-550 8.42e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 8.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  267 EVAQMKERLGTLSARVGELE-DDVDTARRDLikSEEMNTKYqrDI--REAMAQKDdMEERITTLEKRYLGAQREatslhd 343
Cdd:PRK04778   257 EIQDLKEQIDENLALLEELDlDEAEEKNEEI--QERIDQLY--DIleREVKARKY-VEKNSDTLPDFLEHAKEQ------ 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  344 lNDKLENELanteDLLKQS-------EDKTRQLQERLELAEQKLQqtmrkaetlpEVEAELAQRVAAltkYdpsspddsT 416
Cdd:PRK04778   326 -NKELKEEI----DRVKQSytlneseLESVRQLEKQLESLEKQYD----------EITERIAEQEIA---Y--------S 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  417 ILEVKLQDMSILLRKAEERHGDIEERLRQLEtqleeknQEVLRARQRekmneehnkrlSDTVDKLLSESNERLQlhlKER 496
Cdd:PRK04778   380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLR-------KDELEAREK-----------LERYRNKLHEIKRYLE---KSN 438

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822435973  497 MSS-----LEEKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSMVD 550
Cdd:PRK04778   439 LPGlpedyLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-391 9.54e-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: 43.21  E-value: 9.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  166 EKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAKARVTN-GTG 244
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  245 LRDIEGPGRLLELQDLLdkRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKDDMEERI 324
Cdd:COG4942    110 LRALYRLGRQPPLALLL--SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822435973  325 TTLEKryLGAQREatslhDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLP 391
Cdd:COG4942    188 AALEA--LKAERQ-----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 429-695 1.02e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  429 LRKAEERHGDIEERLRQLETQLEEKNQevlrarQREKMNEEHNKRLSdtVDKLLSESNE-RLQLHLKERMSSLEEKNALT 507
Cdd:TIGR02169  172 KEKALEELEEVEENIERLDLIIDEKRQ------QLERLRREREKAER--YQALLKEKREyEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  508 HELDNTRKQLEEAHMDKERMADEVEKVRLEMEQWRLKTSSMVDPVIPR--SHLGSTSDIRYSLGSSVileapgdpfgsSA 585
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLERSI-----------AE 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  586 VLRRQK---GRLSALRDEPGKVQ-TLNEQEWQRMQQAGVLASVaqafesETEASDQEDDRETIFSSADLLSPSG------ 655
Cdd:TIGR02169  313 KERELEdaeERLAKLEAEIDKLLaEIEELEREIEEERKRRDKL------TEEYAELKEELEDLRAELEEVDKEFaetrde 386

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1822435973  656 HSDAQTLALMLQEQLDAINNEIRLIQEEKESTEQRAEEIE 695
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 73-519 1.10e-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: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   73 NSALPQEFAALTKELNACREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSlRMTVVKRQAQSPAGVSSEVEVLK 152
Cdd:pfam01576  147 NSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG-RQELEKAKRKLEGESTDLQEQIA 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  153 ALKSLFEHHKALDEKVRERLRVALERvaaLEEELQATSQELMLLREQAAH-----------------AQRRAGDGSED-- 213
Cdd:pfam01576  226 ELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQiselqedleseraarnkAEKQRRDLGEEle 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  214 ATEMETPPTQNS-AELRPLTSHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEddvdTA 292
Cdd:pfam01576  303 ALKTELEDTLDTtAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE----KA 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  293 RRDLiksEEMNTKYQRDIREAMAQKDDMEER-------ITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDK 365
Cdd:pfam01576  379 KQAL---ESENAELQAELRTLQQAKQDSEHKrkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK 455

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  366 TRQLQErlelaeqklqqtmrkaetlpeveaelaqrvaaltkydpsspdDSTILEVKLQDMSILLRKAEERHGDIEERLRQ 445
Cdd:pfam01576  456 NIKLSK------------------------------------------DVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  446 LE---TQLEEKNQEVLRARQR-EKMNEEHNKRLSDTVDKL---------LSESNERLQLHLKERMSSLEEKNALTHELDN 512
Cdd:pfam01576  494 LEderNSLQEQLEEEEEAKRNvERQLSTLQAQLSDMKKKLeedagtleaLEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573


                   ....*..
gi 1822435973  513 TRKQLEE 519
Cdd:pfam01576  574 TKNRLQQ 580
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 266-523 1.12e-03

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: 43.40  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  266 MEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREAMAQKD-DMEERITTLEKRYLGAQREATSLHDL 344
Cdd:COG3096    836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADeTLADRLEELREELDAAQEAQAFIQQH 915

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  345 NDKLEnELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAETLpeveAELAQRVAALTKYD-PSSPDDSTILEVKLQ 423
Cdd:COG3096    916 GKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSYEDaVGLLGENSDLNEKLR 990

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  424 DMsilLRKAEERHGDIEERLRQLETQLEEKNQEV--LRARQREK--MNEEHNKRLSDTVDKLLSESNERlqlhLKERMSS 499
Cdd:COG3096    991 AR---LEQAEEARREAREQLRQAQAQYSQYNQVLasLKSSRDAKqqTLQELEQELEELGVQADAEAEER----ARIRRDE 1063

                          250       260       270
                   ....*....|....*....|....*....|
gi 1822435973  500 LEEKnalTHELDNTRKQLE------EAHMD 523
Cdd:COG3096   1064 LHEE---LSQNRSRRSQLEkqltrcEAEMD 1090
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-424 1.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   34 LDERDRLLDALRDAQETIAHTQSRLHDVCHDRDSLQRQLNSALPQEFAALTKELNACREQLLEREEEIAELKAERNNTRL 113
Cdd:COG4717    155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  114 LLEHLECLVSRHER--------------SLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERV 179
Cdd:COG4717    235 ELEAAALEERLKEArlllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  180 AALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRPLTSHAK-ARVTNGTGLRDIEGPGRLLELQ 258
Cdd:COG4717    315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEAGVEDEEELRAALEQA 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  259 DLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRdliksEEMNTKYQRDIREAMAQKDDMEERITTLEKRyLGAQREA 338
Cdd:COG4717    395 EEYQELKEELEELEEQLEELLGELEELLEALDEEEL-----EEELEELEEELEELEEELEELREELAELEAE-LEQLEED 468

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  339 TSLHDLNDKLENELANTEDLLKQsedktrqlQERLELAEQKLQQTMRKA--ETLPEVEAELAQRVAALT--KYDPSSPDD 414
Cdd:COG4717    469 GELAELLQELEELKAELRELAEE--------WAALKLALELLEEAREEYreERLPPVLERASEYFSRLTdgRYRLIRIDE 540

                          410
                   ....*....|
gi 1822435973  415 STILEVKLQD 424
Cdd:COG4717    541 DLSLKVDTED 550
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 183-539 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: 43.24  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  183 EEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPT------QNSAELRPLTSHAKARVTN-GTGLRDI--EGPGR 253
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNalqeqlQAETELCAEAEEMRARLAArKQELEEIlhELESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  254 LLELQDLLDKRSMEVAQMKERLGTLSARVGE--------------LEDDVDTARRDLIKSEEMNTKYQRdireamaQKDD 319
Cdd:pfam01576   84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqklqlekvtTEAKIKKLEEDILLLEDQNSKLSK-------ERKL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  320 MEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQsEDKTRQLQERL-------------ELAEQKLQ----- 381
Cdd:pfam01576  157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-EEKGRQELEKAkrklegestdlqeQIAELQAQiaelr 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  382 -QTMRKAE----TLPEVEAELAQRVAALTKYDPSSPDDSTILEvKLQDMSILLRKAEERHGDIEERLRQLETQLEEK--- 453
Cdd:pfam01576  236 aQLAKKEEelqaALARLEEETAQKNNALKKIRELEAQISELQE-DLESERAARNKAEKQRRDLGEELEALKTELEDTldt 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  454 --NQEVLRARqREKMNEEHNKRLSDTVDKLLSESNERLQLHlkerMSSLEEknaLTHELDNTRKQleEAHMDKERMADEV 531
Cdd:pfam01576  315 taAQQELRSK-REQEVTELKKALEEETRSHEAQLQEMRQKH----TQALEE---LTEQLEQAKRN--KANLEKAKQALES 384


                   ....*...
gi 1822435973  532 EKVRLEME 539
Cdd:pfam01576  385 ENAELQAE 392
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 309-519 1.35e-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: 42.75  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  309 DIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTED--------------LLKQSEdktrQLQE--- 371
Cdd:pfam05622    1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkyllLQKQLE----QLQEenf 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  372 RLELAEQKLQQtmrKAETLPEVEAELAQRVAALTKYDP-------------SSPDDSTILEV-------KLQDMSILLRK 431
Cdd:pfam05622   77 RLETARDDYRI---KCEELEKEVLELQHRNEELTSLAEeaqalkdemdilrESSDKVKKLEAtvetykkKLEDLGDLRRQ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  432 A---EERHGDIEERLRQLETQLEEKNqeVLRARQrekmnEEHNKRLSDTVDKLLSESN--ERLQL---HLKERMSSLE-E 502
Cdd:pfam05622  154 VkllEERNAEYMQRTLQLEEELKKAN--ALRGQL-----ETYKRQVQELHGKLSEESKkaDKLEFeykKLEEKLEALQkE 226

                          250
                   ....*....|....*..
gi 1822435973  503 KNALTHELDNTRKQLEE 519
Cdd:pfam05622  227 KERLIIERDTLRETNEE 243
Dynactin_p22 pfam07426
Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex ...
 321-459 1.42e-03

Dynactin subunit p22; This family contains p22, the smallest subunit of dynactin, a complex that binds to cytoplasmic dynein and is a required activator for cytoplasmic dynein-mediated vesicular transport. Dynactin localizes to the cleavage furrow and to the midbodies of dividing cells, suggesting that it may function in cytokinesis. Family members are approximately 170 residues long.


Pssm-ID: 462162 [Multi-domain]  Cd Length: 163  Bit Score: 40.67  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  321 EERITTLEKRYLGAQREAT--------SLHDLNDKLENELANTE---DLLKQSEDKTRQLQ----ERLELAEQKlqqtmr 385
Cdd:pfam07426    2 EERIAELEKRVYGEEKNREkdpnsiidSLLKVQTKLSSAVSKREkikQLFKKIPELNKYLDpqyeDSIALPDAA------ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  386 KAETLPEVEAELAQRVAALTKYDPSSP--DDSTI-----LEVKLQDMSILLRKAEERHGDIEERLRQLetqLEEKNQEVL 458
Cdd:pfam07426   76 KLELILASEDELRSTAALLEQLQELKPvlDSEHIkdvpeLTEKLEKLSQIHLKQQEQANELTEEVKDL---LENYNQLVL 152


                   .
gi 1822435973  459 R 459
Cdd:pfam07426  153 T 153
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 149-338 1.57e-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: 41.83  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  149 EVLKALKSLFEHHKALDEkVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDAtemetpptqnsAEL 228
Cdd:COG1579      4 EDLRALLDLQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-----------EEV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  229 RPLTSHAKARVTNGTGLRdiegpgrllELQDLldkrSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQR 308
Cdd:COG1579     72 EARIKKYEEQLGNVRNNK---------EYEAL----QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138

                          170       180       190
                   ....*....|....*....|....*....|
gi 1822435973  309 DIREAMAQKDDMEERITTLEKRyLGAQREA 338
Cdd:COG1579    139 ELEEKKAELDEELAELEAELEE-LEAEREE 167
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 255-425 1.78e-03

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: 41.05  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  255 LELQDLLDKrsmEVAQMKERLgtlsARVGELEDDVDTARRDLI----KSEEMNTKYQRDIREAMAQKDDME---ERITTL 327
Cdd:pfam13851   25 LELIKSLKE---EIAELKKKE----ERNEKLMSEIQQENKRLTeplqKAQEEVEELRKQLENYEKDKQSLKnlkARLKVL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  328 EKRYLGAQREATSLHDLNDKLENELantEDLLKQSEDKTRQLQERLELAEQKLQQTMRK-AETLPEVEAELAQRVAAltk 406
Cdd:pfam13851   98 EKELKDLKWEHEVLEQRFEKVERER---DELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEVLAA--- 171

                          170       180
                   ....*....|....*....|.
gi 1822435973  407 ydpSSPDDSTILEV--KLQDM 425
Cdd:pfam13851  172 ---ANLDPDALQAVteKLEDV 189
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 300-540 1.82e-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: 42.85  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  300 EEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTED-----------LLKQSEdktRQ 368
Cdd:pfam01576  656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaklrlevnmqaLKAQFE---RD 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  369 LQERLELAEQK---LQQTMRKAETlpEVEAELAQRVAALTKYDPsspddstiLEVKLQDMSILLRKAEERHGDIEERLRQ 445
Cdd:pfam01576  733 LQARDEQGEEKrrqLVKQVRELEA--ELEDERKQRAQAVAAKKK--------LELDLKELEAQIDAANKGREEAVKQLKK 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  446 LETQLEEKNQEVLRARQ-REKM------NEEHNK-----------------RLSDTVDKLLSESNERLQLHLKERMSSLE 501
Cdd:pfam01576  803 LQAQMKDLQRELEEARAsRDEIlaqskeSEKKLKnleaellqlqedlaaseRARRQAQQERDELADEIASGASGKSALQD 882

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1822435973  502 EKNALTHELDNTRKQLEEAHMDKERMADEVEKVRLEMEQ 540
Cdd:pfam01576  883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQ 921
COG5022 COG5022
Myosin heavy chain [General function prediction only];
310-575 2.02e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  310 IREAMAQKDDMEERITTLEKRYLG---AQREATSLHdlNDKLENELANTEDLLKQSEDKTRQL-----QERLELAEQK-- 379
Cdd:COG5022    808 SRKEYRSYLACIIKLQKTIKREKKlreTEEVEFSLK--AEVLIQKFGRSLKAKKRFSLLKKETiylqsAQRVELAERQlq 885

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  380 -LQQTMRKAETLPEVEAELAQRVAALTKYDPSSP--------DDSTILEVKLQDMSILLRKAEERHG-DIEERLRQLETQ 449
Cdd:COG5022    886 eLKIDVKSISSLKLVNLELESEIIELKKSLSSDLienlefktELIARLKKLLNNIDLEEGPSIEYVKlPELNKLHEVESK 965

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  450 LEEKNQEVLRA--------RQREKMNEEhnkrLSDTVDKLLSESNERLQLHlkERMSSLEEKNALTHELDNTRKQLEEAH 521
Cdd:COG5022    966 LKETSEEYEDLlkkstilvREGNKANSE----LKNFKKELAELSKQYGALQ--ESTKQLKELPVEVAELQSASKIISSES 1039

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  522 MDKERMADEVEKVRLEMEQWRLKTSSMVDPVIPRSHLGSTSDIRYSLGSSVILE 575
Cdd:COG5022   1040 TELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLL 1093
PTZ00121 PTZ00121
MAEBL; Provisional
 298-546 2.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  298 KSEEMNTKYQRDIREAMAQKDD---MEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDkTRQLQERLE 374
Cdd:PTZ00121  1105 KTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED-AKKAEAARK 1183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  375 LAEQKLQQTMRKAETLPEVEA----------------ELAQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGD 438
Cdd:PTZ00121  1184 AEEVRKAEELRKAEDARKAEAarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  439 IEERlRQLETQLEE--KNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMSSLEEK-NALTHELDNTR 514
Cdd:PTZ00121  1264 HFAR-RQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKKaDAAKKKAEEAK 1342

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1822435973  515 KQLEEAHMDKERMADEVEKVRLEMEQWRLKTS 546
Cdd:PTZ00121  1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
149-410 2.46e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  149 EVLKALKSLFEHHKALDEkVRERLRVALERVAALEEeLQATSQELMLLREQAAHAQrragdgsedatemetpptqnsAEL 228
Cdd:COG4913    222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLEP-IRELAERYAAARERLAELE---------------------YLR 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  229 RPLTSHAKARvtngtglrdiegpgRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDL--IKSEEMNTkY 306
Cdd:COG4913    279 AALRLWFAQR--------------RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgNGGDRLEQ-L 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  307 QRDIREAMAQKDDMEERITTLEK--RYLGAQREATS---------LHDLNDKLENELANTEDLLKQSEDKTRQLQERLEL 375
Cdd:COG4913    344 EREIERLERELEERERRRARLEAllAALGLPLPASAeefaalraeAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1822435973  376 AEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPS 410
Cdd:COG4913    424 LEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 253-548 3.46e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  253 RLLELQDLLDKRSMEVAQMK---ERLGTLSARVGELEDDVDTARR--DLIKSEEMNTKYQRDIREAMAQKDDMEERITTL 327
Cdd:TIGR00618  247 QKREAQEEQLKKQQLLKQLRariEELRAQEAVLEETQERINRARKaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  328 EKRYLGAQREATSLHDlNDKLENELANTEDLLKQSEDKT-----------------RQLQERLELAEQKLQQTMRKAETL 390
Cdd:TIGR00618  327 LMKRAAHVKQQSSIEE-QRRLLQTLHSQEIHIRDAHEVAtsireiscqqhtltqhiHTLQQQKTTLTQKLQSLCKELDIL 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  391 PEVEAE----------LAQRVAALTKYDPSSPDDSTILEVKLQDMS-------ILLRKAEERHGDIEERLRQLET---QL 450
Cdd:TIGR00618  406 QREQATidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAqceklekIHLQESAQSLKEREQQLQTKEQihlQE 485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  451 EEKNQEVLRARQREKMNE-EHNKRLSD----TVDKLLSESNERLQLHLKERMSSLEEKNA-LTHELDNTRKQLEEahmDK 524
Cdd:TIGR00618  486 TRKKAVVLARLLELQEEPcPLCGSCIHpnpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEdVYHQLTSERKQRAS---LK 562

                          330       340
                   ....*....|....*....|....
gi 1822435973  525 ERMADEVEKVRLEMEQWRLKTSSM 548
Cdd:TIGR00618  563 EQMQEIQQSFSILTQCDNRSKEDI 586
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 322-519 3.71e-03

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: 41.48  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  322 ERITTLEKRYLGAQREATS-LHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRK--AETLPEVEAELA 398
Cdd:COG5185    260 EQNTDLRLEKLGENAESSKrLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQelEESKRETETGIQ 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  399 QRVAALTKYDPSSpdDSTILEVKLQDMSILlrkAEERHGDIEERLRQLETQLEEKNQEVLRARQ-REKMNEEHNKRLSDT 477
Cdd:COG5185    340 NLTAEIEQGQESL--TENLEAIKEEIENIV---GEVELSKSSEELDSFKDTIESTKESLDEIPQnQRGYAQEILATLEDT 414

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1822435973  478 VdKLLSESNERLQLHLKERMSSLEE----KNALTHELDNTRKQLEE 519
Cdd:COG5185    415 L-KAADRQIEELQRQIEQATSSNEEvsklLNELISELNKVMREADE 459
46 PHA02562
endonuclease subunit; Provisional
 250-524 4.05e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  250 GPGRLLELQDLLDKRSMevAQMKErlgTLSARVGELEDDVDT--ARRDLIKSE-EMNTKYQRDIREAMAQkddmeeRITT 326
Cdd:PHA02562   149 APARRKLVEDLLDISVL--SEMDK---LNKDKIRELNQQIQTldMKIDHIQQQiKTYNKNIEEQRKKNGE------NIAR 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  327 LEKRYLGAQREATSLHDLNDKLENELANTE-DLLKQSED--KTRQLQERLELAEQKLQQTM---RKAETLPEVEAELAQR 400
Cdd:PHA02562   218 KQNKYDELVEEAKTIKAEIEELTDELLNLVmDIEDPSAAlnKLNTAAAKIKSKIEQFQKVIkmyEKGGVCPTCTQQISEG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  401 VAALTKydpsspddstiLEVKLQDMSILLRKAEERHGDIEER----------LRQLETQLEEKNQEVLRARQRekmneeh 470
Cdd:PHA02562   298 PDRITK-----------IKDKLKELQHSLEKLDTAIDELEEImdefneqskkLLELKNKISTNKQSLITLVDK------- 359

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822435973  471 NKRLSDTVDKLLSesnerlqlhlkERMSSLEEKNALTHELDNTRKQLEEAHMDK 524
Cdd:PHA02562   360 AKKVKAAIEELQA-----------EFVDNAEELAKLQDELDKIVKTKSELVKEK 402
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
154-452 5.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  154 LKSLFEHHKALDEKVRER---LRVALERVAALEEELQA-----TSQELmllrEQAAHAqrragDGSEDATEMETPPTQNS 225
Cdd:PRK02224   414 LEELREERDELREREAELeatLRTARERVEEAEALLEAgkcpeCGQPV----EGSPHV-----ETIEEDRERVEELEAEL 484

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  226 AELRPLTSHAKARVTNGTGLRDIE-GPGRLLE----LQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSE 300
Cdd:PRK02224   485 EDLEEEVEEVEERLERAEDLVEAEdRIERLEErredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  301 EMNTKYQRDIREAMAQKDDMEERITTLEK-RYLGAQRE--ATSLHDLNDKLEnELANTEDL----LKQSEDKTRQL---- 369
Cdd:PRK02224   565 EEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIAdaEDEIERLREKRE-ALAELNDErrerLAEKRERKRELeaef 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  370 --------QERLELAEQKLQQTMRKAETLPEVEAELAQRVAAltkydpsspddstiLEVKLQDmsilLRKAEERHGDIEE 441
Cdd:PRK02224   644 dearieeaREDKERAEEYLEQVEEKLDELREERDDLQAEIGA--------------VENELEE----LEELRERREALEN 705

                          330
                   ....*....|.
gi 1822435973  442 RLRQLETQLEE 452
Cdd:PRK02224   706 RVEALEALYDE 716
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 346-535 5.29e-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: 39.66  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  346 DKLENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRKAEtlPEVEAELAQRVAALTKydpsspddstilevKLQDM 425
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGN--EELAREALAEKKSLEK--------------QAEAL 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  426 SILLRKAEERHGDIEERLRQLETQLEEKNQEVLRARQREKMnEEHNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNA 505
Cdd:pfam04012  103 ETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKA-AKAQEAVQTSLGSLSTSSATDSFERIEEKIEEREARAD 181

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1822435973  506 LTHELDNTR---KQLEEAHMDKERMADEVEKVR 535
Cdd:pfam04012  182 AAAELASAVdldAKLEQAGIQMEVSEDVLARLK 214
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 1036-1080 5.30e-03

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188900 [Multi-domain]  Cd Length: 69  Bit Score: 36.90  E-value: 5.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1822435973 1036 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHR 1080
Cdd:cd09501     11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLR 55
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 284-696 5.37e-03

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: 41.25  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  284 ELEDDVDTaRRDLIKSEEMNTKYQRDIREAMAqkddmeeRITTLEKRYLGAQREATSLH-DLNDKLENELANTEDLLKQS 362
Cdd:pfam05483  135 KLEEEIQE-NKDLIKENNATRHLCNLLKETCA-------RSAEKTKKYEYEREETRQVYmDLNNNIEKMILAFEELRVQA 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  363 EDKTRQLQERLELAEQKLQQTmrKAETLPEVEAELAQRVAALTKydpsspddSTILEVKLQDMSILLRKAEERHGDIEER 442
Cdd:pfam05483  207 ENARLEMHFKLKEDHEKIQHL--EEEYKKEINDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  443 lrqleTQLEEKNQEVLRARQREKMNEEHNKRL----SDTVDKLLSESnerLQLHLKERMSSLEEKNALTHELDNTRKQLE 518
Cdd:pfam05483  277 -----TKLQDENLKELIEKKDHLTKELEDIKMslqrSMSTQKALEED---LQIATKTICQLTEEKEAQMEELNKAKAAHS 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  519 EAHMDKERMADEVEKVrLEMEQWRLKTSSMVDPVIPRSHLGSTSDI----RYSLGSSVILEAPGDPFGSSAVLRRQKGRL 594
Cdd:pfam05483  349 FVVTEFEATTCSLEEL-LRTEQQRLEKNEDQLKIITMELQKKSSELeemtKFKNNKEVELEELKKILAEDEKLLDEKKQF 427

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  595 SALRDE-PGKVQTL------NEQEWQRMQ-QAGVLASVAQAFESETEASDQEDDRET-----IFSSADLLSPSGH---SD 658
Cdd:pfam05483  428 EKIAEElKGKEQELifllqaREKEIHDLEiQLTAIKTSEEHYLKEVEDLKTELEKEKlknieLTAHCDKLLLENKeltQE 507

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1822435973  659 AQTLALMLQEQLDAINNE-------IRLIQEEKESTEQRAEEIES 696
Cdd:pfam05483  508 ASDMTLELKKHQEDIINCkkqeermLKQIENLEEKEMNLRDELES 552
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 270-457 6.99e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.78  E-value: 6.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  270 QMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKyqrDIREAMAQkdDMEERITTLEKRylgaqreatsLHDLNDKLE 349
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETE---ALRERLQK--DLEEVRAKLEPY----------LEELQAKLG 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  350 nelANTEDLLKQSEDKTRQLQERLELAEQKLQQTMrkAETLPEVEAELAQRVAAL-TKYDPSSPDDSTILEVKLQDMSIL 428
Cdd:pfam01442   66 ---QNVEELRQRLEPYTEELRKRLNADAEELQEKL--APYGEELRERLEQNVDALrARLAPYAEELRQKLAERLEELKES 140

                          170       180       190
                   ....*....|....*....|....*....|
gi 1822435973  429 LR-KAEERHGDIEERLRQLETQLEEKNQEV 457
Cdd:pfam01442  141 LApYAEEVQAQLSQRLQELREKLEPQAEDL 170
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 151-366 7.69e-03

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: 40.13  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  151 LKALKSLFEHHKALDEKVRERLRVALERVAALEEELQATSQELMLLREQAAHAQRRAGDGSEDATEMETPPTQNSAELRP 230
Cdd:COG4942     29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  231 L--TSHAKARVTNGTGLRDIEGPGRLLELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQR 308
Cdd:COG4942    109 LlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822435973  309 DIREAMAQKddmEERITTLEKRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKT 366
Cdd:COG4942    189 ALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
Caldesmon pfam02029
Caldesmon;
197-564 8.14e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 8.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  197 REQAAHAQRRAGDGSEDA---TEMETPPTQNSAELRpltshakARVTNGTGLRDIEGPGRLLELQDLLDKRSMEVAQMKE 273
Cdd:pfam02029   12 RRRAREERRRQKEEEEPSgqvTESVEPNEHNSYEED-------SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  274 RLGTLSARVGELEDDVDTARRDliKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLgaqreatslhdlNDKLENELA 353
Cdd:pfam02029   85 RQKEFDPTIADEKESVAERKEN--NEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQ------------ENKWSTEVR 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  354 NTEDLLKQSEDKTRQLQERLELA----EQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSILL 429
Cdd:pfam02029  151 QAEEEGEEEEDKSEEAEEVPTENfakeEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  430 RKAEERHGDIE---------ERLRQLETQLEEKNQEVLRARQREKMNE-EHNKRLSDTVDKLLSESNERLQLHLKERMSS 499
Cdd:pfam02029  231 SQSQEREEEAEvfleaeqklEELRRRRQEKESEEFEKLRQKQQEAELElEELKKKREERRKLLEEEEQRRKQEEAERKLR 310

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  500 LEEknaltheldntrkqleeahmDKERMADEVEKVRLEMEQWRLK--TSSMVD---PVIPRSHLGSTSDI 564
Cdd:pfam02029  311 EEE--------------------EKRRMKEEIERRRAEAAEKRQKlpEDSSSEgkkPFKCFSPKGSSLKI 360
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 304-463 8.32e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 8.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  304 TKYQRDIREAMAQKDDMEERITTLE---KRYLGAQREATSLHDLNDKLENELANTEDLLKQSEDKTRQLQERLELAEQKL 380
Cdd:pfam00529   54 TDYQAALDSAEAQLAKAQAQVARLQaelDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  381 QQTMRKAETLPEVEAELAQrvaALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIEERLRQLETQLEEKNQEVLRA 460
Cdd:pfam00529  134 PIGGISRESLVTAGALVAQ---AQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERT 210


                   ...
gi 1822435973  461 RQR 463
Cdd:pfam00529  211 EIR 213
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 928-985 8.57e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 35.68  E-value: 8.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822435973  928 VVAWLElWVGMPaWYVAACRANVKSGAIMSALSDTEIQrEIGISNPLHRLKLRLAIQE 985
Cdd:cd09487      2 VAEWLE-SLGLE-QYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAIQR 56
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 291-488 9.00e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 9.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  291 TARRDLIKSEEMNTKYQRDIREAMAQKDDMEERITTLEKRYLGAQREATSLHDLNDKLENELANTEdllKQSEDKTRQLQ 370
Cdd:COG3883     13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELG 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  371 ERLElAEQKLQQTMRKAETLPEVE--AELAQRVAALTKYdpSSPDDSTI---------LEVKLQDMSILLRKAEERHGDI 439
Cdd:COG3883     90 ERAR-ALYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKI--ADADADLLeelkadkaeLEAKKAELEAKLAELEALKAEL 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1822435973  440 EERLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNER 488
Cdd:COG3883    167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 442-548 9.04e-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: 38.17  E-value: 9.04e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973   442 RLRQLETQLEEKNQEVLRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMSSLEEKNALTHELDN--TRKQLEE 519
Cdd:smart01071   33 KQRDIHQARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLREEELSPETPTYNEMLAELQDQLKKELEEANgdSEGLLEE 112

                            90       100
                    ....*....|....*....|....*....
gi 1822435973   520 AHMDKERMADEVEKVRLEMEQWRLKTSSM 548
Cdd:smart01071  113 LKKHRDKLKKEQKELRKKLDELEKEEKKK 141
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 256-386 9.06e-03

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: 38.73  E-value: 9.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  256 ELQDLLDKRSMEVAQMKERLGTLSARVGELEDDVDTARRDLIKSEEMNTKYQRDIREA-MAQKDDMEERITTLEKRYLGA 334
Cdd:pfam15619   57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822435973  335 QREATSLH---DLNDK-LENELANTEDLLKQSEDKTRQLQERLELAEQKLQQTMRK 386
Cdd:pfam15619  137 DEKIQDLErklELENKsFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 319-517 9.13e-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: 39.79  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  319 DMEERITTLEKRYLGAQREATSLHDLNDKLEN---ELANTEDLLKQ--SED----------------------KTRQLQE 371
Cdd:pfam15905   98 ALEEELEKVEAKLNAAVREKTSLSASVASLEKqllELTRVNELLKAkfSEDgtqkkmsslsmelmklrnkleaKMKEVMA 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  372 RLELAEQKLQQTMRKAETLPEVEAELAQRVAALTKYDPSSPDDSTILEVKLQDMSILLRKAEERHGDIeerlRQLETQLE 451
Cdd:pfam15905  178 KQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDI----AQLEELLK 253

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822435973  452 EKNQEVLRARQREKMNEEHnkrLSDTVDKLlsesNERLQL--HLKERMSSLEEKNALTH--ELDNTRKQL 517
Cdd:pfam15905  254 EKNDEIESLKQSLEEKEQE---LSKQIKDL----NEKCKLleSEKEELLREYEEKEQTLnaELEELKEKL 316
 
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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