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Conserved domains on  [gi|767968918|ref|XP_011543617|]
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liprin-alpha-1 isoform X13 [Homo sapiens]

Protein Classification

liprin-alpha( domain architecture ID 13528491)

liprin-alpha belongs to the LAR (leukocyte common antigen-related) family or transmembrane protein-tyrosine phosphatase-interacting proteins and is involved in formation of the presynaptic active zone

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 ...
 1002-1067 1.08e-42

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: 149.55  E-value: 1.08e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918 1002 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1067
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 ...
 885-955 1.55e-42

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: 149.25  E-value: 1.55e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  885 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 955
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 ...
 1087-1158 3.80e-42

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: 148.23  E-value: 3.80e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1087 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-523 2.46e-16

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: 84.60  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  243 LSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERI 322
Cdd:COG1196   225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  323 TTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAAL 402
Cdd:COG1196   305 ARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  403 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 482
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767968918  483 vESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:COG1196   455 -EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-662 3.48e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.16  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNvCREQLLEREEEIAELKAE----RNN 120
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQiaslNNE 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   121 TRLLLEHLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 193
Cdd:TIGR02168  402 IERLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   194 EELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIE------LQEIISKqsREQS 267
Cdd:TIGR02168  482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE--LISVDEGYEAAIEaalggrLQAVVVE--NLNA 557

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   268 QMKErLASLSSH----VTELEEDLDTAR--------------------KDLIKSEE-----MNTKLQR-----DVREAMA 313
Cdd:TIGR02168  558 AKKA-IAFLKQNelgrVTFLPLDSIKGTeiqgndreilkniegflgvaKDLVKFDPklrkaLSYLLGGvlvvdDLDNALE 636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   314 Q--KEDMEERITTLE-----KRYLAA-QREATSVHDLN-----DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ 380
Cdd:TIGR02168  637 LakKLRPGYRIVTLDgdlvrPGGVITgGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   381 TLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL------ 454
Cdd:TIGR02168  717 LRKELE---ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieq 793

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   455 -----------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:TIGR02168  794 lkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   524 GRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASV-LANVAQAFESDAdvSD 602
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEY--SL 951

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968918   603 GEDDRDTLLSSVDLLSPSGQADAHTLAMMLQE----QLDAInkeirliqEEKENTEQRAEEIES 662
Cdd:TIGR02168  952 TLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAI--------EEYEELKERYDFLTA 1007
 
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 ...
 1002-1067 1.08e-42

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: 149.55  E-value: 1.08e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918 1002 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1067
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 ...
 885-955 1.55e-42

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: 149.25  E-value: 1.55e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  885 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 955
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 ...
 1087-1158 3.80e-42

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: 148.23  E-value: 3.80e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1087 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:cd09568     1 DVLVWSNERVIRWVQSIGLREYANNLLESGVHGALIALDETFDANSFALALQIPTQNTQARQILEREFNNLL 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-523 2.46e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.60  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  243 LSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERI 322
Cdd:COG1196   225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  323 TTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAAL 402
Cdd:COG1196   305 ARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  403 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 482
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767968918  483 vESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:COG1196   455 -EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 270-517 9.81e-16

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: 82.80  E-value: 9.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 349
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   350 IANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERH-------GNIEERLRQMEAQ 422
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   423 LEEKNQELQRARQREKMNEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 499
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250
                   ....*....|....*...
gi 767968918   500 LVLNIEALRAELDHMRLR 517
Cdd:TIGR02168  913 LRRELEELREKLAQLELR 930
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1001-1065 8.78e-13

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: 64.21  E-value: 8.78e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918  1001 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1065
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-662 3.48e-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: 68.16  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNvCREQLLEREEEIAELKAE----RNN 120
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQiaslNNE 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   121 TRLLLEHLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 193
Cdd:TIGR02168  402 IERLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   194 EELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIE------LQEIISKqsREQS 267
Cdd:TIGR02168  482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE--LISVDEGYEAAIEaalggrLQAVVVE--NLNA 557

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   268 QMKErLASLSSH----VTELEEDLDTAR--------------------KDLIKSEE-----MNTKLQR-----DVREAMA 313
Cdd:TIGR02168  558 AKKA-IAFLKQNelgrVTFLPLDSIKGTeiqgndreilkniegflgvaKDLVKFDPklrkaLSYLLGGvlvvdDLDNALE 636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   314 Q--KEDMEERITTLE-----KRYLAA-QREATSVHDLN-----DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ 380
Cdd:TIGR02168  637 LakKLRPGYRIVTLDgdlvrPGGVITgGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   381 TLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL------ 454
Cdd:TIGR02168  717 LRKELE---ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieq 793

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   455 -----------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:TIGR02168  794 lkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   524 GRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASV-LANVAQAFESDAdvSD 602
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEY--SL 951

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968918   603 GEDDRDTLLSSVDLLSPSGQADAHTLAMMLQE----QLDAInkeirliqEEKENTEQRAEEIES 662
Cdd:TIGR02168  952 TLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAI--------EEYEELKERYDFLTA 1007
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-512 2.89e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.68  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:PRK02224  233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLD 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  238 SSDGS--LSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQ 314
Cdd:PRK02224  306 DADAEavEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAE 394
Cdd:PRK02224  386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQP 460

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  395 L--AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------L 464
Cdd:PRK02224  461 VegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraE 540

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 767968918  465 HLKERMAALEDKNSLLRevESAKKQLEETQhDKDQLVLNIEALRAELD 512
Cdd:PRK02224  541 ELRERAAELEAEAEEKR--EAAAEAEEEAE-EAREEVAELNSKLAELK 585
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 156-464 3.99e-08

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: 57.83  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   156 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPST 233
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   234 SGK---------RSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLaslsshvtelEEDLDTARKDLIKSEEMNTKL 304
Cdd:pfam17380  346 RERelerirqeeRKRELERIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKILEEERQRKI 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   305 QRDVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:pfam17380  416 QQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   373 LAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 446
Cdd:pfam17380  496 ILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573

                          330
                   ....*....|....*...
gi 767968918   447 LSDTVDKLLSESNERLQL 464
Cdd:pfam17380  574 EREMMRQIVESEKARAEY 591
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 68-655 1.71e-07

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: 55.89  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    68 LHEVGHERDSLQRQLNTA-----------------LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLEC 130
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESnelhekqkfylrqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   131 LVSR--HERSLRMTVVKRQAQSPAGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRVALERCSLLEEE 195
Cdd:pfam15921  160 LKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELDTEISYLKGR 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   196 LGATHKELMILKEQNNQKKTL-----TDGV--LDINHEQENTPST---SGKRSSDGSLSHEedlakvielQEIISKQSRE 265
Cdd:pfam15921  240 IFPVEDQLEALKSESQNKIELllqqhQDRIeqLISEHEVEITGLTekaSSARSQANSIQSQ---------LEIIQEQARN 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   266 QSQMKER-LASLSSHVTELEEDLDTARKD-------------LIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKRY 329
Cdd:pfam15921  311 QNSMYMRqLSDLESTVSQLRSELREAKRMyedkieelekqlvLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKRE 390

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ-----------------ERLELAEQKLQQTLRKA------- 385
Cdd:pfam15921  391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQrleallkamksecqgqmERQMAAIQGKNESLEKVssltaql 470

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   386 ----ETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE- 460
Cdd:pfam15921  471 estkEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEc 550

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   461 ---RLQLHLKERM-----------------------AALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM 514
Cdd:pfam15921  551 ealKLQMAEKDKVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   515 RLRGASL-HHGRPHLGSVPDF---RFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQ-TLNEQDWERAQQASVLAN 589
Cdd:pfam15921  631 ELEKVKLvNAGSERLRAVKDIkqeRDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQ 710

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918   590 VAQAFESdADVSDGEDDRDTLLSSVDLLSPSGQADA-HTLAMMLQEQLDAINKEIRLIQEEKENTEQ 655
Cdd:pfam15921  711 TRNTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1088-1158 2.31e-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: 49.22  E-value: 2.31e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918   1088 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1010-1065 5.20e-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: 5.20e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918   1010 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1065
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 885-951 5.46e-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: 5.46e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918    885 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 951
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1088-1158 6.52e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 6.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  1088 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-435 1.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717   228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  204 MILKEQNNQKKTltdgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTEL 283
Cdd:COG4717   305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  284 EEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDK 363
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEE 447

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  364 NRQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALSKAEERHGnieeRLRQMEAQLEEKNQELQRARQ 435
Cdd:COG4717   448 LEELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 324-445 1.92e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 41.57  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  324 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 390
Cdd:cd07680    61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  391 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 445
Cdd:cd07680   141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 887-949 2.65e-03

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: 37.63  E-value: 2.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968918   887 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 949
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
 
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 ...
 1002-1067 1.08e-42

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: 149.55  E-value: 1.08e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918 1002 MNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRL 1067
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 ...
 885-955 1.55e-42

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: 149.25  E-value: 1.55e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  885 FAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLT 955
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 ...
 1087-1158 3.80e-42

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: 148.23  E-value: 3.80e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1087 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1158
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 ...
 1006-1065 1.09e-28

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: 109.55  E-value: 1.09e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918 1006 WIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1065
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 ...
 892-950 2.06e-26

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: 103.07  E-value: 2.06e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767968918  892 TVVVWLELWVGMPaWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 950
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 ...
 1095-1156 2.57e-24

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: 97.23  E-value: 2.57e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1095 RVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNN 1156
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 ...
 1087-1158 8.23e-22

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: 90.19  E-value: 8.23e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1087 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:cd09570     1 DPVVWTNQRVIKWARSIDLKEYADNLRDSGVHGALMVLEPSFNSDTMATALGIPSSKNIIRRHLTTEMEALV 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-523 2.46e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.60  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  243 LSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERI 322
Cdd:COG1196   225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  323 TTLEKRYLAAQREAtsvhdlnDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAAL 402
Cdd:COG1196   305 ARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAEL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  403 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLRE 482
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767968918  483 vESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:COG1196   455 -EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SAM_kazrin_repeat1 cd09564
SAM domain of kazrin proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of kazrin ...
 886-950 2.62e-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: 74.41  E-value: 2.62e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918  886 AQWDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQE 950
Cdd:cd09564     2 SRWKADMVLAWLEVVMHMPM-YSKACAENVKSGKVLLGLSDSELESGLGISNVLHRRKLRLAIEE 65
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 270-517 9.81e-16

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: 82.80  E-value: 9.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENE 349
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   350 IANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERH-------GNIEERLRQMEAQ 422
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELtllneeaANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   423 LEEKNQELQRARQREKMNEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQ 499
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250
                   ....*....|....*...
gi 767968918   500 LVLNIEALRAELDHMRLR 517
Cdd:TIGR02168  913 LRRELEELREKLAQLELR 930
SAM_liprin-beta1,2_repeat3 cd09569
SAM domain of liprin-beta proteins repeat 3; SAM (sterile alpha motif) domain repea t3 of ...
 1087-1158 1.31e-15

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: 72.49  E-value: 1.31e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1087 DVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:cd09569     1 EVVLWTNHRVMEWLRSVDLAEYAPNLRGSGVHGALMVLEPRFTAETLAALLNIPPNKTLLRRHLATHFNQLL 72
SAM_kazrin_repeat2 cd09567
SAM domain of kazrin proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of kazrin ...
 1001-1065 4.01e-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: 70.90  E-value: 4.01e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918 1001 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1065
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 ...
 1001-1065 5.09e-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: 70.42  E-value: 5.09e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918 1001 DMNHEWIgNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1065
Cdd:cd09566     1 KLDTHWV-LRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLL-HLKVTSALHHASIRRGIQVLR 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-512 9.85e-15

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: 79.72  E-value: 9.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIA 351
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   352 NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHG----NIEERLRQMEAQLEEKN 427
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaeleELESRLEELEEQLETLR 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   428 QELQRARQREKMNEEHNKRLSDTVdKLLSESNERLQLHLKERMAALE--DKNSLLREVESAKKQLEETQHDKDQLVLNIE 505
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEELQEELERLEEALE 464


                   ....*..
gi 767968918   506 ALRAELD 512
Cdd:TIGR02168  465 ELREELE 471
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 1001-1065 8.78e-13

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: 64.21  E-value: 8.78e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918  1001 DMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGIMCLR 1065
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLL-KLGVTLLGHRKKILYAIQRLK 64
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 192-511 2.49e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 71.64  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   192 LEEELGATHKELMILKEQNNQKKTLTDGVLDinheqentpstsgkRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKE 271
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQ--------------ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD------------VREAMAQKEDMEERITTLEKRYLAAQREATSV 339
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   340 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKAEERHGNIEERLRQM 419
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE----------ELEEELEELEAALRDLESRLGDLKKERDEL 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   420 EAQLEEknqelqrarQREKMNEehnkrlsdtvdklLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE---TQHD 496
Cdd:TIGR02169  895 EAQLRE---------LERKIEE-------------LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELS 952

                          330
                   ....*....|....*
gi 767968918   497 KDQLVLNIEALRAEL 511
Cdd:TIGR02169  953 LEDVQAELQRVEEEI 967
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-492 3.19e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 71.24  E-value: 3.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   187 ERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQ 266
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   267 SQMKERLASLSSHVTELEEDLDTARKDLikseemnTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKL 346
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEI-------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   347 ENEIANKDSMHRQTEDKNRQLQERLELAEQ---KLQQTLRKAET-LPEVEAELAQRVAALSKAEERHGNIEERLRQMEaq 422
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESeLEALLNERASLEEALALLRSELEELSEELRELE-- 907

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968918   423 leEKNQELQRARQ--REKMNEEHNK--RLSDTVDKLLSESNERLQL---HLKERMAALEDKNSLLR-EVESAKKQLEE 492
Cdd:TIGR02168  908 --SKRSELRRELEelREKLAQLELRleGLEVRIDNLQERLSEEYSLtleEAEALENKIEDDEEEARrRLKRLENKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-511 3.58e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  268 QMKERLASLSSHVTELEEDLD-------TARKDLIKSEEMNtklQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVH 340
Cdd:COG1196   183 ATEENLERLEDILGELERQLEplerqaeKAERYRELKEELK---ELEAELLLLKLRELEAELEELEAELEELEAELEELE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  341 DLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTL----RKAETLPEVEAELAQRVAALSKAEERHGNIEERL 416
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiaRLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  417 RQMEAQLEEKNQELQRARQREkmnEEHNKRLSDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVESAKKQLEETQHD 496
Cdd:COG1196   340 EELEEELEEAEEELEEAEAEL---AEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLER 415

                         250
                  ....*....|....*
gi 767968918  497 KDQLVLNIEALRAEL 511
Cdd:COG1196   416 LERLEEELEELEEAL 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-463 5.92e-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: 70.47  E-value: 5.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    74 ERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRmTVVKRQAQSPAG 153
Cdd:TIGR02168  678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   154 VSS----EVEVLKALKSLFEHHKALDEK---VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTltdgvldinhe 226
Cdd:TIGR02168  756 LTEleaeIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------- 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   227 qentpstsgkrssdGSLSHEEDLAKVIELQEIISKQSReqsQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQR 306
Cdd:TIGR02168  825 --------------RLESLERRIAATERRLEDLEEQIE---ELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   307 DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhrQTEDKNRQLQERL-ELAEQKLQQTLRKA 385
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERLsEEYSLTLEEAEALE 960

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   386 ETLPEVEAELAQRVAALSKAEERHGNI-----------EERLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSD 449
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLENKIKELGPVnlaaieeyeelKERYDFLTAQKE----DLTEAKETleeaiEEIDREARERFKD 1036

                          410
                   ....*....|....
gi 767968918   450 TVDKLlsesNERLQ 463
Cdd:TIGR02168 1037 TFDQV----NENFQ 1046
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-465 9.93e-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: 69.70  E-value: 9.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   156 SEVEVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEELGATHKELMILK----EQNNQKKTLTDGVLDINHEQENTp 231
Cdd:TIGR02168  223 RELELALLVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIEELQKELYALANEISRL- 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   232 sTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQmkERLASLSSHVTELEEDLDTArkdliksEEMNTKLQRDVREA 311
Cdd:TIGR02168  301 -EQQKQILRERLANLERQLEELEAQLEELESKLDELA--EELAELEEKLEELKEELESL-------EAELEELEAELEEL 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   312 MAQKEDMEERITTLEKRYLAAQREATSvhdlndkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKA--ETLP 389
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIAS-------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELE 443

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918   390 EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 465
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-433 2.04e-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: 68.93  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    54 LRETQETLALTQGKLHEVGHERDSLQRQLNTAlpQEFAALTKELNvcREQLLEREEEIAELKAERNNTRLLLEHLECLVS 133
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKA--ERYKELKAELR--ELELALLVLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   134 RHERSLrmtvvkrqaqspagvssevevlKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQk 213
Cdd:TIGR02168  257 ELTAEL----------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   214 ktltdgvLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARK 292
Cdd:TIGR02168  314 -------LERQLEELEAQLEELESKLDELAEELAELEEKLeELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   293 DLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHdlNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALE 464

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918   373 LAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 433
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-662 3.48e-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: 68.16  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNvCREQLLEREEEIAELKAE----RNN 120
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQiaslNNE 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   121 TRLLLEHLECLVSRHER------SLRMTVVKRQAQSPAGVSSEVE-VLKALKSLFEHHKALDEKVRERLRVALERCSLLE 193
Cdd:TIGR02168  402 IERLEARLERLEDRRERlqqeieELLKKLEEAELKELQAELEELEeELEELQEELERLEEALEELREELEEAEQALDAAE 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   194 EELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIE------LQEIISKqsREQS 267
Cdd:TIGR02168  482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE--LISVDEGYEAAIEaalggrLQAVVVE--NLNA 557

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   268 QMKErLASLSSH----VTELEEDLDTAR--------------------KDLIKSEE-----MNTKLQR-----DVREAMA 313
Cdd:TIGR02168  558 AKKA-IAFLKQNelgrVTFLPLDSIKGTeiqgndreilkniegflgvaKDLVKFDPklrkaLSYLLGGvlvvdDLDNALE 636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   314 Q--KEDMEERITTLE-----KRYLAA-QREATSVHDLN-----DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQ 380
Cdd:TIGR02168  637 LakKLRPGYRIVTLDgdlvrPGGVITgGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   381 TLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL------ 454
Cdd:TIGR02168  717 LRKELE---ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieq 793

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   455 -----------LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:TIGR02168  794 lkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   524 GRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASV-LANVAQAFESDAdvSD 602
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEY--SL 951

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968918   603 GEDDRDTLLSSVDLLSPSGQADAHTLAMMLQE----QLDAInkeirliqEEKENTEQRAEEIES 662
Cdd:TIGR02168  952 TLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAI--------EEYEELKERYDFLTA 1007
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 885-949 4.33e-11

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: 59.55  E-value: 4.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918  885 FAQWDGPTVVVWL-ELWVGMpawYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQ 949
Cdd:cd09563     1 FAEWSTEQVCDWLaELGLGQ---YVDECRRWVKSGQTLLKASPQELEKELGIKHPLHRKKLQLALQ 63
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 246-442 8.73e-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: 63.41  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  246 EEDLAKVIELQEIISkqsrEQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:COG1579     3 PEDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  326 EKRylaaQREATSVHDLNDkLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQqtlrkaetlpEVEAELAQRVAALSKA 405
Cdd:COG1579    79 EEQ----LGNVRNNKEYEA-LQKEIESLKRRISDLEDEILELMERIEELEEELA----------ELEAELAELEAELEEK 143

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767968918  406 EERhgnIEERLRQMEAQLEEKNQElqRARQREKMNEE 442
Cdd:COG1579   144 KAE---LDEELAELEAELEELEAE--REELAAKIPPE 175
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 38-508 2.11e-10

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: 65.45  E-value: 2.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    38 QLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHER--DSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELK 115
Cdd:TIGR00606  353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   116 AERNNTRLLLEHLECLVSRHERSLRMtvVKRQAQSPAGVSSEV-----EVLKALK--SLFEHHKALDEKVRERLRVALER 188
Cdd:TIGR00606  433 DEKKGLGRTIELKKEILEKKQEELKF--VIKELQQLEGSSDRIleldqELRKAERelSKAEKNSLTETLKKEVKSLQNEK 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   189 CSLLEE--ELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPStsgkRSSDGSLSHEEDLAKVIELQEIISKQSREQ 266
Cdd:TIGR00606  511 ADLDRKlrKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKS----RHSDELTSLLGYFPNKKQLEDWLHSKSKEI 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   267 SQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQkEDMEERITTLEKRYLAAQREA---TSVHDLN 343
Cdd:TIGR00606  587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRamlAGATAVY 665

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAET-LPEVEAELA----QRVAALSKAEERHGNIEERLRQ 418
Cdd:TIGR00606  666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKkkekRRDEMLGLAPGRQSIIDLKEKE 745

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   419 MEaQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESN---------ERLQLHLKE------RMAALEDKNSLLREV 483
Cdd:TIGR00606  746 IP-ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDverkiaQQAAKLQGSDLDRTV 824

                          490       500
                   ....*....|....*....|....*
gi 767968918   484 ESAKKQLEETQHDKDQLVLNIEALR 508
Cdd:TIGR00606  825 QQVNQEKQEKQHELDTVVSKIELNR 849
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 44-512 2.24e-10

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: 65.38  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    44 LEERDRLLDTLR-ETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:TIGR00618  417 SAFRDLQGQLAHaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   123 LLLEHLECLVSRHERSLRMTVVkrQAQSPAGVSSEVEvlkALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKE 202
Cdd:TIGR00618  497 LELQEEPCPLCGSCIHPNPARQ--DIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   203 LMILKEQNNQKKTLTDGVLDINHE-QENTPSTSGKRSSDGSLSHEEDLakviELQEIISKQ--SREQSQMKERLASLSSH 279
Cdd:TIGR00618  572 FSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLR----KLQPEQDLQdvRLHLQQCSQELALKLTA 647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   280 VTELEEDLdtarkdlikseemntkLQRDVREAMAQKEDMEERitTLEKRYLAAQREATSVHDLNDKLEnEIANKDSMHR- 358
Cdd:TIGR00618  648 LHALQLTL----------------TQERVREHALSIRVLPKE--LLASRQLALQKMQSEKEQLTYWKE-MLAQCQTLLRe 708

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   359 --QTEDKNRQLQERLELAEQKLQQTLR-KAETLPEVEAEL-AQRVAALSKAEERHGNIEER----------LRQMEAQLE 424
Cdd:TIGR00618  709 leTHIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELmHQARTVLKARTEAHFNNNEEvtaalqtgaeLSHLAAEIQ 788

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   425 EKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNI 504
Cdd:TIGR00618  789 FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868


                   ....*...
gi 767968918   505 EALRAELD 512
Cdd:TIGR00618  869 AKIIQLSD 876
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 233-508 2.69e-10

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 65.09  E-value: 2.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   233 TSGKRSSDG-SLSHEEDLAKVIELQEIISKqsreqsqMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA 311
Cdd:TIGR02169  656 TGGSRAPRGgILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   312 MAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAnkdsmhRQTEDKNrQLQERLELAEQKLQQtlrkaETLPEV 391
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE------ELEEDLH-KLEEALNDLEARLSH-----SRIPEI 796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   392 EAElaqrvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRArqREKMNEEHNKRLS-----DTVDKLLSESN---ERLQ 463
Cdd:TIGR02169  797 QAE-------LSKLEEEVSRIEARLREIEQKLNRLTLEKEYL--EKEIQELQEQRIDlkeqiKSIEKEIENLNgkkEELE 867

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 767968918   464 LHLKERMAALED----KNSLLREVESAKKQLEETQHDKDQLVLNIEALR 508
Cdd:TIGR02169  868 EELEELEAALRDlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-512 2.89e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.68  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  158 VEVLKALKSLFEHHkaldEKVRERLRVALERCSLLEEELGATHKELMILKEQnnqKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:PRK02224  233 RETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLD 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  238 SSDGS--LSHEEDLAKVI-ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQ 314
Cdd:PRK02224  306 DADAEavEARREELEDRDeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQklqqtLRKAETLPEVEAE 394
Cdd:PRK02224  386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA-----LLEAGKCPECGQP 460

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  395 L--AQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLS--DTVDKLLSESNERLQ------L 464
Cdd:PRK02224  461 VegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEekreraE 540

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 767968918  465 HLKERMAALEDKNSLLRevESAKKQLEETQhDKDQLVLNIEALRAELD 512
Cdd:PRK02224  541 ELRERAAELEAEAEEKR--EAAAEAEEEAE-EAREEVAELNSKLAELK 585
mukB PRK04863
chromosome partition protein MukB;
249-509 6.40e-10

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 63.82  E-value: 6.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  249 LAKVIE---LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTL 325
Cdd:PRK04863  337 LNLVQTalrQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQ 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  326 EKR---YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ-------------QTLRKAetLP 389
Cdd:PRK04863  410 QTRaiqYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqaahsqfeqayQLVRKI--AG 487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  390 EVEAELAQRVA--ALSKAEErHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDkllseSNERLQLHLK 467
Cdd:PRK04863  488 EVSRSEAWDVAreLLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-----DEDELEQLQE 561

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767968918  468 ERMAALEDKNSllrEVESAKKQLEETQHDKDQLVLNIEALRA 509
Cdd:PRK04863  562 ELEARLESLSE---SVSEARERRMALRQQLEQLQARIQRLAA 600
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 192-523 1.49e-09

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: 62.35  E-value: 1.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   192 LEEELGATHKELMILK-EQNNQKKTLTDGVLDINH------EQENTPSTSGKRSSDGSLSHEEDLAKviELQEIISKQSR 264
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKdEQNKIKKQLSEKQKELEQnnkkikELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEK 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   265 EQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREamaqKEDMEERIttlekrylaaQREATSVHDLND 344
Cdd:TIGR04523  322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKL----------KKENQSYKQEIK 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   345 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE 424
Cdd:TIGR04523  388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   425 EKNQELQRARQREKMN-EEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDKNSLL----REVESAKKQLE------ET 493
Cdd:TIGR04523  468 TQLKVLSRSINKIKQNlEQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLkekiEKLESEKKEKEskisdlED 545

                          330       340       350
                   ....*....|....*....|....*....|
gi 767968918   494 QHDKDQLVLNIEALRAELDHMRLRGASLHH 523
Cdd:TIGR04523  546 ELNKDDFELKKENLEKEIDEKNKEIEELKQ 575
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-515 1.83e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  113 ELKAERNNTRLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEV-EVLKALKSLFEHHKALDEKVR--ERLRVALERC 189
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLeELKKKLKELEKRLEELEERHElyEEAKAKKEEL 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  190 SLLEEELGATHKELMI--LKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSD--------------GSLSHEEDLAkvi 253
Cdd:PRK03918  375 ERLKKRLTGLTPEKLEkeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkcpvcGRELTEEHRK--- 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  254 elqEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqRDVREAMAQKEDMEERITTLEKRYL-AA 332
Cdd:PRK03918  452 ---ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-----IKLKELAEQLKELEEKLKKYNLEELeKK 523

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  333 QREATSVHDLNDKLENEIAN-KDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLP-EVEAELAQRVAALSKAEER 408
Cdd:PRK03918  524 AEEYEKLKEKLIKLKGEIKSlKKELEKLEELKKKlaELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNE 603

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  409 HgnieERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKN-SLLREVESAK 487
Cdd:PRK03918  604 Y----LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYlELSRELAGLR 679

                         410       420
                  ....*....|....*....|....*...
gi 767968918  488 KQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PRK03918  680 AELEELEKRREEIKKTLEKLKEELEERE 707
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
152-492 1.87e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  152 AGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTL---TDGVLDINHEQE 228
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekAEEYIKLSEFYE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  229 NTpstsgkrsSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQR-- 306
Cdd:PRK03918  304 EY--------LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEle 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  307 --DVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLR 383
Cdd:PRK03918  376 rlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElKKAIEELKKAKGKCPVCGRELTEEHRKELLE 455

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  384 K-AETLPEVEAELAQRVAALSKAEERHGNIEE---------RLRQMEAQLEEKNQELqrarqrEKMNEEHNKRLSDTVDK 453
Cdd:PRK03918  456 EyTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKL------KKYNLEELEKKAEEYEK 529

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 767968918  454 LLSESN--ERLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:PRK03918  530 LKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEE 570
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-521 2.26e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   282 ELEEDLDTARKDLIKSE----EMNTKLQRDVREA-MAQK-EDMEERITTLEKRYLAAQreatsVHDLNDKLENEIANKDS 355
Cdd:TIGR02168  176 ETERKLERTRENLDRLEdilnELERQLKSLERQAeKAERyKELKAELRELELALLVLR-----LEELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   356 MHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 435
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   436 RekmNEEHNKRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSLLREVEsakKQLEETQHDKDQLVLNIEALRAELDH 513
Cdd:TIGR02168  331 K---LDELAEELAELEEKLeeLKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIER 404


                   ....*...
gi 767968918   514 MRLRGASL 521
Cdd:TIGR02168  405 LEARLERL 412
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 305-520 3.52e-09

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: 60.16  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  305 QRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  385 AETLpevEAELAQRVAALSK------------------AEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 446
Cdd:COG4942    99 LEAQ---KEELAELLRALYRlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968918  447 LSDTVDKlLSESNERLQLHLKERMAALedkNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGAS 520
Cdd:COG4942   176 LEALLAE-LEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-492 4.86e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196   337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  125 LEHLEcLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196   417 ERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIE--LQEIISKQSREQSQMKERLAS-LSSHVT 281
Cdd:COG1196   496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAaaLQNIVVEDDEVAAAAIEYLKAaKAGRAT 575

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  282 ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERittleKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:COG1196   576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY-----YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  362 DKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHgniEERLRQMEAQLEEKNQELQRARQREKMNE 441
Cdd:COG1196   651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA---LLAEEEEERELAEAEEERLEEELEEEALE 727

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767968918  442 EHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:COG1196   728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 303-494 6.05e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.46  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  303 KLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTL 382
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  383 RKAETLPEVEA--------ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL 454
Cdd:COG3883    97 RSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767968918  455 LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 494
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 250-442 6.61e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.46  E-value: 6.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKR- 328
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARALYRSg 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  329 ----YLAAQREATSVHDLNDKLE--NEI--ANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAET-LPEVEAELAQ 397
Cdd:COG3883   100 gsvsYLDVLLGSESFSDFLDRLSalSKIadADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAaKAELEAQQAE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767968918  398 RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEE 442
Cdd:COG3883   180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 256-492 6.88e-09

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: 59.39  E-value: 6.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  336 AtsvhdlnDKLENEIANkdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEER 415
Cdd:COG4942    99 L-------EAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918  416 LRQMEAQLEEKNQELQraRQREKMNEEHNKRlsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:COG4942   169 LEAERAELEALLAELE--EERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-442 7.26e-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: 60.47  E-value: 7.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALpqEFAALTKElnvcreqllereeeiaelKAERNNTRLL 124
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE--RYQALLKE------------------KREYEGYELL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   125 LEHLEclvsrHERSLRmtvvkrqaqspagvssevEVLKALKSLFEHHKALDEKVRERLrvalERCSLLEEELGATHKELM 204
Cdd:TIGR02169  230 KEKEA-----LERQKE------------------AIERQLASLEEELEKLTEEISELE----KRLEEIEQLLEELNKKIK 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   205 ILKEqnNQKKTLTDGVLDINHEQENTpstsgKRSSDGSLSHEEDLA-KVIELQEIISKQ-------SREQSQMKERLASL 276
Cdd:TIGR02169  283 DLGE--EEQLRVKEKIGELEAEIASL-----ERSIAEKERELEDAEeRLAKLEAEIDKLlaeieelEREIEEERKRRDKL 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   277 SSHVTELEEDLDTARKDLiksEEMNTKLQRDVREAMAQKEDME---ERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:TIGR02169  356 TEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGI 432

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   354 DSMHRQTEDKNRQLQERLELAEQKLQQTlrkaetlpeveaelaqrVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRA 433
Cdd:TIGR02169  433 EAKINELEEEKEDKALEIKKQEWKLEQL-----------------AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495


                   ....*....
gi 767968918   434 RQREKMNEE 442
Cdd:TIGR02169  496 EAQARASEE 504
PTZ00121 PTZ00121
MAEBL; Provisional
 145-499 1.16e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  145 KRQAQSPAGVSSEVEVLKALKSLFEHHKALDE--KVRERLRVALERCSLLEEELGATHkelmiLKEQNNQKKtltdgvld 222
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAK-------- 1483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  223 iNHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERlASLSSHVTELEEdldtARK--DLIKSEEM 300
Cdd:PTZ00121 1484 -KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAKKAEE----KKKadELKKAEEL 1557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  301 ntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTED---------KNRQLQERL 371
Cdd:PTZ00121 1558 --KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeelkKAEEEKKKV 1635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  372 ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTV 451
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 767968918  452 DKLlsesnERLQLHLKERMAALEDknsLLREVESAKKQLEETQHDKDQ 499
Cdd:PTZ00121 1716 KKA-----EELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEE 1755
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
285-515 1.29e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  285 EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlndkleNEIankdsmhrqtEDKN 364
Cdd:PRK03918  158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-----------NEI----------SSEL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQ---LEEKNQELQRARQREKMNE 441
Cdd:PRK03918  217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEieeLEEKVKELKELKEKAEEYI 296

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968918  442 EHNKRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQL---VLNIEALRAELDHMR 515
Cdd:PRK03918  297 KLSEFYEEYLDELreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEAKAKKEELE 375
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-523 1.37e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  265 EQSQMKERLASLSSHVTELEEdldtarkdlikseemntkLQRDVREAMAQKEDMEeRITTLEKRYLAAQREATSVHDLND 344
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLER------------------AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRA 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  345 KLENEIAnkdsmhrqtEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNieERLRQMEAQLE 424
Cdd:COG4913   280 ALRLWFA---------QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIE 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  425 EKNQELQRARQREKmneehnkRLSDTVDKL---LSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQlv 501
Cdd:COG4913   349 RLERELEERERRRA-------RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR-- 419

                         250       260
                  ....*....|....*....|..
gi 767968918  502 lNIEALRAELDHMRLRGASLHH 523
Cdd:COG4913   420 -ELRELEAEIASLERRKSNIPA 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
246-521 1.41e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.31  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMntklqrdvreamaqkedmEERITTL 325
Cdd:PRK03918  182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------------------KEEIEEL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  326 EKRylaaqreatsvhdlNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAAL 402
Cdd:PRK03918  244 EKE--------------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDEL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  403 SKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdklLSESNERLQ--LHLKERMAALEDKNSLL 480
Cdd:PRK03918  310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----LEERHELYEeaKAKKEELERLKKRLTGL 384

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767968918  481 rEVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 521
Cdd:PRK03918  385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 250-436 1.51e-08

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: 58.24  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  330 lAAQREATSVHDLNDKLENEIANKD------------SMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQ 397
Cdd:COG4942   107 -AELLRALYRLGRQPPLALLLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767968918  398 RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR 436
Cdd:COG4942   186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
PRK12704 PRK12704
phosphodiesterase; Provisional
 361-505 3.23e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 57.87  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  361 EDKNRQLQERLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMN 440
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRN--EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767968918  441 EEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEsakkqlEETQHDKDQLVLNIE 505
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQEL-----ERISGLtaeEAKEILLEKVE------EEARHEAAVLIKEIE 179
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 156-464 3.99e-08

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: 57.83  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   156 SEVEVLKALKSLFEHHKALDEKVRERL--RVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPST 233
Cdd:pfam17380  266 TENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   234 SGK---------RSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLaslsshvtelEEDLDTARKDLIKSEEMNTKL 304
Cdd:pfam17380  346 RERelerirqeeRKRELERIRQEEIAMEISRMRELERLQMERQQKNERV----------RQELEAARKVKILEEERQRKI 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   305 QRDVREAM--------AQKEDM----EERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE 372
Cdd:pfam17380  416 QQQKVEMEqiraeqeeARQREVrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   373 LAEQKLQQtlRKAETLPE------VEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKR 446
Cdd:pfam17380  496 ILEKELEE--RKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMER 573

                          330
                   ....*....|....*...
gi 767968918   447 LSDTVDKLLSESNERLQL 464
Cdd:pfam17380  574 EREMMRQIVESEKARAEY 591
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-535 4.06e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 4.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   32 ADSHFEQLMVSMLEER-DRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-------LPQEFAALTKELNVCREQ 103
Cdd:COG4913   281 LRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqLEREIERLERELEERERR 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  104 LLEREEEIA-----------ELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSP--AGVSSEVEVLKALKSLFEH 170
Cdd:COG4913   361 RARLEALLAalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelRELEAEIASLERRKSNIPA 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  171 HkalDEKVRERLRvalERCSLLEEEL---GathkELMILKEQ------------NNQKKTL------------------T 217
Cdd:COG4913   441 R---LLALRDALA---EALGLDEAELpfvG----ELIEVRPEeerwrgaiervlGGFALTLlvppehyaaalrwvnrlhL 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  218 DGVLDINHEQENTPSTSGKRSSDGSLSHEedlakvielqeIISKQSREQSQMKERLASLSSHVT-ELEEDLDTARKD--- 293
Cdd:COG4913   511 RGRLVYERVRTGLPDPERPRLDPDSLAGK-----------LDFKPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAitr 579

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  294 --LIKSE----EMNTklQRDVRE-------AMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLEN--EIANKDSMHR 358
Cdd:COG4913   580 agQVKGNgtrhEKDD--RRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYS 657

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  359 QTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRek 438
Cdd:COG4913   658 WDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR-- 735

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  439 mneehnkrlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAEldHMRLRG 518
Cdd:COG4913   736 ------------LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWP 801

                         570
                  ....*....|....*..
gi 767968918  519 ASLHHGRPHLGSVPDFR 535
Cdd:COG4913   802 AETADLDADLESLPEYL 818
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 250-525 4.08e-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: 57.00  E-value: 4.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:pfam19220   48 SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERH 409
Cdd:pfam19220  128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDAT 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   410 gniEERLRQMEAQLEEKNQELQRA-RQREKMNEEHNKRLSdTVDKLLSESNERL----QLhLKERMAALEDKNSLLREVE 484
Cdd:pfam19220  208 ---RARLRALEGQLAAEQAERERAeAQLEEAVEAHRAERA-SLRMKLEALTARAaateQL-LAEARNQLRDRDEAIRAAE 282

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 767968918   485 SAkkqLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 525
Cdd:pfam19220  283 RR---LKEASIERDTLERRLAGLEADLERRTQQFQEMQRAR 320
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 175-512 7.70e-08

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: 57.05  E-value: 7.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   175 DEKVRERLRVALERcSLLEEELGATHKELMiLKEQNNQKKTLTDGVLdiNHE---QENTPSTSGKRSSDGSLSHEEDLAK 251
Cdd:pfam15921  136 ESQSQEDLRNQLQN-TVHELEAAKCLKEDM-LEDSNTQIEQLRKMML--SHEgvlQEIRSILVDFEEASGKKIYEHDSMS 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   252 VIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEerITTLEKRYLA 331
Cdd:pfam15921  212 TMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE--ITGLTEKASS 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   332 AQREATSVHDLNDKLENEIANKDSMHRqtedknRQLQErLELAEQKLQQTLRKAETLpeveaelaqrvaalskaeerhgn 411
Cdd:pfam15921  290 ARSQANSIQSQLEIIQEQARNQNSMYM------RQLSD-LESTVSQLRSELREAKRM----------------------- 339

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   412 IEERLRQMEAQLEEKNQELQRAR-------------------------QREK---MNEEHNKRLSD-------TVDKLLS 456
Cdd:pfam15921  340 YEDKIEELEKQLVLANSELTEARterdqfsqesgnlddqlqklladlhKREKelsLEKEQNKRLWDrdtgnsiTIDHLRR 419

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968918   457 ESNER-----------------LQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam15921  420 ELDDRnmevqrleallkamkseCQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 250-514 1.20e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 56.34  E-value: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   250 AKVIELQEIISKQSR-EQSQMKERLASLSSHVTELEEDLDTARK---DLIKS----EEMNTKLQRDVREAMAQKEDMEER 321
Cdd:pfam01576  327 QEVTELKKALEEETRsHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAkqalESENAELQAELRTLQQAKQDSEHK 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   322 -------ITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQ--QTLRKAETLPEVe 392
Cdd:pfam01576  407 rkklegqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtQELLQEETRQKL- 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   393 aelaqrvaalskaeerhgNIEERLRQMEaqlEEKNQELQRARQREKMNEEHNKRLSdTVDKLLSESNERLQLHLKERMAA 472
Cdd:pfam01576  486 ------------------NLSTRLRQLE---DERNSLQEQLEEEEEAKRNVERQLS-TLQAQLSDMKKKLEEDAGTLEAL 543

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 767968918   473 LEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM 514
Cdd:pfam01576  544 EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDL 585
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-469 1.42e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTA-LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:COG4717    87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRELEEELE 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  123 LLLEHLECLVSRHERSLRmtvvkrqaqspagvSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717   167 ELEAELAELQEELEELLE--------------QLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEELEQL 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  200 HKELMILKEQNNQKKT-----LTDGVLDINHEQENTPSTSGKRSSDGSLsheedLAKVIELQEIISKQSREQSQMKERLA 274
Cdd:COG4717   233 ENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFL-----VLGLLALLFLLLAREKASLGKEAEEL 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  275 SLSSHVTELE-EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANK 353
Cdd:COG4717   308 QALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  354 DSMHRQTEDKnRQLQERLELAEQKLQQ------TLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--E 425
Cdd:COG4717   388 RAALEQAEEY-QELKEELEELEEQLEEllgeleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlE 466

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 767968918  426 KNQELQRARQREKMNEEHNKRLSD--TVDKLLSESNERLQLHLKER 469
Cdd:COG4717   467 EDGELAELLQELEELKAELRELAEewAALKLALELLEEAREEYREE 512
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 146-476 1.49e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.23  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   146 RQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL-MILKEQNNQKKTLTDGVLDIN 224
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   225 H-EQENTPSTSGKRSSDGSLSH-EEDLAKVIE---------LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKD 293
Cdd:TIGR02169  748 SlEQEIENVKSELKELEARIEElEEDLHKLEEalndlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   294 LIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREA----TSVHDLNDKLEN---EIANKDSMHRQTEDKNRQ 366
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleAALRDLESRLGDlkkERDELEAQLRELERKIEE 907

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   367 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAA----------LSKAEERHGNIEERLRQMEAQLEEKNQELqrarqr 436
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEY------ 981

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 767968918   437 ekmnEEHNKRLSDTVDKLLSESNERLQlhLKERMAALEDK 476
Cdd:TIGR02169  982 ----EEVLKRLDELKEKRAKLEEERKA--ILERIEEYEKK 1015
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-496 1.59e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   55 RETQETLALTQGKLHevGHERDSLQRQLNTALpQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLeclvsr 134
Cdd:COG1196   216 RELKEELKELEAELL--LLKLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEA------ 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  135 heRSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKK 214
Cdd:COG1196   287 --QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  215 TLTDGVLDINHEQEntpstsgKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDL 294
Cdd:COG1196   365 EALLEAEAELAEAE-------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  295 IKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELA 374
Cdd:COG1196   438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  375 EQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKN------QELQRARQREKMNEEHNKRLS 448
Cdd:COG1196   518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAALAAALARGAI 597

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 767968918  449 DTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHD 496
Cdd:COG1196   598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 68-655 1.71e-07

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: 55.89  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    68 LHEVGHERDSLQRQLNTA-----------------LPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLEC 130
Cdd:pfam15921   80 LEEYSHQVKDLQRRLNESnelhekqkfylrqsvidLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   131 LVSR--HERSLRMTVVKRQAQSPAGVSSEVEVL------KALKSLFEHH-------KALDEKVRERLRVALERCSLLEEE 195
Cdd:pfam15921  160 LKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSIlvdfeeASGKKIYEHDsmstmhfRSLGSAISKILRELDTEISYLKGR 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   196 LGATHKELMILKEQNNQKKTL-----TDGV--LDINHEQENTPST---SGKRSSDGSLSHEedlakvielQEIISKQSRE 265
Cdd:pfam15921  240 IFPVEDQLEALKSESQNKIELllqqhQDRIeqLISEHEVEITGLTekaSSARSQANSIQSQ---------LEIIQEQARN 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   266 QSQMKER-LASLSSHVTELEEDLDTARKD-------------LIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKRY 329
Cdd:pfam15921  311 QNSMYMRqLSDLESTVSQLRSELREAKRMyedkieelekqlvLANSELTEARTERDqfSQESGNLDDQLQKLLADLHKRE 390

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   330 LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ-----------------ERLELAEQKLQQTLRKA------- 385
Cdd:pfam15921  391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQrleallkamksecqgqmERQMAAIQGKNESLEKVssltaql 470

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   386 ----ETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE- 460
Cdd:pfam15921  471 estkEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEc 550

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   461 ---RLQLHLKERM-----------------------AALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHM 514
Cdd:pfam15921  551 ealKLQMAEKDKVieilrqqienmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   515 RLRGASL-HHGRPHLGSVPDF---RFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQ-TLNEQDWERAQQASVLAN 589
Cdd:pfam15921  631 ELEKVKLvNAGSERLRAVKDIkqeRDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQ 710

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918   590 VAQAFESdADVSDGEDDRDTLLSSVDLLSPSGQADA-HTLAMMLQEQLDAINKEIRLIQEEKENTEQ 655
Cdd:pfam15921  711 TRNTLKS-MEGSDGHAMKVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-515 2.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  125 LEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELM 204
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  205 ILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSRE--QSQMKERLASLSSHVTE 282
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLllLLEAEADYEGFLEGVKA 512

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  283 LEEDLDTARKDLIKSEEMNTK--------------LQRDVREAMAQ--------KEDMEERITTLEKRyLAAQREATSVH 340
Cdd:COG1196   513 ALLLAGLRGLAGAVAVLIGVEaayeaaleaalaaaLQNIVVEDDEVaaaaieylKAAKAGRATFLPLD-KIRARAALAAA 591

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  341 DLNDKLENEIANKDSMHRQTEDKNRQLQERL-------ELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIE 413
Cdd:COG1196   592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  414 ERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEET 493
Cdd:COG1196   672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751

                         490       500
                  ....*....|....*....|..
gi 767968918  494 QHDKDQLVLNIEALRAELDHMR 515
Cdd:COG1196   752 ALEELPEPPDLEELERELERLE 773
PRK11281 PRK11281
mechanosensitive channel MscK;
315-521 2.27e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 55.30  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  315 KEDMEERITTLEKRYLAAQREATSVHDLNDKLEnEIANKDsmhrQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEA- 393
Cdd:PRK11281   38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLA-LLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDe 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  394 ELAQRVAALSkaeerhgnieerLRQMEAQLEEKNQELQRARqrekmneehnKRLSDTVDKLLSESN--ERLQLHLKERMA 471
Cdd:PRK11281  113 ETRETLSTLS------------LRQLESRLAQTLDQLQNAQ----------NDLAEYNSQLVSLQTqpERAQAALYANSQ 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767968918  472 ALEDKNSLLREVESAKKQLEETQhdKDQLVLNIEALRAELDHMR--LRGASL 521
Cdd:PRK11281  171 RLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALLNAQNDLQRksLEGNTQ 220
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1088-1158 2.31e-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: 49.22  E-value: 2.31e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918   1088 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDfsalaLLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEE-----DLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 1010-1065 5.20e-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: 5.20e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918   1010 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLR 1065
Cdd:smart00454   11 DWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 885-951 5.46e-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: 5.46e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918    885 FAQWDGPTVVVWLELWvGMPAwYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEI 951
Cdd:smart00454    1 VSQWSPESVADWLESI-GLEQ-YADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKL 65
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
304-662 6.85e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  304 LQRDVREAMAQKEDMEERIttlekrylaaqrEATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLR 383
Cdd:PRK02224  181 VLSDQRGSLDQLKAQIEEK------------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  384 KAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKL--------- 454
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedrdeelrd 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  455 -LSESNERLQLH------LKERMAALEDKNSLLRE--------VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRga 519
Cdd:PRK02224  329 rLEECRVAAQAHneeaesLREDADDLEERAEELREeaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-- 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  520 slhhgrphLGSVPDFRFPMADGHTDSYSTSAVLRrpqkGRLAALRDEPSKVQTLNE--------QDWERAQQASVLANVA 591
Cdd:PRK02224  407 --------LGNAEDFLEELREERDELREREAELE----ATLRTARERVEEAEALLEagkcpecgQPVEGSPHVETIEEDR 474

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  592 QAFES-DADVSDGEDDRDTLLSSVDLLSPSGQADAHtlAMMLQEQLDAINKeirLIQEEKENTEQRAEEIES 662
Cdd:PRK02224  475 ERVEElEAELEDLEEEVEEVEERLERAEDLVEAEDR--IERLEERREDLEE---LIAERRETIEEKRERAEE 541
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
45-492 8.62e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   45 EERDRLLDTLRETQETlaltQGKLHEVGHERDSLQRQLNT--ALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTR 122
Cdd:PRK03918  197 EKEKELEEVLREINEI----SSELPELREELEKLEKEVKEleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  123 LLLEHLECLVSRHE--RSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRErLRVALERCSLLEEELGATH 200
Cdd:PRK03918  273 KEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELE 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  201 KELMILKEqnnqKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKV-IELQEIISKQSREQSQMKERLASLSSH 279
Cdd:PRK03918  352 KRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKELKKA 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  280 VTELE-----------EDLDTARKDLIKS--EEMNtKLQRDVREAMAQKEDMEERITTLEKrYLAAQREATSVHDLNDKL 346
Cdd:PRK03918  428 IEELKkakgkcpvcgrELTEEHRKELLEEytAELK-RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQL 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  347 EN-----EIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQM-- 419
Cdd:PRK03918  506 KEleeklKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgf 584

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918  420 --EAQLEEKNQELqrarqrEKMNEEHNkRLSDTVDKL--LSESNERLQLHLKERMAALEDKNSllrEVESAKKQLEE 492
Cdd:PRK03918  585 esVEELEERLKEL------EPFYNEYL-ELKDAEKELerEEKELKKLEEELDKAFEELAETEK---RLEELRKELEE 651
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 354-515 1.27e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.14  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  354 DSMHRQTEDKNRQLQERLELAEQKLQQTLRKAEtlpEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQEL-QR 432
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  433 ARQREKmneehNKRLSDTVDKLL-SESNERL--QLHLKERMAalEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRA 509
Cdd:COG3883    92 ARALYR-----SGGSVSYLDVLLgSESFSDFldRLSALSKIA--DADADLLEELKADKAELEAKKAELEAKLAELEALKA 164


                  ....*.
gi 767968918  510 ELDHMR 515
Cdd:COG3883   165 ELEAAK 170
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
282-474 1.47e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  282 ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTE 361
Cdd:COG4717    50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  362 D--KNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLR-QMEAQLEEKNQELQRARQREK 438
Cdd:COG4717   130 LyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLA 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767968918  439 MNEEHNKRLSDTVDKLLSE----SNERLQLHLKERMAALE 474
Cdd:COG4717   210 ELEEELEEAQEELEELEEEleqlENELEAAALEERLKEAR 249
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-453 1.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   37 EQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELnvcreqllEREEEIAELKA 116
Cdd:COG1196   413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--------LLEAALAELLE 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  117 ERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKslfehhKALDEKVRERLRVALERCSLLEEEL 196
Cdd:COG1196   485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE------AAYEAALEAALAAALQNIVVEDDEV 558

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  197 GATHKELmiLKEQNNQKKTLtDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASL 276
Cdd:COG1196   559 AAAAIEY--LKAAKAGRATF-LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  277 SSHVTELEEDLDTARKDL-----------IKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDK 345
Cdd:COG1196   636 LRRAVTLAGRLREVTLEGeggsaggsltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  346 LENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNI-----------EE 414
Cdd:COG1196   716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVnllaieeyeelEE 795

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 767968918  415 RLRQMEAQLEeknqELQRARQR-----EKMNEEHNKRLSDTVDK 453
Cdd:COG1196   796 RYDFLSEQRE----DLEEARETleeaiEEIDRETRERFLETFDA 835
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
154-492 1.77e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  154 VSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMI------LKEQNNQKKTLTDGVLDINHEQ 227
Cdd:PRK03918  403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLeeytaeLKRIEKELKEIEEKERKLRKEL 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  228 ENTPSTSGKRSSdgsLSHEEDLAKVI-ELQEIISKQSREQSQMKERLA-SLSSHVTELEEDLDTARKDLIKSEEMNTKLq 305
Cdd:PRK03918  483 RELEKVLKKESE---LIKLKELAEQLkELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKL- 558

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  306 rdvREAMAQKEDMEERITTLEKRYLaaQREATSVHDLNDKLEN--EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLR 383
Cdd:PRK03918  559 ---AELEKKLDELEEELAELLKELE--ELGFESVEELEERLKElePFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  384 K-AETLPEVEaELAQRVAALSK--AEERHGNIEERLRqmeaqleEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesne 460
Cdd:PRK03918  634 ElAETEKRLE-ELRKELEELEKkySEEEYEELREEYL-------ELSRELAGLRAELEELEKRREEIKKTLEKL------ 699

                         330       340       350
                  ....*....|....*....|....*....|..
gi 767968918  461 rlqlhlKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:PRK03918  700 ------KEELEEREKAKKELEKLEKALERVEE 725
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 1010-1061 2.13e-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: 46.08  E-value: 2.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767968918 1010 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRgQLKMVDSFHRNSFQCGI 1061
Cdd:cd09487     4 EWLESLGLEQYADLFRKNEIDGDALLLLTDEDLK-ELGITSPGHRKKILRAI 54
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 36-439 2.61e-06

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: 51.22  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    36 FEQLMVSMLEERDRL--LDTLRE---------TQETLALTQGKLHEVGHERD-SLQRQLNTALPQEFAALTKELNVCREQ 103
Cdd:pfam19220    5 NELLRVRLGEMADRLedLRSLKAdfsqliepiEAILRELPQAKSRLLELEALlAQERAAYGKLRRELAGLTRRLSAAEGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   104 LLEREEEIAELKAERNNTRLLLEHLECLVSrhERSLRMTVVKRQAqspagvSSEVEVLKALKslfEHHKALdekvRERLR 183
Cdd:pfam19220   85 LEELVARLAKLEAALREAEAAKEELRIELR--DKTAQAEALERQL------AAETEQNRALE---EENKAL----REEAQ 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   184 VALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQ-EIISKQ 262
Cdd:pfam19220  150 AAEKALQRAEGELATARERLALLEQENRRLQALSE-------EQAAELAELTRRLAELETQLDATRARLRALEgQLAAEQ 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   263 SREQSQMKERLASLSSHVTE---LEEDLDTARKDLIKSEEMNTklqrdvrEAMAQKEDMEERITTLEKRYLAAQREATSV 339
Cdd:pfam19220  223 AERERAEAQLEEAVEAHRAErasLRMKLEALTARAAATEQLLA-------EARNQLRDRDEAIRAAERRLKEASIERDTL 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   340 HDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTLRKAetlpeveaeLAQRVAALSKAEERHGNIEERLRQM 419
Cdd:pfam19220  296 ERRLAGLEADLERRTQQFQEMQRARAELEERAE--------MLTKA---------LAAKDAALERAEERIASLSDRIAEL 358

                          410       420
                   ....*....|....*....|....*..
gi 767968918   420 E-------AQLEEKNQELQRARQREKM 439
Cdd:pfam19220  359 TkrfeverAALEQANRRLKEELQRERA 385
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 192-512 3.44e-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: 51.56  E-value: 3.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   192 LEEELGATHKELMILKEQNNQKKtltdgvldinheQENTPSTSGKRSSDGSLSHEEDLAKviELQEIISKQSREQSQMKE 271
Cdd:TIGR04523  361 KQRELEEKQNEIEKLKKENQSYK------------QEIKNLESQINDLESKIQNQEKLNQ--QKDEQIKKLQQEKELLEK 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   272 RLASLSSHVTELEEDLdtarKDLiksEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREAtsvhdlnDKLENEIA 351
Cdd:TIGR04523  427 EIERLKETIIKNNSEI----KDL---TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL-------EQKQKELK 492

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   352 NKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERHGNIEERLR--QMEAQLEEKNQE 429
Cdd:TIGR04523  493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL---ESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKE 569

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   430 LQRARQREKMNEEHNKRLSDTVDKLLSESNE-RLQLHLKERMAA-LED----------------------KNSLLREVES 485
Cdd:TIGR04523  570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDlIKEIEEKEKKISsLEKelekakkeneklssiiknikskKNKLKQEVKQ 649

                          330       340
                   ....*....|....*....|....*..
gi 767968918   486 AKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:TIGR04523  650 IKETIKEIRNKWPEIIKKIKESKTKID 676
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 254-384 3.64e-06

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 49.13  E-value: 3.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   254 ELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREA-MAQKEDMEERITTLEKRYLAA 332
Cdd:pfam15619   57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDK 136

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767968918   333 QREatsVHDLNDKLEN-------EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK 384
Cdd:pfam15619  137 DEK---IQDLERKLELenksfrrQLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKERE 192
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-511 4.95e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTaLPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  124 LLEHLECLVSRH--------ERSLRMTVVKRQAQSPAGVsSEVEVLKALKSLFEHHKALDEkVRERLRVALERCSLLEEE 195
Cdd:PRK02224  329 RLEECRVAAQAHneeaeslrEDADDLEERAEELREEAAE-LESELEEAREAVEDRREEIEE-LEEEIEELRERFGDAPVD 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  196 LGATHKEL-MILKEQNNQKKTLTDGVLDINHEQENTPST-----SGKRSSDGSLSHEEDLAKVIElqeiiskQSREQ-SQ 268
Cdd:PRK02224  407 LGNAEDFLeELREERDELREREAELEATLRTARERVEEAealleAGKCPECGQPVEGSPHVETIE-------EDRERvEE 479

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  269 MKERLASLSSHVTELEEDLDTArKDLIKSE-EMNTKLQR--DVREAMAQK----EDMEERITTLEKR------------- 328
Cdd:PRK02224  480 LEAELEDLEEEVEEVEERLERA-EDLVEAEdRIERLEERreDLEELIAERretiEEKRERAEELRERaaeleaeaeekre 558

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  329 -----YLAAQREATSVHDLNDKLEneiANKDSmhRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 403
Cdd:PRK02224  559 aaaeaEEEAEEAREEVAELNSKLA---ELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  404 kaeERHGNIEERLRqmEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSE----SNERLQLH-LKERMAALEDKNS 478
Cdd:PRK02224  634 ---ERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELEeLRERREALENRVE 708

                         490       500       510
                  ....*....|....*....|....*....|...
gi 767968918  479 LLREVESAKKQLEETQHDkdqlvlnieaLRAEL 511
Cdd:PRK02224  709 ALEALYDEAEELESMYGD----------LRAEL 731
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 303-475 5.60e-06

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: 49.15  E-value: 5.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  303 KLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLElaeqklqqTL 382
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--------NV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  383 RKAETLPEVEAELAQrvaalskAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERL 462
Cdd:COG1579    86 RNNKEYEALQKEIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                         170
                  ....*....|...
gi 767968918  463 QLHLKERMAALED 475
Cdd:COG1579   159 EELEAEREELAAK 171
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 244-512 7.52e-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: 50.56  E-value: 7.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   244 SHEEDLakvIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERIT 323
Cdd:pfam01576  135 KLEEDI---LLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   324 TLEkrylaaqREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAET-LPEVEAELAQRV 399
Cdd:pfam01576  212 KLE-------GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetAQKNNALKKIRELEAqISELQEDLESER 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   400 AALSKAEERHGNIEERLRQMEAQLEEK------NQELQRARQRE--------------------KMNEEHNKRLSDTVDK 453
Cdd:pfam01576  285 AARNKAEKQRRDLGEELEALKTELEDTldttaaQQELRSKREQEvtelkkaleeetrsheaqlqEMRQKHTQALEELTEQ 364

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   454 LlsESNERLQLHLKERMAALEDKNSLLR-EVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam01576  365 L--EQAKRNKANLEKAKQALESENAELQaELRTLQQAKQDSEHKRKKLEGQLQELQARLS 422
PRK01156 PRK01156
chromosome segregation protein; Provisional
 175-486 7.79e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 50.29  E-value: 7.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  175 DEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIE 254
Cdd:PRK01156  464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE---YLESEEINKSINEYNKIESARADLEDIKIKINE 540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  255 LQEIISKQSreqsQMKERLASLSShvteleEDLDTARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTLEKRylaAQR 334
Cdd:PRK01156  541 LKDKHDKYE----EIKNRYKSLKL------EDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESR---LQE 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErLELAEQKLQQTLrkaETLPEVEAELAQRVAALSKAEERHGNIEE 414
Cdd:PRK01156  606 IEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKI---DNYKKQIAEIDSIIPDLKEITSRINDIED 681

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  415 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVdkllSESNERLqlhlkERMAALEDKNSLLREVESA 486
Cdd:PRK01156  682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETL-----ESMKKIKKAIGDLKRLREA 744
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
254-457 7.79e-06

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 50.07  E-value: 7.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  254 ELQEIISKQSREQSQMKERLASLSSHVTELE---------EDLDTARKDLIKSEemntKLQRDVREAMAQKEDMEERITT 324
Cdd:COG0497   169 ALKKELEELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAE----KLREALQEALEALSGGEGGALD 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  325 LekryLA-AQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQ----------ERLELAEQKLQ---QTLRK----AE 386
Cdd:COG0497   245 L----LGqALRALERLAEYDPSLAELAERLESALIELEEAASELRryldslefdpERLEEVEERLAllrRLARKygvtVE 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  387 TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQrekmneEHNKRLSDTVDKLLSE 457
Cdd:COG0497   321 ELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARK------KAAKKLEKAVTAELAD 385
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-335 1.23e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    44 LEERDRLLDTLRETQETLALTQGKLHE-----VGHERDSLQRQLnTALPQEFAALTKELNVCREQLLEREEEIAELKAER 118
Cdd:TIGR02169  210 AERYQALLKEKREYEGYELLKEKEALErqkeaIERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   119 NNT-RLLLEHLECLVSRHERSLRmtVVKRQAQSPAGVSSEVEV--------LKALKSLFEHHKALDEKVRERLRVALERC 189
Cdd:TIGR02169  289 QLRvKEKIGELEAEIASLERSIA--EKERELEDAEERLAKLEAeidkllaeIEELEREIEEERKRRDKLTEEYAELKEEL 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   190 SLLEEELGATHKELMILKEQNNQKKTLTDgvlDINHEQEntpstsgkrssdgSLSHEEDlakviELQEIISKQSREQSQM 269
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLE---KLKREIN-------------ELKRELD-----RLQEELQRLSEELADL 425

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918   270 KERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQRE 335
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-513 1.29e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   47 RDRLLDTLRETQETLALTQGKLHEVG-HERDSLQRQLNTA--LPQEFAALTKELNvcreqllEREEEIAELKAERNNTRL 123
Cdd:COG4717    44 RAMLLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeeKEEEYAELQEELE-------ELEEELEELEAELEELRE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  124 LLEHLECLVSRHERSLRMTVVKRQ-AQSPAGVSSEVEVLKALKSLFEHHKALDEKV---RERLRVALERCSLLEEELGAT 199
Cdd:COG4717   117 ELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEELEELEAELaelQEELEELLEQLSLATEEELQD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  200 HKE-----LMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLA 274
Cdd:COG4717   197 LAEeleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  275 SLSSHVTELeedLDTARKDLIKSEEMNTKLQRDVREAMAQKE-DMEERITTLEKRYLAAQREATSVHDLNDKleneIANK 353
Cdd:COG4717   277 GVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDR----IEEL 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  354 DSMHRQTEDKNRQLQerLELAEQKLQQTLRKAETlpEVEAELAQRVAALSKAEErhgnIEERLRQMEAQLEEKNQELQRA 433
Cdd:COG4717   350 QELLREAEELEEELQ--LEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQE----LKEELEELEEQLEELLGELEEL 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  434 RQREKmNEEHNKRLSDTVDKLLSESNERLQLH-----LKERMAALEDKNSL---LREVESAKKQLEETQHDKDQLVLNIE 505
Cdd:COG4717   422 LEALD-EEELEEELEELEEELEELEEELEELReelaeLEAELEQLEEDGELaelLQELEELKAELRELAEEWAALKLALE 500


                  ....*...
gi 767968918  506 ALRAELDH 513
Cdd:COG4717   501 LLEEAREE 508
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 207-499 1.48e-05

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: 48.65  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   207 KEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHE-----EDLAKVIELQEIISKQSREQSQMKERLASLSSHVT 281
Cdd:pfam15905   25 KSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKsqknlKESKDQKELEKEIRALVQERGEQDKRLQALEEELE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   282 ELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEE-----------RITTLEKRYLAAQREAT--SVHDLNDKLEN 348
Cdd:pfam15905  105 KVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAkfsedgtqkkmSSLSMELMKLRNKLEAKmkEVMAKQEGMEG 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   349 EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTlrKAETLpeveaELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 428
Cdd:pfam15905  185 KLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE--KSETE-----KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKND 257

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918   429 ELQRARQREKMNEEHNKRLSDTVD---KLLSESNERLQLHLKERmaaledKNSLLREVESAKKQL--EETQHDKDQ 499
Cdd:pfam15905  258 EIESLKQSLEEKEQELSKQIKDLNekcKLLESEKEELLREYEEK------EQTLNAELEELKEKLtlEEQEHQKLQ 327
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
255-515 1.57e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  255 LQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQR 334
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  335 EATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEE 414
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  415 RLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 494
Cdd:COG4372   189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268

                         250       260
                  ....*....|....*....|.
gi 767968918  495 HDKDQLVLNIEALRAELDHMR 515
Cdd:COG4372   269 VEKDTEEEELEIAALELEALE 289
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 245-516 1.63e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 49.12  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   245 HEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITT 324
Cdd:pfam07888   96 HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   325 LEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQK---LQQTLRKAETLPEVEAELAQRVAA 401
Cdd:pfam07888  176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEG 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   402 L-----SKAEERHGNIEE----RLR--QMEAQLEEKN-----------QELQRARQREKMNEEHNKRLSDTVDKLlsesN 459
Cdd:pfam07888  256 LgeelsSMAAQRDRTQAElhqaRLQaaQLTLQLADASlalregrarwaQERETLQQSAEADKDRIEKLSAELQRL----E 331

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918   460 ERLQlhlKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRL 516
Cdd:pfam07888  332 ERLQ---EERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQA 385
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 38-496 1.70e-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: 49.45  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    38 QLMVSMLEERDR--LLDTLRETQETLALTQGKLHE--VGHERDSLQRQ-----LNTALPQEFAALTKELNvcreqlLERE 108
Cdd:pfam12128  231 QAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFgyKSDETLIASRQeerqeTSAELNQLLRTLDDQWK------EKRD 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   109 EEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKR---QAQSPAgVSSEVEVL-KALKSLFEHHKALDEKVRERLRV 184
Cdd:pfam12128  305 ELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaadQEQLPS-WQSELENLeERLKALTGKHQDVTAKYNRRRSK 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   185 ALERCSlleEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRS-SDGSLSHEEDL--AKVIELQEIISK 261
Cdd:pfam12128  384 IKEQNN---RDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEfNEEEYRLKSRLgeLKLRLNQATATP 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   262 QSREQ--------SQMKERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRylaaq 333
Cdd:pfam12128  461 ELLLQlenfderiERAREEQEAANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQ----- 532

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   334 reatsVHDLNDKLENEIAN-KDS---------MHR----------QTEDKNRQLQERLELAEQKLQQTLRKAETLpevEA 393
Cdd:pfam12128  533 -----AGTLLHFLRKEAPDwEQSigkvispelLHRtdldpevwdgSVGGELNLYGVKLDLKRIDVPEWAASEEEL---RE 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   394 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDtvdkllSESNERLQLHlKERMAAL 473
Cdd:pfam12128  605 RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD------EKQSEKDKKN-KALAERK 677

                          490       500
                   ....*....|....*....|...
gi 767968918   474 EDKNSLLREVESAKKQLEETQHD 496
Cdd:pfam12128  678 DSANERLNSLEAQLKQLDKKHQA 700
PTZ00121 PTZ00121
MAEBL; Provisional
 115-521 1.84e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  115 KAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKA--LKSLFEHHKALDEKVR-ERLRVALERCSL 191
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKaEEAKKADEAKKK 1323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  192 LEEelgaTHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELqeiisKQSREQSQMKE 271
Cdd:PTZ00121 1324 AEE----AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-----KKKAEEKKKAD 1394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  272 RLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQrDVREAMAQKEDMEERITTLEKRYLAaqREATSVHDLNDKLEnEIA 351
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE-EAK 1470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  352 NKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVE----AELAQRVAALSKAEERHGNIEERLRQMEAQLEE 425
Cdd:PTZ00121 1471 KADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADeakkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  426 --KNQELQRARQR----EKMNEEHNKRLSDTVDKLLSESNER-----LQLHLKERMAALED---------KNSLLREVES 485
Cdd:PTZ00121 1551 lkKAEELKKAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEArieevMKLYEEEKKMKAEEakkaeeakiKAEELKKAEE 1630

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 767968918  486 AKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 521
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
342-525 1.86e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  342 LNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQME- 420
Cdd:COG4717    47 LLERLEKE---ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEk 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  421 ---------------AQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVES 485
Cdd:COG4717   124 llqllplyqelealeAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767968918  486 AKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGR 525
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
RNase_Y_N pfam12072
RNase Y N-terminal region;
365-506 2.22e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 46.80  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   365 RQLQERLELAEQKLQQTLRKAETLP----------------EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ 428
Cdd:pfam12072   27 AKIGSAEELAKRIIEEAKKEAETKKkealleakeeihklraEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   429 ELQRARQREKMNEEHNKRLSDTVDKLLSESNERLqlhlkERMAAL---EDKNSLLREVEsakkqlEETQHDKDQLVLNIE 505
Cdd:pfam12072  107 SLEKKEKELEAQQQQLEEKEEELEELIEEQRQEL-----ERISGLtseEAKEILLDEVE------EELRHEAAVMIKEIE 175


                   .
gi 767968918   506 A 506
Cdd:pfam12072  176 E 176
PTZ00121 PTZ00121
MAEBL; Provisional
 246-500 2.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARK--DLIKSEEMNTKLQRDVREAMAQKEDMEERIT 323
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  324 TLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS 403
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  404 KAEERHGNIEERLRQMEA-----QLEEKNQELQRARQREKMNEEhnKRLSDTVDKLLSESN--ERLQLHLKERMAA--LE 474
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAkkkadEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKkaEEAKKKAEEAKKAdeAK 1476

                         250       260
                  ....*....|....*....|....*.
gi 767968918  475 DKNSLLREVESAKKQLEETQHDKDQL 500
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEA 1502
PTZ00121 PTZ00121
MAEBL; Provisional
 169-515 2.45e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  169 EHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDgvLDINHEQENTPSTSGKRSSDGSLSHEED 248
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEA 1423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  249 LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQ--RDVREAMAQKEDMEERITTLE 326
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAK 1503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  327 KRYlAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA---ELAQRVAALS 403
Cdd:PTZ00121 1504 KAA-EAKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEakkAEEDKNMALR 1581

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  404 KAEE----RHGNIEERLRQMEAQLEEKNQELQRARQ-----REKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALE 474
Cdd:PTZ00121 1582 KAEEakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 767968918  475 DKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 250-485 2.99e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   250 AKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY 329
Cdd:TIGR00606  843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   330 LAAQREATSVHDLNDKLENEIankdsmhRQTEDKNRQLQERLELAEQKLQQTlrKAETLPEVEAELAQRVAALSKAEERH 409
Cdd:TIGR00606  923 QEKEELISSKETSNKKAQDKV-------NDIKEKVKNIHGYMKDIENKIQDG--KDDYLKQKETELNTVNAQLEECEKHQ 993

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968918   410 GNIEERLRQMEAQLEEKNQE---LQRARQREKMNEEHnKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVES 485
Cdd:TIGR00606  994 EKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENEL-KEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
PTZ00121 PTZ00121
MAEBL; Provisional
 247-496 3.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  247 EDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLI----------KSEEMNTKLQRDVR-EAMAQK 315
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeekkmKAEEAKKAEEAKIKaEELKKA 1628

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  316 EDMEERITTLEKRYLAAQREATSVHDLNDklENEIANKDSMHRQTEDKNR--QLQERLELAEQKLQQTLRKAETLPEVEA 393
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  394 ELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKrlsdtVDKLLSESNERLQLHLKERMAAL 473
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVI 1781

                         250       260
                  ....*....|....*....|...
gi 767968918  474 EDKnsLLREVESAKKQLEETQHD 496
Cdd:PTZ00121 1782 EEE--LDEEDEKRRMEVDKKIKD 1802
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-474 3.33e-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: 48.58  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918    31 DADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQ---LNTALPQEFAAL---TKELNVCREQL 104
Cdd:pfam15921  321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLhkrEKELSLEKEQN 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   105 LE-------REEEIAELKAERNNTRLLLEHLECLVsRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEK 177
Cdd:pfam15921  401 KRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   178 VRERL---RVALER---------CSLLEEE--LGATHKELMILKE-------------------QNNQKK--------TL 216
Cdd:pfam15921  480 VVEELtakKMTLESsertvsdltASLQEKEraIEATNAEITKLRSrvdlklqelqhlknegdhlRNVQTEcealklqmAE 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   217 TDGVLDINHEQ-ENTPSTSGK--RSSDGSLSHEEDLAKVI-----ELQEIISKQSREQSQMKERLASLSS---------- 278
Cdd:pfam15921  560 KDKVIEILRQQiENMTQLVGQhgRTAGAMQVEKAQLEKEIndrrlELQEFKILKDKKDAKIRELEARVSDlelekvklvn 639

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   279 -------HVTELEEDLD-------TARKDLIKSEEMNTKLQRDVREamaQKEDMEERITTLEKRYLAAQREATSVHDLND 344
Cdd:pfam15921  640 agserlrAVKDIKQERDqllnevkTSRNELNSLSEDYEVLKRNFRN---KSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   345 KLE----NEIANKDSMHRQTEDKNRQ---LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLR 417
Cdd:pfam15921  717 SMEgsdgHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR 796

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918   418 QMEAQLEEKNQELQRARQREKMneehnkRLSDTVDKLLSESNERLQLHLKERMAALE 474
Cdd:pfam15921  797 SQERRLKEKVANMEVALDKASL------QFAECQDIIQRQEQESVRLKLQHTLDVKE 847
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
400-517 3.72e-05

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 46.36  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  400 AALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLlsesNERLQLHLK---ERMA--ALE 474
Cdd:COG1842    16 ALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW----EEKARLALEkgrEDLAreALE 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767968918  475 DKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 517
Cdd:COG1842    92 RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 251-437 4.98e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAmaqKEDMEERITTLEKRYL 330
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERAR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  331 AAQR------------EATSVHDLNDKLEN--------------------EIANKDSMHRQTEDKNRQLQERLELAEQKL 378
Cdd:COG3883    94 ALYRsggsvsyldvllGSESFSDFLDRLSAlskiadadadlleelkadkaELEAKKAELEAKLAELEALKAELEAAKAEL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968918  379 QQTLRKAE----TLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRE 437
Cdd:COG3883   174 EAQQAEQEallaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 177-512 5.45e-05

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.54  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTsgKRSSDGS--------LSH-EE 247
Cdd:pfam06160   83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLA--NRFSYGPaidelekqLAEiEE 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   248 DLAKVIEL---------QEIISKQSRE----QSQMK--------------ERLASLSSHVTELEED------------LD 288
Cdd:pfam06160  161 EFSQFEELtesgdyleaREVLEKLEEEtdalEELMEdipplyeelktelpDQLEELKEGYREMEEEgyalehlnvdkeIQ 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   289 TARKDLIKSEEMNTKLqrDVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIANKDSMHRQTEDKN 364
Cdd:pfam06160  241 QLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKK----YVEKNLPEIEDYLEHAEEQNKELKEEL 314

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--EKNQE-----LQRARQRE 437
Cdd:pfam06160  315 ERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEeiEEEQEefkesLQSLRKDE 394

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918   438 KmneEHNKRLsDTVDKLLSESNERLQlhlKERMAALEDknSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam06160  395 L---EAREKL-DEFKLELREIKRLVE---KSNLPGLPE--SYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLD 460
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1088-1158 6.52e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 41.87  E-value: 6.52e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  1088 VLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFsalalLLQIPTQNTQARAVLEREFNNLL 1158
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLED-----LKRLGITSVGHRRKILKKIQELK 66
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 321-517 6.70e-05

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 45.76  E-value: 6.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   321 RITTLEKRYLAAQREATSVHDLNDKLENeIANKDSmhrqTEDKNRQLQERLELAEQKLQQTLRKAETL------------ 388
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSL-LDKIDA----SKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeil 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   389 -----PEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTvDKLLSESnerLQ 463
Cdd:pfam12795   76 aslslEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPP-GEPLSEA---QR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918   464 LHLKERMAALEDKNSLLRE--------VESAKKQLEETQHDKDQLVLNIEALRAELDHMRLR 517
Cdd:pfam12795  152 WALQAELAALKAQIDMLEQellsnnnrQDLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQ 213
PRK01156 PRK01156
chromosome segregation protein; Provisional
 46-519 7.70e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.20  E-value: 7.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   46 ERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtalpqEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLL 125
Cdd:PRK01156  160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNL-----ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  126 EHLEC----LVSRHERSLRMTVVKRQAQSPagVSSEVEVLKALKSLFEHHKAL-----------------DEKVRERLRV 184
Cdd:PRK01156  235 NNLKSalneLSSLEDMKNRYESEIKTAESD--LSMELEKNNYYKELEERHMKIindpvyknrnyindyfkYKNDIENKKQ 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  185 ALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSdgSLSHEEDLAKVIELQEIisKQSR 264
Cdd:PRK01156  313 ILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS--YLKSIESLKKKIEEYSK--NIER 388

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  265 EQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKR--------YLAAQREA 336
Cdd:PRK01156  389 MSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgtTLGEEKSN 468

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  337 TSVHDLNDK---LENEIANKDSMHRQTEDKNRQLQERLE-LAEQKLQQTLRKAETLPEVEAELAQ---RVAALSKAEERH 409
Cdd:PRK01156  469 HIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINKSINEYNKIESARADLEDikiKINELKDKHDKY 548

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  410 GNIEERLRQMEAQ-LEEKNQELQRA-RQREKMNEEHNKRLSDTVDKLLSESNERLQlhlkERMAALEDKNS----LLREV 483
Cdd:PRK01156  549 EEIKNRYKSLKLEdLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLESRLQ----EIEIGFPDDKSyidkSIREI 624

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 767968918  484 ESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGA 519
Cdd:PRK01156  625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 34-511 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 767968918    34 SHFEQLMVSMleerDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTK-ELNVCREQLLEREEeia 112
Cdd:pfam05483  296 KELEDIKMSL----QRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfEATTCSLEELLRTE--- 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   113 ELKAERNNTRLLLEHLEcLVSRHERSLRMTVVKRqaqspagvSSEVEVLKALKSLFEHHKALDEKvrerlrvalERCSLL 192
Cdd:pfam05483  369 QQRLEKNEDQLKIITME-LQKKSSELEEMTKFKN--------NKEVELEELKKILAEDEKLLDEK---------KQFEKI 430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   193 EEELGATHKELMILKEQNNQKktltdgVLDInhEQENTPSTSgkrssdgslSHEEDLAKVIELQEIISKQSREQSQMKER 272
Cdd:pfam05483  431 AEELKGKEQELIFLLQAREKE------IHDL--EIQLTAIKT---------SEEHYLKEVEDLKTELEKEKLKNIELTAH 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   273 LASLSSHVTELEEDLDTARKDLIKSEEmntklqrDVREAMAQKEDMEERITTLEKRYLAAQREATSVHD----LNDKLEN 348
Cdd:pfam05483  494 CDKLLLENKELTQEASDMTLELKKHQE-------DIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqKGDEVKC 566

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   349 EIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSK---AEERHGNIEE-RLRQMEAQLE 424
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsAENKQLNAYEiKVNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   425 EKNQEL-------QRARQREKMNEEH-------NKRLSDTVDKLLSESNERLQLHLKERMAALEDK----NSLLREVESA 486
Cdd:pfam05483  647 SAKQKFeeiidnyQKEIEDKKISEEKlleevekAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHkhqyDKIIEERDSE 726

                          490       500
                   ....*....|....*....|....*....
gi 767968918   487 ----KKQLEETQHDKDQLVLNIEALRAEL 511
Cdd:pfam05483  727 lglyKNKEQEQSSAKAALEIELSNIKAEL 755
PTZ00121 PTZ00121
MAEBL; Provisional
 236-510 1.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  236 KRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTELEEDLDTARK--DLIKSEEMNTKLQRDVREAMA 313
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--AEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAE 1507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  314 QKEDMEERITTLEKRYLAAQREATSVHDLND-KLENEIANKDSMHRQTEDKNRQLQERLE---LAEQKLQQTLRKAETLP 389
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEKKKAEeakKAEEDKNMALRKAEEAK 1587

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  390 EVE------------AELAQRVAALSKAEERHGNIE-----ERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVD 452
Cdd:PTZ00121 1588 KAEearieevmklyeEEKKMKAEEAKKAEEAKIKAEelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767968918  453 KLLSESNERLQLHLKERMAALEDKNSLLREVESAKKqLEETQHDKDQLVLNIEALRAE 510
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKKAEELKKA 1724
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
346-517 1.29e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  346 LENEIANKDSMHRQTEDknrqLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEE 425
Cdd:PRK03918  174 IKRRIERLEKFIKRTEN----IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  426 KNQEL----QRARQREKMNEEHNKRLSDtvdklLSESNERLQlHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLV 501
Cdd:PRK03918  250 LEGSKrkleEKIRELEERIEELKKEIEE-----LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323

                         170
                  ....*....|....*.
gi 767968918  502 LNIEALRAELDHMRLR 517
Cdd:PRK03918  324 NGIEERIKELEEKEER 339
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 261-521 1.49e-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: 46.12  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   261 KQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQReatsvh 340
Cdd:TIGR00618  283 QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH------ 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   341 dLNDKLENEIANKDSMHRQTEDKN--RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS-------------KA 405
Cdd:TIGR00618  357 -IRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdlqgqlahakkqqEL 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   406 EERHGNIEERLRQMEAQLEE-KNQELQRARQR---EKMNEEHNKRLSDTVDKLLSESNERLQLH------LKERMAALED 475
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKlEKIHLQESAQSlkeREQQLQTKEQIHLQETRKKAVVLARLLELqeepcpLCGSCIHPNP 515

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 767968918   476 KNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASL 521
Cdd:TIGR00618  516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL 561
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 360-663 1.55e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  360 TEDKNRQLqERLEL-AEQKLQ-QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQ-ELQRARQR 436
Cdd:COG1196   195 LGELERQL-EPLERqAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAElEAELEELR 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  437 EKMNEEhnkrlsdtvDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRL 516
Cdd:COG1196   274 LELEEL---------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  517 RGASLhhgrphlgsvpdfrfpmadghTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQA--SVLANVAQAF 594
Cdd:COG1196   345 ELEEA---------------------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAlrAAAELAAQLE 403

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968918  595 ESDADVSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESR 663
Cdd:COG1196   404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
264-435 1.59e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  264 REQSQMKERLASLSSHVTELEEDLDTARKDLIK----------SEEMNTKLQR------DVREAMAQKEDMEERITTLEK 327
Cdd:COG3206   168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQQlselesQLAEARAELAEAEARLAALRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  328 R------YLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN---RQLQERLELAEQKLQQTLRKAETLPEVEAE-LAQ 397
Cdd:COG3206   248 QlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEaLQA 327

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767968918  398 RVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ 435
Cdd:COG3206   328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 176-430 1.60e-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: 45.97  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   176 EKVRERLRVALER-CSLLEEELGATHKELMILKEQ-NNQKKTLTDGVLDINHEQENTPS--------TSGKRSSDGSLSH 245
Cdd:pfam10174  449 ERIIERLKEQREReDRERLEELESLKKENKDLKEKvSALQPELTEKESSLIDLKEHASSlassglkkDSKLKSLEIAVEQ 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   246 EEDLAKVIELQEIISKQSREQSQMKErlaSLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTL 325
Cdd:pfam10174  529 KKEECSKLENQLKKAHNAEEAVRTNP---EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   326 EKRYLAAQREATsVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 405
Cdd:pfam10174  606 ESLTLRQMKEQN-KKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQS 684

                          250       260       270
                   ....*....|....*....|....*....|
gi 767968918   406 -EERHGNIE----ERLRQMEAQLEEKNQEL 430
Cdd:pfam10174  685 lAEKDGHLTnlraERRKQLEEILEMKQEAL 714
PTZ00121 PTZ00121
MAEBL; Provisional
 260-494 1.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  260 SKQSREQSQMKERLAslsshvTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKED---MEERITTLEKRYLAAQREA 336
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRA------DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDarkAEEARKAEDARKAEEARKA 1148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  337 TSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERLELAEQKLQQTLRKAETLPEVEA----------ELAQRVAALSKAE 406
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAarkaeeerkaEEARKAEDAKKAE 1227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  407 ERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESA 486
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307


                  ....*...
gi 767968918  487 KKQLEETQ 494
Cdd:PTZ00121 1308 KKKAEEAK 1315
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 244-429 1.71e-04

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   244 SHEEDLAKVIELQEIISKQ----SREQSQMKERLASLSSHVTELEEDLDTARKDliKSEEMNTKlqrdvreamaqkedme 319
Cdd:pfam13851   30 SLKEEIAELKKKEERNEKLmseiQQENKRLTEPLQKAQEEVEELRKQLENYEKD--KQSLKNLK---------------- 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   320 ERITTLEKRYLAAQREATSVHDLNDKLENEianKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK-AETLPEVEAELAQR 398
Cdd:pfam13851   92 ARLKVLEKELKDLKWEHEVLEQRFEKVERE---RDELYDKFEAAIQDVQQKTGLKNLLLEKKLQAlGETLEKKEAQLNEV 168

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767968918   399 VAALSKAEERHGNIEERLRQMeaqLEEKNQE 429
Cdd:pfam13851  169 LAAANLDPDALQAVTEKLEDV---LESKNQL 196
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-435 1.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   44 LEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRL 123
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  124 LLEHLECLVSRHERSLRmtvVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKEL 203
Cdd:COG4717   228 ELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  204 MILKEQNNQKKTltdgvldinhEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKErlASLSSHVTEL 283
Cdd:COG4717   305 EELQALPALEEL----------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  284 EEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSvhdlnDKLENEIANKDSMHRQTEDK 363
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELEEE 447

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  364 NRQLQERLELAEQKLQQtLRKAETLPEVEAELAQRVAALSKAEERHGnieeRLRQMEAQLEEKNQELQRARQ 435
Cdd:COG4717   448 LEELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYREERL 514
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
364-502 2.05e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.04  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  364 NRQLQERLELAEQKLQQtlrkaetlpeVEAELAqRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQ-------- 435
Cdd:COG1566    78 PTDLQAALAQAEAQLAA----------AEAQLA-RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlykkgavs 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918  436 REKMNEEHNKRlsDTVDKLLSESNERLQLhLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVL 502
Cdd:COG1566   147 QQELDEARAAL--DAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTI 210
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 245-460 2.10e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 45.69  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  245 HEEDLAKVIELQEI-----ISKQSREQSQMKERLASLSSHVTELEEDLDTARK-------DLIKSEEMNT-KLQRDVREA 311
Cdd:PRK05771   26 HELGVVHIEDLKEElsnerLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvsvksleELIKDVEEELeKIEKEIKEL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  312 MAQKEDMEERITTLEKRylaaQREATSVHDLNDKLENEIANKdSMHRQTEDKNRQLQERLELAEQKLQQTLRK------- 384
Cdd:PRK05771  106 EEEISELENEIKELEQE----IERLEPWGNFDLDLSLLLGFK-YVSVFVGTVPEDKLEELKLESDVENVEYIStdkgyvy 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  385 ------AETLPEVEAELAQrvAALSKAE-ERHGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNKRLSDTVDKLLS 456
Cdd:PRK05771  181 vvvvvlKELSDEVEEELKK--LGFERLElEEEGTPSELIREIKEELEEIEKERESLLEElKELAKKYLEELLALYEYLEI 258


                  ....
gi 767968918  457 ESNE 460
Cdd:PRK05771  259 ELER 262
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 177-512 2.15e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.60  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  177 KVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTsgKRSSDGS--------LSH-EE 247
Cdd:PRK04778  102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLA--NRFSFGPaldelekqLENlEE 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  248 DLAKVIEL---------QEIISKQSREQSQMKERLASLSSHVTELE-------EDLDTARKDLIKS-------------E 298
Cdd:PRK04778  180 EFSQFVELtesgdyveaREILDQLEEELAALEQIMEEIPELLKELQtelpdqlQELKAGYRELVEEgyhldhldiekeiQ 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  299 EMNTKLQR--------DVREAMAQKEDMEERITTL----EKRYLAAQreatSVHDLNDKLENEIANKDSMHRQTEDKNRQ 366
Cdd:PRK04778  260 DLKEQIDEnlalleelDLDEAEEKNEEIQERIDQLydilEREVKARK----YVEKNSDTLPDFLEHAKEQNKELKEEIDR 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  367 LQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE--EKNQE-----LQRARQREKm 439
Cdd:PRK04778  336 VKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQEklsemLQGLRKDEL- 414

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968918  440 neEHNKRLsDTVDKLLSESNERLQlhlKERMAALEDknSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:PRK04778  415 --EAREKL-ERYRNKLHEIKRYLE---KSNLPGLPE--DYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLE 479
SAM_STIM-1,2-like cd09504
SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like ...
 888-946 2.28e-04

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: 40.78  E-value: 2.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  888 WDGPTVVVWLELWVGMPAwYVAACRANVKSGAIMSALSDTE---IQREIGISNPLHRLKLRL 946
Cdd:cd09504     5 WTVEDTVEWLVNSVELPQ-YVEAFKENGVDGSALPRLAVNNpsfLTSVLGIKDPIHRQKLSL 65
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 380-512 2.29e-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: 44.15  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  380 QTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNE----EHNKRLSDTVDKLL 455
Cdd:COG1579     4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleieEVEARIKKYEEQLG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767968918  456 SESNER----LQL---HLKERMAALEDK-NSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:COG1579    84 NVRNNKeyeaLQKeieSLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELD 148
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
266-438 2.33e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  266 QSQMKERLASLSSHVTELEEDLDTARKDLIKSEE--MNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLN 343
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  344 DKLENEIA-NKDSMHRQTEDKN-RQLQERLELAEQKLQQTLRK-AETLPEVEAELAQRVAALSKAEERHGNIEERLRQME 420
Cdd:COG3206   243 AALRAQLGsGPDALPELLQSPViQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322

                         170
                  ....*....|....*...
gi 767968918  421 AQLEEKNQELQRARQREK 438
Cdd:COG3206   323 EALQAREASLQAQLAQLE 340
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 127-486 2.58e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   127 HLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMIL 206
Cdd:pfam02463  676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   207 KEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEdLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEED 286
Cdd:pfam02463  756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL-KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   287 LDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 366
Cdd:pfam02463  835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   367 LQERLELAEQKLQQTLRKAETLPEVEaeLAQRVAALSKAEERHGNIEERLRQMEAQLEEK-----NQELQRARQREKMNE 441
Cdd:pfam02463  915 KENEIEERIKEEAEILLKYEEEPEEL--LLEEADEKEKEENNKEEEEERNKRLLLAKEELgkvnlMAIEEFEEKEERYNK 992

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 767968918   442 EH--NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESA 486
Cdd:pfam02463  993 DEleKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFY 1039
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
251-422 2.81e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  251 KVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRD--VREAMAQKEDMEERITTLEKR 328
Cdd:COG3206   206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSAR 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  329 YLAAQREATSVHDLNDKLENEIAN-KDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEE 407
Cdd:COG3206   286 YTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365

                         170
                  ....*....|....*
gi 767968918  408 RHGNIEERLRQMEAQ 422
Cdd:COG3206   366 LYESLLQRLEEARLA 380
PRK12704 PRK12704
phosphodiesterase; Provisional
 365-510 2.89e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  365 RQLQERLELAEQKLQQTLRKAETlpevEAELAQRVAALSKAEERHgnieERLRQMEAQLEEKNQELQRARQREKMNEEHN 444
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIH----KLRNEFEKELRERRNELQKLEKRLLQKEENL 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918  445 KRLSDTVDKllseSNERLQLHLKERmaaledkNSLLREVESAKKQLEETQHDKDQLVLNIEALRAE 510
Cdd:PRK12704   99 DRKLELLEK----REEELEKKEKEL-------EQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
1010-1065 2.93e-04

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 40.33  E-value: 2.93e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918  1010 EWLPSLGLPQYRSYFMECLVD-ARMLDHLTKKDLrGQLKMVDSFHRNSFQCGIMCLR 1065
Cdd:pfam07647   11 DWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDL-KRLGITSVGHRRKILKKIQELK 66
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 343-447 3.00e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  343 NDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRV-----AALSKAEERHGNIEERLR 417
Cdd:PRK00409  515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELR 594

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767968918  418 QMEAQL--EEKNQELQRARQR-EKMNEEHNKRL 447
Cdd:PRK00409  595 QLQKGGyaSVKAHELIEARKRlNKANEKKEKKK 627
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 154-517 3.02e-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: 45.10  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   154 VSSEVEVLKALKSLFEHHKALD--EKVRERLRVALERCSLLEEELGATHKELMilkEQNNQKKTLTDGVldinheqENTP 231
Cdd:pfam05483   95 VSIEAELKQKENKLQENRKIIEaqRKAIQELQFENEKVSLKLEEEIQENKDLI---KENNATRHLCNLL-------KETC 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   232 STSGKRSSDGSLSHEEDLAKVIELQEIISKqsreqsqmkerlasLSSHVTELEEDLDTARKdlikseEMNTKLQRDVREA 311
Cdd:pfam05483  165 ARSAEKTKKYEYEREETRQVYMDLNNNIEK--------------MILAFEELRVQAENARL------EMHFKLKEDHEKI 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   312 MAQKEDMEERITTLEKRYLAAQREATsvhdlndKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpev 391
Cdd:pfam05483  225 QHLEEEYKKEINDKEKQVSLLLIQIT-------EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHL--- 294

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   392 EAELAQRVAALSKAEERHGNIEERLR-----------QMEAQLEEKN--------------------QELQRA-RQREKM 439
Cdd:pfam05483  295 TKELEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNkakaahsfvvtefeattcslEELLRTeQQRLEK 374

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   440 NEEHNKRLSDTVDKLLSESNERLQL------HLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDH 513
Cdd:pfam05483  375 NEDQLKIITMELQKKSSELEEMTKFknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454


                   ....
gi 767968918   514 MRLR 517
Cdd:pfam05483  455 LEIQ 458
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 249-508 3.24e-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: 45.20  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   249 LAKVIE-LQEIISKQSREQSQMKERLASLS-------SHVTELEEDLdtARKDLIkSEEMNTKLQRDVREAMAQKEDMEE 320
Cdd:pfam10174  399 LQKKIEnLQEQLRDKDKQLAGLKERVKSLQtdssntdTALTTLEEAL--SEKERI-IERLKEQREREDRERLEELESLKK 475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   321 RITTLEKRYLAAQREAT----SVHDLNDK---LENEIANKDSMHRQTEDKNRQLQE---RLELAEQKLQQTLRKAETLPE 390
Cdd:pfam10174  476 ENKDLKEKVSALQPELTekesSLIDLKEHassLASSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVRTNPE 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   391 V-------EAELAQRVAALSKAEERHGNIEERLRQME----------AQLEE------KNQELQRARQREKMNEEHNKRL 447
Cdd:pfam10174  556 IndrirllEQEVARYKEESGKAQAEVERLLGILREVEnekndkdkkiAELESltlrqmKEQNKKVANIKHGQQEMKKKGA 635

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918   448 SDTVDKLLSESNER---LQLHLKERMAALEDKNSllrEVESAKKQLEETQ---HDKDQLVLNIEALR 508
Cdd:pfam10174  636 QLLEEARRREDNLAdnsQQLQLEELMGALEKTRQ---ELDATKARLSSTQqslAEKDGHLTNLRAER 699
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 260-492 3.74e-04

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 44.83  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   260 SKQSREQSQMKERLASLSShVTELEEDLdtARKDLIKseemntKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATS- 338
Cdd:pfam15066  288 SGASQENCKTPDTEQSFES-LQPLEEDM--ALNEVLQ------KLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKq 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   339 ------VHDLNDKLENEIANKDSMHRQTEDKNRQLQ---ERLELAEQKLQQTLRKAETLpevEAELAQRVAALSKAEERH 409
Cdd:pfam15066  359 qvfvdiINKLKENVEELIEDKYNVILEKNDINKTLQnlqEILANTQKHLQESRKEKETL---QLELKKIKVNYVHLQERY 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   410 GN-IEERLR------QMEAQLEEKNQELQRARQrekMNEEHNKRLSDTVDKLLSESNERLQ--LHLKERMAALEDKNslL 480
Cdd:pfam15066  436 ITeMQQKNKsvsqclEMDKTLSKKEEEVERLQQ---LKGELEKATTSALDLLKREKETREQefLSLQEEFQKHEKEN--L 510

                          250
                   ....*....|..
gi 767968918   481 REVESAKKQLEE 492
Cdd:pfam15066  511 EERQKLKSRLEK 522
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 160-664 4.39e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   160 VLKALKSLFEHHKALDEK--VRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKR 237
Cdd:pfam02463  228 YLDYLKLNEERIDLLQELlrDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   238 SSDGSLS----HEEDLAKVIELQEIISKQSREQSQMKERL----ASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVR 309
Cdd:pfam02463  308 RKVDDEEklkeSEKEKKKAEKELKKEKEEIEELEKELKELeikrEAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   310 EAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSM--HRQTEDKNRQLQERLELAEQKLqqtlrkaeT 387
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEeeESIELKQGKLTEEKEELEKQEL--------K 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   388 LPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLsdTVDKLLSESNERLQLHLK 467
Cdd:pfam02463  460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG--VGGRIISAHGRLGDLGVA 537

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   468 ERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPhLGSVPDFRFPMADGHTDSYs 547
Cdd:pfam02463  538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEA- 615

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   548 TSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLAnvAQAFESDADVSDGEDDRDTLLSSVDLLSPSGQADaht 627
Cdd:pfam02463  616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE--GLAEKSEVKASLSELTKELLEIQELQEKAESELA--- 690

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 767968918   628 LAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRV 664
Cdd:pfam02463  691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV 727
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 176-353 4.95e-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: 43.98  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  176 EKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIEL 255
Cdd:COG4942    58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  256 QEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM----EERITTLEKRYLA 331
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLlarlEKELAELAAELAE 217

                         170       180
                  ....*....|....*....|..
gi 767968918  332 AQREATSVHDLNDKLENEIANK 353
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAA 239
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 281-512 5.91e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   281 TELEEDLDTARKDLIKSEEMNTKLQrdVREAMAQKEDMEERI----TTLEKRYLAAQREATSVHDLNDKLENEIANKDSM 356
Cdd:pfam02463  156 LEIEEEAAGSRLKRKKKEALKKLIE--ETENLAELIIDLEELklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   357 HRQTEDKNRQLQERLElaeqklQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRqmeAQLEEKNQELQRARQR 436
Cdd:pfam02463  234 LNEERIDLLQELLRDE------QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL---KLLAKEEEELKSELLK 304

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918   437 EKMNEEHNKRlsdtVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam02463  305 LERRKVDDEE----KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 254-501 6.18e-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: 44.17  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  254 ELQEIiskqSREQSQMKERLASLSSHVTELEEDLDTARKDLikseemnTKLQRDVREAMA-QKEDMEERITTLEKRYLAA 332
Cdd:COG3096   837 ELAAL----RQRRSELERELAQHRAQEQQLRQQLDQLKEQL-------QLLNKLLPQANLlADETLADRLEELREELDAA 905

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  333 QREATSVHDLNDKLEnEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLpeveAELAQRVAALS--------- 403
Cdd:COG3096   906 QEAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFSyedavgllg 980

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  404 --------------KAEERHGNIEERLRQMEAQLEEKNQELQ----RARQREKMNEEHNKRLSDTVDKLLSESNERLQLH 465
Cdd:COG3096   981 ensdlneklrarleQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELGVQADAEAEERARIR 1060

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 767968918  466 LKERMAALEDKNSLLREVEsakKQLEETQHDKDQLV 501
Cdd:COG3096  1061 RDELHEELSQNRSRRSQLE---KQLTRCEAEMDSLQ 1093
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 268-431 7.33e-04

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: 41.87  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   268 QMKERLASLSSHVTELEEDLDTARKDLIK---------SEEMNTKLQrDVREAMAQK-EDMEERIT-TLEKrylAAQREA 336
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQELVDrleketealRERLQKDLE-EVRAKLEPYlEELQAKLGqNVEE---LRQRLE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   337 TSVHDLNDKLENEIankDSMHRQTEDKNRQLQERLELAEQKLQQTLrkAETLPEVEAELAQRVAALSK-----AEERHGN 411
Cdd:pfam01442   77 PYTEELRKRLNADA---EELQEKLAPYGEELRERLEQNVDALRARL--APYAEELRQKLAERLEELKEslapyAEEVQAQ 151

                          170       180
                   ....*....|....*....|
gi 767968918   412 IEERLRQMEAQLEEKNQELQ 431
Cdd:pfam01442  152 LSQRLQELREKLEPQAEDLR 171
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 366-511 1.04e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  366 QLQERLELAE--QKLQQTLRKAETLP----EVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQR--- 436
Cdd:COG1579     5 DLRALLDLQEldSELDRLEHRLKELPaelaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgn 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  437 ----------EKMNEEHNKRLSDTVDKLLsESNERLQlHLKERMAALEDK-NSLLREVESAKKQLEETQHDKDQLVLNIE 505
Cdd:COG1579    85 vrnnkeyealQKEIESLKRRISDLEDEIL-ELMERIE-ELEEELAELEAElAELEAELEEKKAELDEELAELEAELEELE 162


                  ....*.
gi 767968918  506 ALRAEL 511
Cdd:COG1579   163 AEREEL 168
mukB PRK04863
chromosome partition protein MukB;
326-492 1.08e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  326 EKRYLAAQREAtsvhdlndkLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA 405
Cdd:PRK04863  507 EQRHLAEQLQQ---------LRMRLSELEQRLRQQQRAERLLAE----FCKRLGKNLDDEDELEQLQEELEARLESLSES 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  406 EERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNE----RLQLHLKERMAALEDknsllR 481
Cdd:PRK04863  574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDvteyMQQLLERERELTVER-----D 648

                         170
                  ....*....|.
gi 767968918  482 EVESAKKQLEE 492
Cdd:PRK04863  649 ELAARKQALDE 659
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 291-494 1.76e-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: 42.65  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   291 RKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRY----LAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQ 366
Cdd:TIGR00618  165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   367 LQERLELAEQKLQQtlrkaetlpevEAELAQRVAAlskaeerhgniEERLRQMEAQLEEKNQELQRARQREKMnEEHNKR 446
Cdd:TIGR00618  245 LTQKREAQEEQLKK-----------QQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPL-AAHIKA 301

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 767968918   447 LSDtVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQ 494
Cdd:TIGR00618  302 VTQ-IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
PLN02939 PLN02939
transferase, transferring glycosyl groups
 222-476 1.76e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.58  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  222 DINHEQENTPSTSGKRSSDGSLSHEED--LAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEE 299
Cdd:PLN02939   70 DENGQLENTSLRTVMELPQKSTSSDDDhnRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  300 MNTKLQRDVREAMAQKEDMEERITTLEKRY--------LAAQrEATSVHDLNDKLENeiANKDSMHRQTEDKNRQLQERL 371
Cdd:PLN02939  150 ARLQALEDLEKILTEKEALQGKINILEMRLsetdarikLAAQ-EKIHVEILEEQLEK--LRNELLIRGATEGLCVHSLSK 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  372 ELAEQKLQQTLRK--AETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLE------------------EKNQELQ 431
Cdd:PLN02939  227 ELDVLKEENMLLKddIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIvaqedvsklsplqydcwwEKVENLQ 306

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767968918  432 RARQREKMNEEH-------NKRLSDTVDKL---LSESN------ERLQLhLKERMAALEDK 476
Cdd:PLN02939  307 DLLDRATNQVEKaalvldqNQDLRDKVDKLeasLKEANvskfssYKVEL-LQQKLKLLEER 366
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 344-492 1.76e-03

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   344 DKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAE----------------TLPEVEAELAQRVAALSKAEE 407
Cdd:pfam04012   39 VKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNeelarealaekkslekQAEALETQLAQQRSAVEQLRK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   408 RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEehnkrlsdTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAK 487
Cdd:pfam04012  119 QLAALETKIQQLKAKKNLLKARLKAAKAQEAVQT--------SLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190


                   ....*
gi 767968918   488 KQLEE 492
Cdd:pfam04012  191 DLDAK 195
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
345-511 1.78e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  345 KLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRK---------AETLPEVEAELAQRVAALSKAEERHGNIEER 415
Cdd:COG1842    41 EARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlareaLERKAELEAQAEALEAQLAQLEEQVEKLKEA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  416 LRQMEAQLEEKNQELQRARQREKMNeEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAK---KQLEE 492
Cdd:COG1842   121 LRQLESKLEELKAKKDTLKARAKAA-KAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEAAAELAAGDsldDELAE 199

                         170       180
                  ....*....|....*....|..
gi 767968918  493 TQHDK---DQLvlniEALRAEL 511
Cdd:COG1842   200 LEADSeveDEL----AALKAKM 217
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 358-507 1.79e-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: 42.63  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  358 RQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALskaEERHGNIEERLRQMEAQLEEKNQELQRARQRE 437
Cdd:COG3096   525 EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKELAARA 601

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  438 KMNEEHNKRLSdtvdKLLSESNERLQlHLKERMAALEDKNSLLREVESAKKQLEETqhdKDQLVLNIEAL 507
Cdd:COG3096   602 PAWLAAQDALE----RLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERL 663
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 324-445 1.92e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 41.57  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  324 TLEKRYLAAQREATSVHDLNDKLENEIAN----------KDSMHRQTE---DKNRQLQERLELAEQKLQQTLRKAETLPE 390
Cdd:cd07680    61 SLERAWGAIMTEADKVSELHQEVKNNLLNedlekvknwqKDAYHKQIMggfKETKEAEDGFRKAQKPWAKKMKELEAAKK 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767968918  391 V------EAELAQRVAALSKAEErhGNIEERLRQMEAQLEEKNQELQRARQR-EKMNEEHNK 445
Cdd:cd07680   141 AyhlackEEKLAMTREANSKAEQ--SVTPEQQKKLQDKVDKCKQDVQKTQEKyEKVLDDVGK 200
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 236-522 1.95e-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: 42.63  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  236 KRSSDGSLSHEEDLAKviELQEIISKQSREQSQMKErLASLSSHVTELEEDLDTARKDLIKseemntklqrdVREAMAQK 315
Cdd:COG3096   281 RELSERALELRRELFG--ARRQLAEEQYRLVEMARE-LEELSARESDLEQDYQAASDHLNL-----------VQTALRQQ 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  316 EDME---ERITTLEKRyLAAQREAtsVHDLNDKLENEIANK-------DSMHRQTEDKNRQL--QERLELAEQKLQQTLR 383
Cdd:COG3096   347 EKIEryqEDLEELTER-LEEQEEV--VEEAAEQLAEAEARLeaaeeevDSLKSQLADYQQALdvQQTRAIQYQQAVQALE 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  384 KAETLPEvEAELAQRvaalskaeerhgNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNkrlsdtvdkllSESNERLQ 463
Cdd:COG3096   424 KARALCG-LPDLTPE------------NAEDYLAAFRAKEQQATEEVLELEQKLSVADAAR-----------RQFEKAYE 479

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767968918  464 LHLK-----ERMAALEDKNSLLREVESAKKQLEetqhdkdqlvlNIEALRAELDHMRLRGASLH 522
Cdd:COG3096   480 LVCKiagevERSQAWQTARELLRRYRSQQALAQ-----------RLQQLRAQLAELEQRLRQQQ 532
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 193-516 1.99e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.42  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   193 EEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSgkrssdgsLSHEEdlaKVIELQEIISKQ---SREQSQM 269
Cdd:pfam05557  124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--------AEAEQ---RIKELEFEIQSQeqdSEIVKNS 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   270 KERLASLSshvtELEedldtarKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEkRYLAAQREATSVHDLNDKLENE 349
Cdd:pfam05557  193 KSELARIP----ELE-------KELERLREHNKHLNENIENKLLLKEEVEDLKRKLE-REEKYREEAATLELEKEKLEQE 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   350 I---ANKDSMH----RQTEDKNRQ----LQERLELAEQK---LQQTLRKAETLPEVEAELAQ---RVAALSKAEERHGNI 412
Cdd:pfam05557  261 LqswVKLAQDTglnlRSPEDLSRRieqlQQREIVLKEENsslTSSARQLEKARRELEQELAQylkKIEDLNKKLKRHKAL 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   413 EERLRQ-----------MEAQLEEKNQELQRARQREKMNEEHnKRLSDTVDK---LLSESNERLQLHLKERMAALEDKNS 478
Cdd:pfam05557  341 VRRLQRrvllltkerdgYRAILESYDKELTMSNYSPQLLERI-EEAEDMTQKmqaHNEEMEAQLSVAEEELGGYKQQAQT 419

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 767968918   479 LLREVESAKKQleETQHDKDQLVLNIEALRAELDHMRL 516
Cdd:pfam05557  420 LERELQALRQQ--ESLADPSYSKEEVDSLRRKLETLEL 455
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 246-513 2.05e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   246 EEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEemntklQRDVREAMAQKEDMEERITTL 325
Cdd:TIGR00606  258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDCQRELEKL 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   326 --EKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQ--------------KLQQTLRKAETLP 389
Cdd:TIGR00606  332 nkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfserqiknfhtlVIERQEDEAKTAA 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   390 EVEAELAQRvaaLSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNErlqLHLKER 469
Cdd:TIGR00606  412 QLCADLQSK---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE---LRKAER 485

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 767968918   470 MAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDH 513
Cdd:TIGR00606  486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
SAM_SARM1-like_repeat1 cd09501
SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 1010-1057 2.08e-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: 38.05  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767968918 1010 EWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSF 1057
Cdd:cd09501    11 TWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSGLLRKRF 58
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
161-425 2.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  161 LKALKSLFEHHKALDEKVR----ERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTpstsgk 236
Cdd:PRK03918  495 LIKLKELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL------ 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  237 rssdgslshEEDLAKVieLQEIISKQSREQSQMKERLASLSSHVTELEEdLDTARKDLIKSEEMNTKLQRDVREAMAQKE 316
Cdd:PRK03918  569 ---------EEELAEL--LKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELA 636

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  317 DMEERITTLEKRYLAAQREATsvhdlndklENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAEL- 395
Cdd:PRK03918  637 ETEKRLEELRKELEELEKKYS---------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERe 707

                         250       260       270
                  ....*....|....*....|....*....|..
gi 767968918  396 --AQRVAALSKAEERHGNIEERLRQMEAQLEE 425
Cdd:PRK03918  708 kaKKELEKLEKALERVEELREKVKKYKALLKE 739
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
 267-442 2.37e-03

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 41.72  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   267 SQMKERLASLSSHVTELEEDLDTARKDLIKSeemntkLQRDVREAMAQKEDMEERITTLekrYLAAQREATSVHDLNDKL 346
Cdd:pfam17097  114 SVSDPKYASLEDEVSQLEDDTLTVLNQEIDQ------IKGDILQVAQEIADKQDQVNEL---CLETSNELDECWELLNEL 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   347 ENeiankdsMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEveaelaqrvaalSKAEERHgnIEERLRQMEAQLEEK 426
Cdd:pfam17097  185 ER-------LRDQRITVEEQTSNEKDTELDPVEETYEEWKSLQE------------SLQQLEH--LKEELDQLQKQKDSL 243

                          170
                   ....*....|....*.
gi 767968918   427 NQELQRARQREKMNEE 442
Cdd:pfam17097  244 EKVDKSSINRTQNDEE 259
Caldesmon pfam02029
Caldesmon;
134-471 2.42e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   134 RHERSLRMTVvkRQAQSPAGVSSEVEVLKAlKSLFEHHKALDEKVRERLRvalERCSLLEEELGATHKELMILKEQNNQK 213
Cdd:pfam02029   13 RRAREERRRQ--KEEEEPSGQVTESVEPNE-HNSYEEDSELKPSGQGGLD---EEEAFLDRTAKREERRQKRLQEALERQ 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   214 K----TLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQ--SQMKERLASLSSHVTELEEDL 287
Cdd:pfam02029   87 KefdpTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENkwSTEVRQAEEEGEEEEDKSEEA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   288 DTARKDLIKSEEM---NTKLQRDVREAMAQKEDMEERITTLekrylAAQREATSVHDLNDKLENEIANKDSMHRQTEDKN 364
Cdd:pfam02029  167 EEVPTENFAKEEVkdeKIKKEKKVKYESKVFLDQKRGHPEV-----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   365 RQLQerlelAEQKLQQTLRKAETLPEVEAE-LAQRVA-ALSKAEERHGNIEERLRQMEaqlEEKNQELQRARQREKMNEE 442
Cdd:pfam02029  242 VFLE-----AEQKLEELRRRRQEKESEEFEkLRQKQQeAELELEELKKKREERRKLLE---EEEQRRKQEEAERKLREEE 313

                          330       340
                   ....*....|....*....|....*....
gi 767968918   443 HNKRLSDTVDKLLSESNERLQLHLKERMA 471
Cdd:pfam02029  314 EKRRMKEEIERRRAEAAEKRQKLPEDSSS 342
PTZ00121 PTZ00121
MAEBL; Provisional
 223-510 2.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  223 INHEQENTPST-----SGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASlSSHVTELEEdldtARK--DLI 295
Cdd:PTZ00121 1066 VGQDEGLKPSYkdfdfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK-AEDARKAEE----ARKaeDAR 1140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  296 KSEEMNtKLQRDVREAMAQKED----MEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKnRQLQERL 371
Cdd:PTZ00121 1141 KAEEAR-KAEDAKRVEIARKAEdarkAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE-RKAEEAR 1218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  372 ELAEQKLQQTLRKAETLPEvEAELAQRVAALSKAEERHGNIEERL-----RQMEAQLEE--KNQELQRARQREKMNEehn 444
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKK-DAEEAKKAEEERNNEEIRKFEEARMahfarRQAAIKAEEarKADELKKAEEKKKADE--- 1294

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918  445 KRLSDTVDKLlsesnERLQLHLKERMAALEDKnsllREVESAKKQLEETQHDKDQLVLNIEALRAE 510
Cdd:PTZ00121 1295 AKKAEEKKKA-----DEAKKKAEEAKKADEAK----KKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 887-949 2.65e-03

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: 37.63  E-value: 2.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767968918   887 QWDGPTVVVWLElWVGMPAwYVAACRANVKSGAIMSALSDTEIqREIGISNPLHRLKLRLAIQ 949
Cdd:pfam00536    2 GWSVEDVGEWLE-SIGLGQ-YIDSFRAGYIDGDALLQLTEDDL-LKLGVTLLGHRKKILYAIQ 61
mukB PRK04863
chromosome partition protein MukB;
237-525 2.89e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  237 RSSDGSLSHEEDLAKvielqeiiSKQSREQSQmkERLASLSSHVTELEEdldtARKDL-IKSEEMNTKLQRdVREAMAQK 315
Cdd:PRK04863  283 VHLEEALELRRELYT--------SRRQLAAEQ--YRLVEMARELAELNE----AESDLeQDYQAASDHLNL-VQTALRQQ 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  316 EDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQL---QERLELAE------QKLQQTLRKAE 386
Cdd:PRK04863  348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQtraiqyQQAVQALERAK 427

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  387 TL---PEVEAElaqrvaalskaeerhgNIEERLRQMEAQLEEKNQELQRARQREKMNEEHN----------KRLSDTVD- 452
Cdd:PRK04863  428 QLcglPDLTAD----------------NAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvRKIAGEVSr 491

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  453 -----------------KLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMR 515
Cdd:PRK04863  492 seawdvarellrrlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571

                         330
                  ....*....|
gi 767968918  516 LRGASLHHGR 525
Cdd:PRK04863  572 ESVSEARERR 581
MAP65_ASE1 pfam03999
Microtubule associated protein (MAP65/ASE1 family);
254-512 2.92e-03

Microtubule associated protein (MAP65/ASE1 family);


Pssm-ID: 427641 [Multi-domain]  Cd Length: 477  Bit Score: 41.53  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   254 ELQEIISKQSREQSQMKERLASLSSHVTELEEDLdtarkdLIKSEEMNTKLQRDV----REAMAQKEDMEERITTLEkRY 329
Cdd:pfam03999    6 HLHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDA------LSEENDKEQRILQSIadlrAEAAILCLYMRNRLLHEE-RD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   330 LAAQREATSVH----DLNDKLENEIANKDSMHRQTEDKNRQLQERL-ELAEQKLQQTlrkAETLPEVE--AELAQRVAAL 402
Cdd:pfam03999   79 PFEPKKGMSLLqkekKLDTQLEHLRKEKAPRLAEIKELLEQLQQLCeELGEEPLPLL---IDPLPSLEelESFRKHLENL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   403 SKA-EERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEH-NKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLL 480
Cdd:pfam03999  156 RNEkERRLEEVNELKKQIKLLMEELDLVPGTDFEEDLLCESEdNFCLSRENIDKLRKLIKQLEEQKAEREEKIDDLREKI 235

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 767968918   481 REV-----ESAKKQLEETQHDKDQLVLNIEALRAELD 512
Cdd:pfam03999  236 LELwnrlqVPQEEQESFVRENNSLSQDTIDALREELQ 272
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 193-492 3.14e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   193 EEELGATHKELMILKEQNNQ-KKTLTDgvldinHEQENTPSTSGKRSSDGSLSHEEDL------------AKVIELQEII 259
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKaESELKE------LEKKHQQLCEEKNALQEQLQAETELcaeaeemrarlaARKQELEEIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   260 --------SKQSREQSQMKERlASLSSHVTELEEDLD---TARK------------------DLIKSEEMNTKLQRdvre 310
Cdd:pfam01576   78 helesrleEEEERSQQLQNEK-KKMQQHIQDLEEQLDeeeAARQklqlekvtteakikkleeDILLLEDQNSKLSK---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   311 amaQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQtEDKNRQLQERL---------ELAEQKLQQT 381
Cdd:pfam01576  153 ---ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-EEKGRQELEKAkrklegestDLQEQIAELQ 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   382 LRKAETLPEVEAELAQRVAALSKAEE---RHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSEs 458
Cdd:pfam01576  229 AQIAELRAQLAKKEEELQAALARLEEetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE- 307

                          330       340       350
                   ....*....|....*....|....*....|....
gi 767968918   459 nerLQLHLKERMAALEDKNSLLREVESAKKQLEE 492
Cdd:pfam01576  308 ---LEDTLDTTAAQQELRSKREQEVTELKKALEE 338
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 337-511 3.55e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  337 TSVHDLNDKLENEIANKDSMHRQTEDKNRQLQErlelAEQKLQQTLRKAETLPEVEAELAQRVAALSKA-EERHGNIEER 415
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEE----LNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  416 LRQM----------EAQLEEKNQE--LQRARQREKMNEEHNKRLSDtvdklLSESNERLQLHLKERMAALEDKNSLLREV 483
Cdd:COG3883    92 ARALyrsggsvsylDVLLGSESFSdfLDRLSALSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAEL 166

                         170       180
                  ....*....|....*....|....*...
gi 767968918  484 ESAKKQLEETQHDKDQLVLNIEALRAEL 511
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQLSAEEAAA 194
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 1088-1152 3.68e-03

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 37.25  E-value: 3.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767968918 1088 VLVWSNDRVIRWILSIGLKEYANNLIESGVHG-ALLALDETfDFSALALllqiptQNTQARAVLER 1152
Cdd:cd09512     4 VSEWSVQQVCQWLMGLGLEQYIPEFTANNIDGqQLLQLDSS-KLKALGI------TSSSDRSLLKK 62
PRK12705 PRK12705
hypothetical protein; Provisional
 365-513 4.11e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.23  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  365 RQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERlrqmeaqlEEKNQELQRARQREKMNEEHN 444
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER--------EELQREEERLVQKEEQLDARA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767968918  445 KRLSDTVDKLLSESNerlqlHLKERMAALEDKNSLLREVESAKKQLEETQHdKDQLvlnIEALRAELDH 513
Cdd:PRK12705   98 EKLDNLENQLEEREK-----ALSARELELEELEKQLDNELYRVAGLTPEQA-RKLL---LKLLDAELEE 157
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 250-488 4.91e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   250 AKVIELQEIISKQSREQSQM----KERLASLSSHVTELEEDLDTARKdliKSEEMNTKLQ----RDVREAMAQKEDMEEr 321
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMelehKRARIELEKKASALKRQLDRESD---RNQELQKRIRllekREAEAEEALREQAEL- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   322 iTTLEKRYLAAQREA--------TSVHDLNDKLENEIA-------NKDSMHRQTEDKNRQLQERLEL-------AEQKLQ 379
Cdd:pfam05557   78 -NRLKKKYLEALNKKlnekesqlADAREVISCLKNELSelrrqiqRAELELQSTNSELEELQERLDLlkakaseAEQLRQ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   380 QTLRKAETLPEVEA---ELAQRVAALSKAEERHGNIEERLrqmeAQLEEKNQELQRARqrekmneEHNKRLSDTVDK--L 454
Cdd:pfam05557  157 NLEKQQSSLAEAEQrikELEFEIQSQEQDSEIVKNSKSEL----ARIPELEKELERLR-------EHNKHLNENIENklL 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 767968918   455 LSESNERLQLHL------KERMAALEDKNS-LLREVESAKK 488
Cdd:pfam05557  226 LKEEVEDLKRKLereekyREEAATLELEKEkLEQELQSWVK 266
mukB PRK04863
chromosome partition protein MukB;
112-488 5.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  112 AELKAERNNTRLLLEHLECLVSRH---------ERSLRMTVVKRQaqspagvssevEVLKALKSLFEHHKaldeKVRERL 182
Cdd:PRK04863  803 ATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRV-----------ELERALADHESQEQ----QQRSQL 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  183 RVALERCSLLEEELGathkELMILKEQnnqkkTLTDGVLDInheqentpstsgkrssdgslshEEDLAKVIELQEIISKQ 262
Cdd:PRK04863  868 EQAKEGLSALNRLLP----RLNLLADE-----TLADRVEEI----------------------REQLDEAEEAKRFVQQH 916

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  263 SREQSQMKERLASLSSHvtelEEDLDTarkdlikseemntkLQRDVREAMAQKEDMEERITTLEkrYLAAQREATSVHDL 342
Cdd:PRK04863  917 GNALAQLEPIVSVLQSD----PEQFEQ--------------LKQDYQQAQQTQRDAKQQAFALT--EVVQRRAHFSYEDA 976

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  343 NDKLEneiankdsmhrQTEDKNRQLQERLELAEqklQQTLRKAETLPEVEAELAQRVAALSKAEERHgnieERLRQMEAQ 422
Cdd:PRK04863  977 AEMLA-----------KNSDLNEKLRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQE 1038

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  423 LEEKNQEL---------QRARQREkmnEEHNKRLSDT------VDKLLSESNERLQlHLKERMAALEDKNSLLRE-VESA 486
Cdd:PRK04863 1039 LKQELQDLgvpadsgaeERARARR---DELHARLSANrsrrnqLEKQLTFCEAEMD-NLTKKLRKLERDYHEMREqVVNA 1114


                  ..
gi 767968918  487 KK 488
Cdd:PRK04863 1115 KA 1116
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 268-499 5.77e-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: 40.93  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   268 QMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDM-------EERITTLEKRYL-------AAQ 333
Cdd:pfam01576  774 KLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLqlqedlaASE 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   334 REATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALS---KAEERHG 410
Cdd:pfam01576  854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTtelAAERSTS 933

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   411 NIEERLRQmeaQLEEKNQELQ-RARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAAledkNSLLREVESAKK- 488
Cdd:pfam01576  934 QKSESARQ---QLERQNKELKaKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAA----NKLVRRTEKKLKe 1006

                          250
                   ....*....|....
gi 767968918   489 ---QLEETQHDKDQ 499
Cdd:pfam01576 1007 vllQVEDERRHADQ 1020
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 342-512 6.11e-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: 39.17  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   342 LNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAetLPEVEAELAQRVAALSK-----AEERHGNIEERL 416
Cdd:pfam01442    2 LEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEALRERLQKD--LEEVRAKLEPYLEELQAklgqnVEELRQRLEPYT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   417 RQMEAQLEEKNQELQRaRQREKMnEEHNKRLSDTVDKL---LSESNERLQLHLKERMAALedKNSLLREVESAKKQLEET 493
Cdd:pfam01442   80 EELRKRLNADAEELQE-KLAPYG-EELRERLEQNVDALrarLAPYAEELRQKLAERLEEL--KESLAPYAEEVQAQLSQR 155

                          170       180
                   ....*....|....*....|
gi 767968918   494 QHD-KDQLVLNIEALRAELD 512
Cdd:pfam01442  156 LQElREKLEPQAEDLREKLD 175
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-277 7.01e-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: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   45 EERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNtALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLL 124
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918  125 LEHLECLVSRHERSLRMTVVKRQAQ---SPAGVSSEVEVLKALKSLFEHhkalDEKVRERLRVALERCSLLEEELGATHK 201
Cdd:COG4942    99 LEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767968918  202 ELM-ILKEQNNQKKTLTDGVldinHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLS 277
Cdd:COG4942   175 ELEaLLAELEEERAALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 256-511 8.17e-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: 40.54  E-value: 8.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   256 QEIISKQSREQSQMKERLASLSSHVTELE--------------EDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEER 321
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKELEkkhqqlceeknalqEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   322 ITTLEKRYLAAQRE----ATSVHDLNDKLENEIANKDSMHRQ---TEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAE 394
Cdd:pfam01576   84 LEEEEERSQQLQNEkkkmQQHIQDLEEQLDEEEAARQKLQLEkvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767968918   395 LAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQRekmnEEHNKRLSDTVDKLLSESNERLQLHLKERMAALE 474
Cdd:pfam01576  164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQE----LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 767968918   475 DKNsllREVESAKKQLEETQHDKDQLVLNIEALRAEL 511
Cdd:pfam01576  240 KKE---EELQAALARLEEETAQKNNALKKIRELEAQI 273
 
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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