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Conserved domains on  [gi|1907081929|ref|XP_036012620|]
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myosin phosphatase Rho-interacting protein isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
 16-151 7.94e-80

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269942  Cd Length: 136  Bit Score: 259.29  E-value: 7.94e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   16 IFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQ 95
Cdd:cd01236      1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929   96 GTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRT 151
Cdd:cd01236     81 GSIDMSQCTEVTDAEARTGHPHSLAITTPERIHFVKADSKEEIRWWLELLAVYPRT 136
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 471-549 6.55e-26

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13275:

Pssm-ID: 473070  Cd Length: 104  Bit Score: 103.95  E-value: 6.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  471 KKGWLTKQ---------------------YEDGQAAD---LDGEINLSTCYDVTEYPVQRNYGFQIHTKEGE-FTLSAMT 525
Cdd:cd13275      1 KKGWLMKQgsrqgewskhwfvlrgaalkyYRDPSAEEageLDGVIDLSSCTEVTELPVSRNYGFQVKTWDGKvYVLSAMT 80

                           90       100
                   ....*....|....*....|....
gi 1907081929  526 SGIRRNWIQTIMKHVLPASAPDVT 549
Cdd:cd13275     81 SGIRTNWIQALRKAAGLPSPPALP 104
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 737-1051 8.31e-13

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: 74.20  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEAS------DLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATspsgawQRLHRVNQDLQSELEAQCRR 810
Cdd:COG1196    198 LERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEEL------EAELEELEAELAELEAELEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  811 QEL----ITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQgkvrEQLEEWQHSKA 886
Cdd:COG1196    272 LRLeleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEELEEELE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  887 MLSGQLRASEQKLRSTEARLLEKTQELrdLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytlll 966
Cdd:COG1196    348 EAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL------ 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  967 escEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDE 1046
Cdd:COG1196    420 ---EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496


                   ....*
gi 1907081929 1047 RDLIK 1051
Cdd:COG1196    497 LEAEA 501
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1994-2259 4.12e-09

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: 62.26  E-value: 4.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1994 AAKDEAESMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQrdfeslkatcERGFAAMEETHQKKIEDLQRQH- 2072
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRREl 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2073 QRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQ 2152
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2153 YSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLtgdgggestglpltqgKDAYELEVLL 2232
Cdd:COG1196    395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA----------------EEEAELEEEE 458

                          250       260
                   ....*....|....*....|....*..
gi 1907081929 2233 RVKESEIQYLKQEISSLKDELQTALRD 2259
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1699-2301 3.09e-06

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1699 QEPLQALHQSPEVLAAIQDELAQQLREKASILEEISAALPVLppTEPLGGCQ------RLLRMSQHLSYESCLEGLGQYS 1772
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--KEELESLEaeleelEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1773 S----LLVQDAIIQAQVCYAACRI-RLEYEKELRFYKKACQEAKGASGQKraQAVGALKEEYEELLHKQKSEYQKVITLI 1847
Cdd:TIGR02168  386 SkvaqLELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEAL 463

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1848 EKENTELKAKVSQMDHQQRCLQEAENKhSESMFALQGRYEEEIRcMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEq 1927
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAIE- 540

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1928 hhvqqmKMLEDRFQ-LKVRELQAVhqeelRALQEHYIWSLRG-----ALSLYQPSHPDSSLAPG-PSEPRAVPAAKDEAE 2000
Cdd:TIGR02168  541 ------AALGGRLQaVVVENLNAA-----KKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVK 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2001 SMSGLRERIQELEAQMGV---------MREELGHKE----LEGDVAAlqekyqrdfeslkatceRGFAAMEETHQKKIED 2067
Cdd:TIGR02168  610 FDPKLRKALSYLLGGVLVvddldnaleLAKKLRPGYrivtLDGDLVR-----------------PGGVITGGSAKTNSSI 672

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2068 LQRQhqRELEKLREEKDRLLAEETAATISAIEAMKNahREEMERELEKSQRsQISSINSDIEALRRQYLEELQSVQR--- 2144
Cdd:TIGR02168  673 LERR--REIEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRK-ELEELSRQISALRKDLARLEAEVEQlee 747

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2145 ELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTL-----LTGDGGGESTGLPL 2219
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLRERLE 827

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2220 TQGKDAYELEVLLRVKESEIQYLKQEISSLKDElqtaLRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEAL 2299
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903


                   ..
gi 1907081929 2300 GE 2301
Cdd:TIGR02168  904 RE 905
 
Name Accession Description Interval E-value
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
 16-151 7.94e-80

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269942  Cd Length: 136  Bit Score: 259.29  E-value: 7.94e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   16 IFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQ 95
Cdd:cd01236      1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929   96 GTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRT 151
Cdd:cd01236     81 GSIDMSQCTEVTDAEARTGHPHSLAITTPERIHFVKADSKEEIRWWLELLAVYPRT 136
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
 471-549 6.55e-26

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270094  Cd Length: 104  Bit Score: 103.95  E-value: 6.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  471 KKGWLTKQ---------------------YEDGQAAD---LDGEINLSTCYDVTEYPVQRNYGFQIHTKEGE-FTLSAMT 525
Cdd:cd13275      1 KKGWLMKQgsrqgewskhwfvlrgaalkyYRDPSAEEageLDGVIDLSSCTEVTELPVSRNYGFQVKTWDGKvYVLSAMT 80

                           90       100
                   ....*....|....*....|....
gi 1907081929  526 SGIRRNWIQTIMKHVLPASAPDVT 549
Cdd:cd13275     81 SGIRTNWIQALRKAAGLPSPPALP 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 737-1051 8.31e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEAS------DLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATspsgawQRLHRVNQDLQSELEAQCRR 810
Cdd:COG1196    198 LERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEEL------EAELEELEAELAELEAELEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  811 QEL----ITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQgkvrEQLEEWQHSKA 886
Cdd:COG1196    272 LRLeleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEELEEELE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  887 MLSGQLRASEQKLRSTEARLLEKTQELrdLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytlll 966
Cdd:COG1196    348 EAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL------ 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  967 escEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDE 1046
Cdd:COG1196    420 ---EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496


                   ....*
gi 1907081929 1047 RDLIK 1051
Cdd:COG1196    497 LEAEA 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 725-1006 6.71e-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: 6.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  725 SERLSTHELtSLLEKELEQSQKEASDLLEQNRLLQDQLRvALGREQSAREGYVLQTEVATSPsgawqrLHRVNQDLQSEL 804
Cdd:TIGR02168  219 KAELRELEL-ALLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSE------LEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  805 EAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEqgkvREQLEEWQHS 884
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  885 KAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDR----QKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKR 960
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907081929  961 NYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQK 1006
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
789-1154 3.52e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.47  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  789 AWQRLHRVNQDLQSELEaqcRRQELITQQiqtlkhsyGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELK 868
Cdd:PRK03918   163 AYKNLGEVIKEIKRRIE---RLEKFIKRT--------ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  869 mEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-----------------QALQRDRQKEVQ 931
Cdd:PRK03918   232 -ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeyiklSEFYEEYLDELR 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  932 RLQECIAELSQQL-GTSEQAQRLMEKKLKrnytllLESCEQEKQALLQNLKEVEDKASAYED------QLQGHVQQVEAL 1004
Cdd:PRK03918   311 EIEKRLSRLEEEInGIEERIKELEEKEER------LEELKKKLKELEKRLEELEERHELYEEakakkeELERLKKRLTGL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1005 QKEKLSETCKGSEQVHKLEEELEAREAS-IRQLAQHVQSLHDE---------------RDLIKHQFQELMER----VATS 1064
Cdd:PRK03918   385 TPEKLEKELEELEKAKEEIEEEISKITArIGELKKEIKELKKAieelkkakgkcpvcgRELTEEHRKELLEEytaeLKRI 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1065 DGDVAELQEKLRGKEVDYQNLEHSHHRVS--VQLQSVRTLLREKEEELKHI------------KETHERV--LEKKDQDL 1128
Cdd:PRK03918   465 EKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYnleelekkaeeyEKLKEKLikLKGEIKSL 544

                          410       420
                   ....*....|....*....|....*.
gi 1907081929 1129 NEALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEE 570
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1994-2259 4.12e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 4.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1994 AAKDEAESMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQrdfeslkatcERGFAAMEETHQKKIEDLQRQH- 2072
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRREl 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2073 QRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQ 2152
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2153 YSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLtgdgggestglpltqgKDAYELEVLL 2232
Cdd:COG1196    395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA----------------EEEAELEEEE 458

                          250       260
                   ....*....|....*....|....*..
gi 1907081929 2233 RVKESEIQYLKQEISSLKDELQTALRD 2259
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEE 485
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 44-145 1.63e-08

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 54.09  E-value: 1.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929    44 PIYGGWLLLAPDGtdfdnpvhRSRKWQRRFFILYEHGLLRYALDEMPTTL-PQGTINMNQCT-DVVDGEARTGQKFSLCI 121
Cdd:smart00233    1 VIKEGWLYKKSGG--------GKKSWKKRYFVLFNSTLLYYKSKKDKKSYkPKGSIDLSGCTvREAPDPDSSKKPHCFEI 72

                            90       100
                    ....*....|....*....|....*
gi 1907081929   122 LTPDKE-HFIRAETKEIISGWLEML 145
Cdd:smart00233   73 KTSDRKtLLLQAESEEEREKWVEAL 97
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 685-1180 5.32e-08

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 58.65  E-value: 5.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  685 LKTQNVHVEIEQRWHQV--ETTPLREEKQVPiAPLHLSLEDRSERLST---------HELTSLLEKELEQSQKEASDLLE 753
Cdd:pfam01576   22 QKAESELKELEKKHQQLceEKNALQEQLQAE-TELCAEAEEMRARLAArkqeleeilHELESRLEEEEERSQQLQNEKKK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  754 QNRLLQDqLRVALGREQSAREGyvLQTEVATSPS----------------GAWQRLHRVNQDLQSELEAQCRRQELITQQ 817
Cdd:pfam01576  101 MQQHIQD-LEEQLDEEEAARQK--LQLEKVTTEAkikkleedillledqnSKLSKERKLLEERISEFTSNLAEEEEKAKS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  818 IQTLKHSygeakdairhHEAEIQTLQTRLGNAAAelaiKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQ 897
Cdd:pfam01576  178 LSKLKNK----------HEAMISDLEERLKKEEK----GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  898 KLRSTEARLlektqelrdlETQQALQRDRQKEVQRLQECIAELSQQLgTSEQAQRLMEKKLKRNYTLLLESCEQEKQALL 977
Cdd:pfam01576  244 ELQAALARL----------EEETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGEELEALKTELEDTL 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  978 ------QNLK-----EVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDE 1046
Cdd:pfam01576  313 dttaaqQELRskreqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1047 RDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEelKHIKETHE-RVLEKKD 1125
Cdd:pfam01576  393 LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG--KNIKLSKDvSSLESQL 470

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929 1126 QDLNEALV----KMIALGSSLEETEI-------KLQEKEECLRRF----------VSDSPKDAKEPLSTTEPTEEG 1180
Cdd:pfam01576  471 QDTQELLQeetrQKLNLSTRLRQLEDernslqeQLEEEEEAKRNVerqlstlqaqLSDMKKKLEEDAGTLEALEEG 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2005-2197 8.15e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 8.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2005 LRERIQELEAQMGVMREELGH-----KELEGDVAALQEKyqrdFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKL 2079
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEElesklDELAEELAELEEK----LEELKEELESLEAELEELEAELEELESRLEELEEQLE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2080 REEKDRLLAEETAATIsaieamkNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLE 2159
Cdd:TIGR02168  383 TLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907081929 2160 NAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAA 2197
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 44-145 4.20e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.25  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   44 PIYGGWLLLAPDGtdfdnpvhRSRKWQRRFFILYEHGLLRYALDEMPTTL-PQGTINMNQCTDV-VDGEARTGQKFSLCI 121
Cdd:pfam00169    1 VVKEGWLLKKGGG--------KKKSWKKRYFVLFDGSLLYYKDDKSGKSKePKGSISLSGCEVVeVVASDSPKRKFCFEL 72

                           90       100
                   ....*....|....*....|....*...
gi 1907081929  122 LTPD----KEHFIRAETKEIISGWLEML 145
Cdd:pfam00169   73 RTGErtgkRTYLLQAESEEERKDWIKAI 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1699-2301 3.09e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1699 QEPLQALHQSPEVLAAIQDELAQQLREKASILEEISAALPVLppTEPLGGCQ------RLLRMSQHLSYESCLEGLGQYS 1772
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--KEELESLEaeleelEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1773 S----LLVQDAIIQAQVCYAACRI-RLEYEKELRFYKKACQEAKGASGQKraQAVGALKEEYEELLHKQKSEYQKVITLI 1847
Cdd:TIGR02168  386 SkvaqLELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEAL 463

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1848 EKENTELKAKVSQMDHQQRCLQEAENKhSESMFALQGRYEEEIRcMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEq 1927
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAIE- 540

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1928 hhvqqmKMLEDRFQ-LKVRELQAVhqeelRALQEHYIWSLRG-----ALSLYQPSHPDSSLAPG-PSEPRAVPAAKDEAE 2000
Cdd:TIGR02168  541 ------AALGGRLQaVVVENLNAA-----KKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVK 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2001 SMSGLRERIQELEAQMGV---------MREELGHKE----LEGDVAAlqekyqrdfeslkatceRGFAAMEETHQKKIED 2067
Cdd:TIGR02168  610 FDPKLRKALSYLLGGVLVvddldnaleLAKKLRPGYrivtLDGDLVR-----------------PGGVITGGSAKTNSSI 672

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2068 LQRQhqRELEKLREEKDRLLAEETAATISAIEAMKNahREEMERELEKSQRsQISSINSDIEALRRQYLEELQSVQR--- 2144
Cdd:TIGR02168  673 LERR--REIEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRK-ELEELSRQISALRKDLARLEAEVEQlee 747

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2145 ELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTL-----LTGDGGGESTGLPL 2219
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLRERLE 827

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2220 TQGKDAYELEVLLRVKESEIQYLKQEISSLKDElqtaLRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEAL 2299
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903


                   ..
gi 1907081929 2300 GE 2301
Cdd:TIGR02168  904 RE 905
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1838-2307 1.42e-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: 50.50  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1838 SEYQKVITLIEKENTELKAKVSQMDHQQRCLQ-EAENK-------HSESMFALQGRYEEEIRCMVEQLSHTENTLQAERS 1909
Cdd:pfam15921  220 SAISKILRELDTEISYLKGRIFPVEDQLEALKsESQNKielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1910 RvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEHYIWSlrgalslyqpshpDSSLAPGPSEp 1989
Cdd:pfam15921  300 Q-LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLA-------------NSELTEARTE- 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1990 ravpaaKDEAESMSG-LRERIQELEAQMGVMREELG---------------------HKELEGDVAALQ-EKYQRDFESL 2046
Cdd:pfam15921  365 ------RDQFSQESGnLDDQLQKLLADLHKREKELSlekeqnkrlwdrdtgnsitidHLRRELDDRNMEvQRLEALLKAM 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2047 KATC----ERGFAAMEETHQ--KKIEDLQRQHQRELEKLREEKDRLLA-----EETAATISAIeamkNAHREEMERELEK 2115
Cdd:pfam15921  439 KSECqgqmERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtlESSERTVSDL----TASLQEKERAIEA 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2116 SQrSQISSINS--DIEALRRQYL----EELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQ 2189
Cdd:pfam15921  515 TN-AEITKLRSrvDLKLQELQHLknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2190 ELNNRLAAEITRLRTLLTgdgggestglpLTQGKDAYELEVLLRVKESEIQY----------------LKQEISSLKDEL 2253
Cdd:pfam15921  594 QLEKEINDRRLELQEFKI-----------LKDKKDAKIRELEARVSDLELEKvklvnagserlravkdIKQERDQLLNEV 662

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081929 2254 QTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGE-----KSPEGT 2307
Cdd:pfam15921  663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlKSMEGS 721
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1824-2305 1.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1824 ALKEEYEELLhKQKSEYQKVITLIEKENTELKAKVSQmdhqqrcLQEAENKHSESMFALQGRYE--EEIRCMVEQLSHTE 1901
Cdd:PRK03918   176 RRIERLEKFI-KRTENIEELIKEKEKELEEVLREINE-------ISSELPELREELEKLEKEVKelEELKEEIEELEKEL 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1902 NTLQAErsrvLSQLDASVKDRQAMEQHHVQQMKMLEDrfqlKVRELqavhqEELRALQEHYIwSLRGALSLY--QPSHPD 1979
Cdd:PRK03918   248 ESLEGS----KRKLEEKIRELEERIEELKKEIEELEE----KVKEL-----KELKEKAEEYI-KLSEFYEEYldELREIE 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1980 SSLAPGPSEPRAVPAAKDEAESMSglrERIQELEAQMGVMREELGhkELEGDVAALQEKYQRDFESLKATCERGFAAMEE 2059
Cdd:PRK03918   314 KRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRLE--ELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2060 ThQKKIEDLQRQH---QRELEKLREEKDRLLAEEtAATISAIEAMKNAHR----------EEMERELEKSQRSQISSINS 2126
Cdd:PRK03918   389 L-EKELEELEKAKeeiEEEISKITARIGELKKEI-KELKKAIEELKKAKGkcpvcgreltEEHRKELLEEYTAELKRIEK 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2127 DIEALRRQyLEELQSVQRELEVLSEQYSQkclenahlaqaLEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLL 2206
Cdd:PRK03918   467 ELKEIEEK-ERKLRKELRELEKVLKKESE-----------LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2207 TGDGGgESTGLpLTQGKDAYELEVLLRVKESEIQYLKQEISSLK-----------DELQTALRDKKYASDKY---KDIYT 2272
Cdd:PRK03918   535 IKLKG-EIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEYlelKDAEK 612

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1907081929 2273 ELSIAKAKadcdISRLKEQLKAATEALGEKSPE 2305
Cdd:PRK03918   613 ELEREEKE----LKKLEEELDKAFEELAETEKR 641
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 462-540 2.78e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 42.15  E-value: 2.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   462 RKRPDLLNFKKGW---------LTKQYEDGQAADLDGEINLSTC---YDVTEYPVQRNYGFQIHTKEGE-FTLSAMTSGI 528
Cdd:smart00233   10 KSGGGKKSWKKRYfvlfnstllYYKSKKDKKSYKPKGSIDLSGCtvrEAPDPDSSKKPHCFEIKTSDRKtLLLQAESEEE 89

                            90
                    ....*....|..
gi 1907081929   529 RRNWIQTIMKHV 540
Cdd:smart00233   90 REKWVEALRKAI 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1699-2176 5.62e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1699 QEPLQALHQSPEVLAAIQDELAQQLREKASILEEISAALPVLPPTEPLGGCQRLLRMSQHlSYESCLEGLGQYSSLLVQd 1778
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE-RLEELEERLEELRELEEE- 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1779 aiiqaqvcyaacriRLEYEKELRFYKKACQEAKGASGQKRAQAVGALKEEYEELlHKQKSEYQKVITLIEKENTELKAKV 1858
Cdd:COG4717    165 --------------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL-QQRLAELEEELEEAQEELEELEEEL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1859 SQMDHQQRCLQEAENKHSESMFALqgryeeeIRCMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLED 1938
Cdd:COG4717    230 EQLENELEAAALEERLKEARLLLL-------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1939 RFQlkvrelQAVHQEELRALQEHYIWSLRGALSLyqpshpdsslaPGPSEPRAVPAAKDEAESMSGLRERIQELEAQMgv 2018
Cdd:COG4717    303 EAE------ELQALPALEELEEEELEELLAALGL-----------PPDLSPEELLELLDRIEELQELLREAEELEEEL-- 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2019 mreelghkelegDVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQR--QHQRELEKLREEKDRLLAEETAATIS 2096
Cdd:COG4717    364 ------------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEELE 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2097 AIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQY-----LEELQSVQRELEVLSEQYSQKCLenahLAQALEAER 2171
Cdd:COG4717    432 EELEELEEELEELEEELEE-LREELAELEAELEQLEEDGelaelLQELEELKAELRELAEEWAALKL----ALELLEEAR 506


                   ....*
gi 1907081929 2172 QALRQ 2176
Cdd:COG4717    507 EEYRE 511
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1658-2293 1.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1658 ERVIQQILetlrhptgREDQVQTSWDQnpLGEILRPgTDGSQEPLQALHQSPEvlaAIQDELAQQLREKASILEEISAAL 1737
Cdd:PRK03918   148 EKVVRQIL--------GLDDYENAYKN--LGEVIKE-IKRRIERLEKFIKRTE---NIEELIKEKEKELEEVLREINEIS 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1738 PVLPPT-EPLGGCQRLLRmsqhlSYESCLEGLgqySSLLVQDAIIQAQVCYAACRIRlEYEKELRFYKKACQEAKgaSGQ 1816
Cdd:PRK03918   214 SELPELrEELEKLEKEVK-----ELEELKEEI---EELEKELESLEGSKRKLEEKIR-ELEERIEELKKEIEELE--EKV 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1817 KRAQAVGALKEEYEElLHKQKSEYQKVITLIEKENTELKAKVSQMdhqQRCLQEAENKHSEsMFALQGRyEEEIRCMVEQ 1896
Cdd:PRK03918   283 KELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGI---EERIKELEEKEER-LEELKKK-LKELEKRLEE 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1897 LSHTENTLQAERsRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALqEHYIWSLRGALSLYQPS 1976
Cdd:PRK03918   357 LEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKA 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1977 HPDSSL--APGPSEPRAVPAAKDEAEsMSGLRERIQELEAQMGVMREELghKELEGDVaalqeKYQRDFESLKATCERGF 2054
Cdd:PRK03918   435 KGKCPVcgRELTEEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKEL--RELEKVL-----KKESELIKLKELAEQLK 506

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2055 AAMEETHQKKIEDLQRQhQRELEKLREEKDRLLAE--ETAATISAIEAMKNaHREEMERELEKSQRsQISSINSDIEALR 2132
Cdd:PRK03918   507 ELEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKGEikSLKKELEKLEELKK-KLAELEKKLDELEE-ELAELLKELEELG 583

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2133 RQYLEELQSVQRELEVLSEQYsqkcLENAHLAQALEAERQALRQCQRENQELNAHNQELNNR---LAAEITRLRTLLTGD 2209
Cdd:PRK03918   584 FESVEELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRleeLRKELEELEKKYSEE 659

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2210 GGGESTGLPLtqgkdayELEVLLRVKESEIQYLKqeisSLKDELQTALRDKKYASDKYKDIYTEL-SIAKAKAdcDISRL 2288
Cdd:PRK03918   660 EYEELREEYL-------ELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELeKLEKALE--RVEEL 726


                   ....*
gi 1907081929 2289 KEQLK 2293
Cdd:PRK03918   727 REKVK 731
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 1990-2086 8.91e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 40.80  E-value: 8.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  1990 RAVPaaKDEAESMSGLRERIQELEAQMGVMREELGHKELEGDV-AALQEKYQRDFESLKATCERGFAAM--EETHQKKIE 2066
Cdd:smart00435  269 RTVS--KTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLkRKLKSKFERDNEKLDAEVKEKKKEKkkEEKKKKQIE 346

                            90       100
                    ....*....|....*....|
gi 1907081929  2067 DLQRQHQReLEKLREEKDRL 2086
Cdd:smart00435  347 RLEERIEK-LEVQATDKEEN 365
 
Name Accession Description Interval E-value
PH_RIP cd01236
Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen ...
 16-151 7.94e-80

Rho-Interacting Protein Pleckstrin homology (PH) domain; RIP1-RhoGDI2 was obtained in a screen for proteins that bind to wild-type RhoA. RIP2, RIP3, and RIP4 were isolated from cDNA libraries with constitutively active V14RhoA (containing the C190R mutation). RIP2 represents a novel GDP/GTP exchange factor (RhoGEF), while RIP3 (p116Rip) and RIP4 are thought to be structural proteins. RhoGEF contains a Dbl(DH)/PH region, a a zinc finger motif, a leucine-rich domain, and a coiled-coil region. The last 2 domains are thought to be involved in mediating protein-protein interactions. RIP3 is a negative regulator of RhoA signaling that inhibits, either directly or indirectly, RhoA-stimulated actomyosin contractility. In plants RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in Rho proteins of plants (ROP)-regulated polar growth. It has a PH domain, two proline-rich regions which are putative binding sites for SH3 domains, and a COOH-terminal coiled-coil region which overlaps with the RhoA-binding region. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269942  Cd Length: 136  Bit Score: 259.29  E-value: 7.94e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   16 IFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQ 95
Cdd:cd01236      1 NKSKCKCCFCFRPRHSHLALEEARMQRKVIYCGWLYVAPPGTDFSNPSHRSKRWQRRWFVLYDDGELTYALDEMPDTLPQ 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929   96 GTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRT 151
Cdd:cd01236     81 GSIDMSQCTEVTDAEARTGHPHSLAITTPERIHFVKADSKEEIRWWLELLAVYPRT 136
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
 471-549 6.55e-26

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270094  Cd Length: 104  Bit Score: 103.95  E-value: 6.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  471 KKGWLTKQ---------------------YEDGQAAD---LDGEINLSTCYDVTEYPVQRNYGFQIHTKEGE-FTLSAMT 525
Cdd:cd13275      1 KKGWLMKQgsrqgewskhwfvlrgaalkyYRDPSAEEageLDGVIDLSSCTEVTELPVSRNYGFQVKTWDGKvYVLSAMT 80

                           90       100
                   ....*....|....*....|....
gi 1907081929  526 SGIRRNWIQTIMKHVLPASAPDVT 549
Cdd:cd13275     81 SGIRTNWIQALRKAAGLPSPPALP 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 737-1051 8.31e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEAS------DLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATspsgawQRLHRVNQDLQSELEAQCRR 810
Cdd:COG1196    198 LERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAELEELEAELEEL------EAELEELEAELAELEAELEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  811 QEL----ITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQgkvrEQLEEWQHSKA 886
Cdd:COG1196    272 LRLeleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEELEEELE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  887 MLSGQLRASEQKLRSTEARLLEKTQELrdLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytlll 966
Cdd:COG1196    348 EAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL------ 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  967 escEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDE 1046
Cdd:COG1196    420 ---EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496


                   ....*
gi 1907081929 1047 RDLIK 1051
Cdd:COG1196    497 LEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 791-1150 1.40e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  791 QRLHRVNqDLQSELEAQcrRQELITQQIQTLKhsYGEAKDAIRHHEAEIQTLQTRlgNAAAELAIKEQALAKLKGELKME 870
Cdd:COG1196    186 ENLERLE-DILGELERQ--LEPLERQAEKAER--YRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  871 QGKVREQLEEWQHSKAmlsgQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEV----QRLQECIAELSQQLGT 946
Cdd:COG1196    259 EAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELAELEEELEE 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  947 SEQAQRLMEKKLKRNytlllescEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSEtckgseqvhklEEEL 1026
Cdd:COG1196    335 LEEELEELEEELEEA--------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAA 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1027 EAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREK 1106
Cdd:COG1196    396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907081929 1107 EEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQ 1150
Cdd:COG1196    476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 725-1006 6.71e-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: 6.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  725 SERLSTHELtSLLEKELEQSQKEASDLLEQNRLLQDQLRvALGREQSAREGYVLQTEVATSPsgawqrLHRVNQDLQSEL 804
Cdd:TIGR02168  219 KAELRELEL-ALLVLRLEELREELEELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSE------LEEEIEELQKEL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  805 EAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEqgkvREQLEEWQHS 884
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  885 KAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDR----QKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKR 960
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907081929  961 NYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQK 1006
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
789-1154 3.52e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.47  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  789 AWQRLHRVNQDLQSELEaqcRRQELITQQiqtlkhsyGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELK 868
Cdd:PRK03918   163 AYKNLGEVIKEIKRRIE---RLEKFIKRT--------ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  869 mEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-----------------QALQRDRQKEVQ 931
Cdd:PRK03918   232 -ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaeeyiklSEFYEEYLDELR 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  932 RLQECIAELSQQL-GTSEQAQRLMEKKLKrnytllLESCEQEKQALLQNLKEVEDKASAYED------QLQGHVQQVEAL 1004
Cdd:PRK03918   311 EIEKRLSRLEEEInGIEERIKELEEKEER------LEELKKKLKELEKRLEELEERHELYEEakakkeELERLKKRLTGL 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1005 QKEKLSETCKGSEQVHKLEEELEAREAS-IRQLAQHVQSLHDE---------------RDLIKHQFQELMER----VATS 1064
Cdd:PRK03918   385 TPEKLEKELEELEKAKEEIEEEISKITArIGELKKEIKELKKAieelkkakgkcpvcgRELTEEHRKELLEEytaeLKRI 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1065 DGDVAELQEKLRGKEVDYQNLEHSHHRVS--VQLQSVRTLLREKEEELKHI------------KETHERV--LEKKDQDL 1128
Cdd:PRK03918   465 EKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYnleelekkaeeyEKLKEKLikLKGEIKSL 544

                          410       420
                   ....*....|....*....|....*.
gi 1907081929 1129 NEALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:PRK03918   545 KKELEKLEELKKKLAELEKKLDELEE 570
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 791-1186 4.44e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 4.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  791 QRLHRVNQDLQ------SELEAQCRRqeLITQQIQTLKhsYGEAKDAIRHHEAEIQTLQtrlgnaaaelaiKEQALAKLK 864
Cdd:TIGR02168  179 RKLERTRENLDrledilNELERQLKS--LERQAEKAER--YKELKAELRELELALLVLR------------LEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  865 gELKMEQGKVREQLEEwqhskamLSGQLRASEQKLRSTEARLLEKTQELRDLetqqalqrdrQKEVQRLQECIAELSQQL 944
Cdd:TIGR02168  243 -ELQEELKEAEEELEE-------LTAELQELEEKLEELRLEVSELEEEIEEL----------QKELYALANEISRLEQQK 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  945 GTSEQAQRLMEKKLKRnYTLLLESCEQEKQALLQNLKEVEDKasayEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEE 1024
Cdd:TIGR02168  305 QILRERLANLERQLEE-LEAQLEELESKLDELAEELAELEEK----LEELKEELESLEAELEELEAELEELESRLEELEE 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1025 EleareasIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEklrgkevdyQNLEHSHHRVSVQLQSVRTLLR 1104
Cdd:TIGR02168  380 Q-------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ---------EIEELLKKLEEAELKELQAELE 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1105 EKEEELKHIKETHERV---LEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECLRRFvSDSPKDAKEPLsttEPTEEGS 1181
Cdd:TIGR02168  444 ELEEELEELQEELERLeeaLEELREELEEAEQALDAAERELAQLQARLDSLERLQENL-EGFSEGVKALL---KNQSGLS 519


                   ....*
gi 1907081929 1182 GILPL 1186
Cdd:TIGR02168  520 GILGV 524
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
739-948 1.44e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 63.78  E-value: 1.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  739 KELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATSPsgAWQRLHRVN------QDLQSELEAQCRRQE 812
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLElleaelEELRAELARLEAELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  813 LITQQIQTLKHSYGEAKDAIRHH--------EAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHS 884
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081929  885 KAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEV-QRLQECIAELSQQLGTSE 948
Cdd:COG4913    393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLALRDALAEALGLDE 457
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 856-1154 1.63e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  856 KEQALAKLKGELKMEQGKVREQLEEwqhsKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQqaLQRDRQkEVQRLQE 935
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKA----LAELRKELEELEEELEQLRKELEELSRQISALRKD--LARLEA-EVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  936 CIAELSQQLgtSEQAQRLMEKKLKrnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEkLSETckg 1015
Cdd:TIGR02168  748 RIAQLSKEL--TELEAEIEELEER------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLL--- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1016 SEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQ 1095
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081929 1096 LQSVRTLLREKE----------EELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:TIGR02168  896 LEELSEELRELEskrselrrelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 836-1144 1.77e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  836 EAEIQTLQTRLGNAAAELAIKEQALAKLKGE---LKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQE 912
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  913 LRDLETQ-QALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytllLESCEQEKQALLQNLKEVEDKASAYE 991
Cdd:TIGR02168  756 LTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  992 DQLQGHVQQVEALQKEKLSEtckgSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAEL 1071
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081929 1072 QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEEL----KHIKETHERVLEKKDQDLNEALVKMIALGSSLEE 1144
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 48-145 2.69e-09

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 56.01  E-value: 2.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   48 GWLLLAPDGTdfdnpvhrSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEaRTGQKFSLCILTPDKE 127
Cdd:cd00821      3 GYLLKRGGGG--------LKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIPLSGILEVEEVS-PKERPHCFELVTPDGR 73

                           90
                   ....*....|....*....
gi 1907081929  128 HF-IRAETKEIISGWLEML 145
Cdd:cd00821     74 TYyLQADSEEERQEWLKAL 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 873-1157 3.66e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 3.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  873 KVREQLEEWQHSKAMLsgQLRASEQKLRSTEARLLEKTQELRDLETQQALqrdRQKEVQRLQECIAELSQQLGTSEQAQR 952
Cdd:COG1196    217 ELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  953 LMEKKLKRnytlllesCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETckgsEQVHKLEEELEAREAS 1032
Cdd:COG1196    292 ELLAELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1033 IRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKH 1112
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1907081929 1113 IKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECLR 1157
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1994-2259 4.12e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 4.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1994 AAKDEAESMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQrdfeslkatcERGFAAMEETHQKKIEDLQRQH- 2072
Cdd:COG1196    247 ELEELEAELEELEAELAELEAELEELRLE--LEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRREl 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2073 QRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQ 2152
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2153 YSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLtgdgggestglpltqgKDAYELEVLL 2232
Cdd:COG1196    395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA----------------EEEAELEEEE 458

                          250       260
                   ....*....|....*....|....*..
gi 1907081929 2233 RVKESEIQYLKQEISSLKDELQTALRD 2259
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 791-1152 8.13e-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: 61.24  E-value: 8.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  791 QRLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKme 870
Cdd:TIGR02169  684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-- 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  871 qgKVREQLEEWQHSKAMLSGQLRASEQKLRstEARLLEKTQELRDLEtqqalqrdrqKEVQRLQECIAELSQQLGTSEQA 950
Cdd:TIGR02169  762 --ELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE----------EEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  951 QRLMEKKLkrnytlllesceQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEARE 1030
Cdd:TIGR02169  828 KEYLEKEI------------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1031 ASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELqEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEE-E 1109
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvN 974

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1907081929 1110 LKHIKEtHERVLEKKDqDLNEALVKMIALGSSLEETEIKLQEK 1152
Cdd:TIGR02169  975 MLAIQE-YEEVLKRLD-ELKEKRAKLEEERKAILERIEEYEKK 1015
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 875-1179 1.17e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  875 REQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQalqRDRQKEVQRLQEciaelsqqlgtSEQAQRLM 954
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI---GEIEKEIEQLEQ-----------EEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  955 EKKLKRNytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEAL-QKEKLSETCKGSEQVHKLEEELEAREASI 1033
Cdd:TIGR02169  739 LEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1034 RQLAQHVQSLHDERDLIKHQFQELMERVatsdgDVAELQEKLRGKEVDyqNLEHSHHRVSVQLQSVRTLLREKEEELKHI 1113
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQR-----IDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDL 887

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081929 1114 K------ETHERVLEKKDQDLNEALVKmiaLGSSLEETEIKLQEKEECLRRFvsDSPKDAKEPLSTTEPTEE 1179
Cdd:TIGR02169  888 KkerdelEAQLRELERKIEELEAQIEK---KRKRLSELKAKLEALEEELSEI--EDPKGEDEEIPEEELSLE 954
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 44-145 1.63e-08

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 54.09  E-value: 1.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929    44 PIYGGWLLLAPDGtdfdnpvhRSRKWQRRFFILYEHGLLRYALDEMPTTL-PQGTINMNQCT-DVVDGEARTGQKFSLCI 121
Cdd:smart00233    1 VIKEGWLYKKSGG--------GKKSWKKRYFVLFNSTLLYYKSKKDKKSYkPKGSIDLSGCTvREAPDPDSSKKPHCFEI 72

                            90       100
                    ....*....|....*....|....*
gi 1907081929   122 LTPDKE-HFIRAETKEIISGWLEML 145
Cdd:smart00233   73 KTSDRKtLLLQAESEEEREKWVEAL 97
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 791-1007 1.77e-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: 59.01  E-value: 1.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  791 QRLHRVNQDL---QSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGEl 867
Cdd:COG4942     27 AELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  868 kmeqgkvreqleewqhskamLSGQLRASEQKLRSTEARLL----EKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQ 943
Cdd:COG4942    106 --------------------LAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081929  944 LGTSEQAQRLMEKKLKRNytlllescEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKE 1007
Cdd:COG4942    166 RAELEAERAELEALLAEL--------EEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
837-1008 3.96e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 3.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  837 AEIQTLQTRLGNAAAELAIKEQALAKLKgELKMEQGKVREQLEEWQHSKAMLSGQLRASE--QKLRSTEARLLEKTQELR 914
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  915 DLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQL 994
Cdd:COG4717    150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                          170
                   ....*....|....
gi 1907081929  995 QGHVQQVEALQKEK 1008
Cdd:COG4717    230 EQLENELEAAALEE 243
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 685-1180 5.32e-08

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 58.65  E-value: 5.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  685 LKTQNVHVEIEQRWHQV--ETTPLREEKQVPiAPLHLSLEDRSERLST---------HELTSLLEKELEQSQKEASDLLE 753
Cdd:pfam01576   22 QKAESELKELEKKHQQLceEKNALQEQLQAE-TELCAEAEEMRARLAArkqeleeilHELESRLEEEEERSQQLQNEKKK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  754 QNRLLQDqLRVALGREQSAREGyvLQTEVATSPS----------------GAWQRLHRVNQDLQSELEAQCRRQELITQQ 817
Cdd:pfam01576  101 MQQHIQD-LEEQLDEEEAARQK--LQLEKVTTEAkikkleedillledqnSKLSKERKLLEERISEFTSNLAEEEEKAKS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  818 IQTLKHSygeakdairhHEAEIQTLQTRLGNAAAelaiKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQ 897
Cdd:pfam01576  178 LSKLKNK----------HEAMISDLEERLKKEEK----GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  898 KLRSTEARLlektqelrdlETQQALQRDRQKEVQRLQECIAELSQQLgTSEQAQRLMEKKLKRNYTLLLESCEQEKQALL 977
Cdd:pfam01576  244 ELQAALARL----------EEETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGEELEALKTELEDTL 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  978 ------QNLK-----EVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDE 1046
Cdd:pfam01576  313 dttaaqQELRskreqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1047 RDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEelKHIKETHE-RVLEKKD 1125
Cdd:pfam01576  393 LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG--KNIKLSKDvSSLESQL 470

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929 1126 QDLNEALV----KMIALGSSLEETEI-------KLQEKEECLRRF----------VSDSPKDAKEPLSTTEPTEEG 1180
Cdd:pfam01576  471 QDTQELLQeetrQKLNLSTRLRQLEDernslqeQLEEEEEAKRNVerqlstlqaqLSDMKKKLEEDAGTLEALEEG 546
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 893-1154 6.81e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  893 RASEQKLRSTEARLL-------EKTQELRDLETQ-------QALQ---RDRQKEVQRLQecIAELSQQLGTSEQAQRLME 955
Cdd:COG1196    175 EEAERKLEATEENLErledilgELERQLEPLERQaekaeryRELKeelKELEAELLLLK--LRELEAELEELEAELEELE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  956 KKLKRnYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETckgsEQVHKLEEELEAREASIRQ 1035
Cdd:COG1196    253 AELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1036 LAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEvdyQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKE 1115
Cdd:COG1196    328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907081929 1116 ThERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:COG1196    405 L-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
PH2_MyoX cd13296
Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular ...
 48-145 7.26e-08

Myosin X Pleckstrin homology (PH) domain, repeat 2; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270108  Cd Length: 103  Bit Score: 52.47  E-value: 7.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   48 GWLLLAPDGTdfdNPVHRsRKWQRRFFILYEHGLLRYALDEmPTTLPQGTINMNQCTDVVDgeaRTGQKFSLCILTPDKE 127
Cdd:cd13296      3 GWLTKKGGGS---STLSR-RNWKSRWFVLRDTVLKYYENDQ-EGEKLLGTIDIRSAKEIVD---NDPKENRLSITTEERT 74

                           90
                   ....*....|....*...
gi 1907081929  128 HFIRAETKEIISGWLEML 145
Cdd:cd13296     75 YHLVAESPEDASQWVNVL 92
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2005-2197 8.15e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 8.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2005 LRERIQELEAQMGVMREELGH-----KELEGDVAALQEKyqrdFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKL 2079
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEElesklDELAEELAELEEK----LEELKEELESLEAELEELEAELEELESRLEELEEQLE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2080 REEKDRLLAEETAATIsaieamkNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLE 2159
Cdd:TIGR02168  383 TLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907081929 2160 NAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAA 2197
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
816-1006 1.04e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  816 QQIQTLKHSYGEAKDAIRHHEA--EIQTLQTRLGNAAAELAIKEQALAKLK--------GELKMEQGKVREQLEEWQHSK 885
Cdd:COG4913    232 EHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAEL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  886 AMLSGQLRASEQKLRSTEARLLE-KTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTL 964
Cdd:COG4913    312 ERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1907081929  965 LLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQK 1006
Cdd:COG4913    392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1993-2259 1.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1993 PAAKDEAESMSGLRERIQELEAQMGVMREELGHkeLEgDVAALQEKYQRDFESLKA--TCERGFAAmeETHQKKIEDLQR 2070
Cdd:COG4913    221 PDTFEAADALVEHFDDLERAHEALEDAREQIEL--LE-PIRELAERYAAARERLAEleYLRAALRL--WFAQRRLELLEA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2071 qhqrELEKLREEKDRLLAEETAATISAIEAmkNAHREEMERELEKSQRSQISSINSDIEALRRqyleELQSVQRELEVLS 2150
Cdd:COG4913    296 ----ELEELRAELARLEAELERLEARLDAL--REELDELEAQIRGNGGDRLEQLEREIERLER----ELEERERRRARLE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2151 EQysqkcLENAHLAQALEAE--RQALRQCQRENQELNAHNQELNNRLAAEITRLRtlltgdgggestglpltqgkdayEL 2228
Cdd:COG4913    366 AL-----LAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALR-----------------------DL 417

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907081929 2229 EVLLRVKESEIQYLKQEISSLKDELQTALRD 2259
Cdd:COG4913    418 RRELRELEAEIASLERRKSNIPARLLALRDA 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1820-2181 1.78e-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: 57.00  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1820 QAVGALKEEYEELLhkqksEYQKVitLIEKENTELKAKVSQMDHQQRCLQEAENKHSESmfalqgryEEEIRCMVEQLSH 1899
Cdd:TIGR02169  198 QQLERLRREREKAE-----RYQAL--LKEKREYEGYELLKEKEALERQKEAIERQLASL--------EEELEKLTEEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1900 TENTLqAERSRVLSQLDASVKDRQAMEQHHVQ--------QMKMLEDRFQLKVRELQ------AVHQEELRALQEHyIWS 1965
Cdd:TIGR02169  263 LEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKekigeleaEIASLERSIAEKERELEdaeerlAKLEAEIDKLLAE-IEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1966 LRGALSLYQpshpdsslapgpSEPRAVPAA-KDEAESMSGLRERIQELEAQMGVMREElgHKELegdvaalqekyqrdfe 2044
Cdd:TIGR02169  341 LEREIEEER------------KRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDE--LKDY---------------- 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2045 slkatcergfaameethQKKIEDLQRQH---QRELEKLREEKDRLLAE--ETAATISAIEAMKNAHREEME--RELEKSQ 2117
Cdd:TIGR02169  391 -----------------REKLEKLKREInelKRELDRLQEELQRLSEElaDLNAAIAGIEAKINELEEEKEdkALEIKKQ 453

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081929 2118 RSQISSINSDIEALRRQYL---EELQSVQRELEVLSEQYSQkclenahlaqaLEAERQALRQCQREN 2181
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYdlkEEYDRVEKELSKLQRELAE-----------AEAQARASEERVRGG 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2011-2305 1.80e-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: 57.00  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2011 ELEAQMGVMREELGhkELEGDVAALQEKyqrdFESLKATCERGFAAMEETHqKKIEDLQRQHQRELEKLREEKDRLlaEE 2090
Cdd:TIGR02169  671 SEPAELQRLRERLE--GLKRELSSLQSE----LRRIENRLDELSQELSDAS-RKIGEIEKEIEQLEQEEEKLKERL--EE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2091 TAATISAIEAMKNAHREEMErELEK---SQRSQISSINSDIEALRRQYLEE-LQSVQRELEVLSEQYSQKCLENAHLAQA 2166
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELK-ELEArieELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2167 LEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEStglpltqgkDAYELEVLLRVKESEIQYLKQEI 2246
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE---------ELEELEAALRDLESRLGDLKKER 891

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081929 2247 SSLKDELQTALRDKKYASDKYKDIYTELSIAKAKAdcdiSRLKEQLKAATEALGEKSPE 2305
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKL----EALEEELSEIEDPKGEDEEI 946
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 709-1114 2.12e-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: 56.67  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  709 EKQVPIAPLHLSlEDRSER----LSTHELTSLLEK---ELEQSQKEASDLLEQNRLLQDQ-LRVALGREQSAREGYVLQT 780
Cdd:pfam15921  348 EKQLVLANSELT-EARTERdqfsQESGNLDDQLQKllaDLHKREKELSLEKEQNKRLWDRdTGNSITIDHLRRELDDRNM 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  781 EVatspsgawQRLHRVNQDLQSELEAQCRRQ--------------ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRL 846
Cdd:pfam15921  427 EV--------QRLEALLKAMKSECQGQMERQmaaiqgkneslekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  847 GNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHskamlsgqLRASEQKLRSTEArllektqELRDLETQQAlQRDR 926
Cdd:pfam15921  499 SDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQT-------ECEALKLQMA-EKDK 562

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  927 QKEVQRLQ-ECIAELSQQLGTSEQAQRLMEKKLKRNYtlllesceQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEaLQ 1005
Cdd:pfam15921  563 VIEILRQQiENMTQLVGQHGRTAGAMQVEKAQLEKEI--------NDRRLELQEFKILKDKKDAKIRELEARVSDLE-LE 633

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1006 KEKLSETckGSEQVhkleeeleareasirqlaQHVQSLHDERDlikhqfqELMERVATSDGDVAELQEKLRGKEVDYQN- 1084
Cdd:pfam15921  634 KVKLVNA--GSERL------------------RAVKDIKQERD-------QLLNEVKTSRNELNSLSEDYEVLKRNFRNk 686

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1907081929 1085 ---LEHSHHRVSVQLQSVRTLLREKEEELKHIK 1114
Cdd:pfam15921  687 seeMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 692-937 2.35e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 2.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  692 VEIEQRWHQVET--TPLREEKQVPIAPLHLSLEdrSERLSTHELTSLLEKELEQSQKE-ASDLLEQNRLLQD--QLRVAL 766
Cdd:TIGR02169  268 EEIEQLLEELNKkiKDLGEEEQLRVKEKIGELE--AEIASLERSIAEKERELEDAEERlAKLEAEIDKLLAEieELEREI 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  767 GREQSAREGyvLQTEVATSPsgawQRLHRVNQDLQS-ELEAQCRRQEL--ITQQIQTLKHSYGEAKDAIRHHEAEIQTLQ 843
Cdd:TIGR02169  346 EEERKRRDK--LTEEYAELK----EELEDLRAELEEvDKEFAETRDELkdYREKLEKLKREINELKRELDRLQEELQRLS 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  844 TRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSG---QLRASEQKLRSTEARLLEKTQELRDLETQQ 920
Cdd:TIGR02169  420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKyeqELYDLKEEYDRVEKELSKLQRELAEAEAQA 499

                          250
                   ....*....|....*..
gi 1907081929  921 ALQRDRQKEVQRLQECI 937
Cdd:TIGR02169  500 RASEERVRGGRAVEEVL 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1887-2184 3.65e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 3.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1887 EEEIRCMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLE--DRFQLKVRELQAVHQEELRALQehyiw 1964
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqlEQEEEKLKERLEELEEDLSSLE----- 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1965 slrgalslyqpshpdsslapgpsepRAVPAAKDEaesMSGLRERIQELEAQMGVMREELGHKELEGDVAALQEKyQRDFE 2044
Cdd:TIGR02169  751 -------------------------QEIENVKSE---LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI-QAELS 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2045 SLKATCERGFAAMEETHQKkiedLQRQHQRE--LEKLREEK--DRLLAEETAATISAIEAMKNAHREEMERELEKSQRS- 2119
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQK----LNRLTLEKeyLEKEIQELqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAl 877

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929 2120 -QISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQEL 2184
Cdd:TIGR02169  878 rDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 44-145 4.20e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 50.25  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   44 PIYGGWLLLAPDGtdfdnpvhRSRKWQRRFFILYEHGLLRYALDEMPTTL-PQGTINMNQCTDV-VDGEARTGQKFSLCI 121
Cdd:pfam00169    1 VVKEGWLLKKGGG--------KKKSWKKRYFVLFDGSLLYYKDDKSGKSKePKGSISLSGCEVVeVVASDSPKRKFCFEL 72

                           90       100
                   ....*....|....*....|....*...
gi 1907081929  122 LTPD----KEHFIRAETKEIISGWLEML 145
Cdd:pfam00169   73 RTGErtgkRTYLLQAESEEERKDWIKAI 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 837-1177 4.99e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 4.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  837 AEIQTLQTRLGNAAAELAIKEQALAKLKGElkmeqgkvREQLEEWQHskamLSGQLRASEQKLRSTEARLLEKTQE--LR 914
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRRE--------REKAERYQA----LLKEKREYEGYELLKEKEALERQKEaiER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  915 DLETQQALQRDRQKEVQRLQECIAELSQQLgtSEQAQRLMEKKLKRNYTLllesceQEKQALLQ-NLKEVEDKASAYEDQ 993
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLL--EELNKKIKDLGEEEQLRV------KEKIGELEaEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  994 LQghvqQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQE 1073
Cdd:TIGR02169  317 LE----DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1074 KLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETH---ERVLEKKDQDLNEALVKMIALGSSLEETEIKLQ 1150
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472

                          330       340
                   ....*....|....*....|....*..
gi 1907081929 1151 EKEECLRRfVSDSPKDAKEPLSTTEPT 1177
Cdd:TIGR02169  473 DLKEEYDR-VEKELSKLQRELAEAEAQ 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2003-2301 5.04e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2003 SGLRERIQELEAQMGVMREELG-----HKELEGDVAALQE---------KYQRDFESLKAtcergfaameETHQKKIEDL 2068
Cdd:COG1196    168 SKYKERKEEAERKLEATEENLErlediLGELERQLEPLERqaekaeryrELKEELKELEA----------ELLLLKLREL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2069 QRQHQRELEKLREEKDRL--LAEETAATISAIEAMKNAHREEMERELEKSQR-----SQISSINSDIEAL---RRQYLEE 2138
Cdd:COG1196    238 EAELEELEAELEELEAELeeLEAELAELEAELEELRLELEELELELEEAQAEeyellAELARLEQDIARLeerRRELEER 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2139 LQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDgggestglp 2218
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--------- 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2219 LTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEA 2298
Cdd:COG1196    389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                   ...
gi 1907081929 2299 LGE 2301
Cdd:COG1196    469 LEE 471
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1928-2254 5.72e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 5.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1928 HHVQQMKMLEDRFQLKVRELQAVhQEELRALQEHYIWSLRGALSLYQPSHpdsslapgpsepravpaakDEAESMSGLRE 2007
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQIS-------------------ALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2008 RIQELEAQMGVMREELghKELEGDVAALQEKYQRDFESLKATcergfaameETHQKKIEDLQRQHQRELEKLREEKDRL- 2086
Cdd:TIGR02168  741 EVEQLEERIAQLSKEL--TELEAEIEELEERLEEAEEELAEA---------EAEIEELEAQIEQLKEELKALREALDELr 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2087 -----LAEETAATISAIEAMKNAHREEmERELEKSQRsQISSINSDIEALRRQyLEELQS----VQRELEVLSEQYSQKC 2157
Cdd:TIGR02168  810 aeltlLNEEAANLRERLESLERRIAAT-ERRLEDLEE-QIEELSEDIESLAAE-IEELEElieeLESELEALLNERASLE 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2158 LENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLltgdgggESTGLPLTQ-----GKDAYE-LEVL 2231
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQErlseeYSLTLEeAEAL 959

                          330       340
                   ....*....|....*....|...
gi 1907081929 2232 LRVKESEIQYLKQEISSLKDELQ 2254
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1848-2233 9.43e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 9.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1848 EKENTELKAKVSQMDHQQRCLQEAENKHSESmfalqgryEEEIRCMVEQLSHTENTLQAERSRvLSQLDASVKDRQAMEQ 1927
Cdd:COG1196    221 ELKELEAELLLLKLRELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLE-LEELELELEEAQAEEY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1928 HHVQQMKMLEDRFQLKVRELQAVHQEELRALQEhyiwslrgalslyqpshpdsslapgpsepravpaakdEAEsmsgLRE 2007
Cdd:COG1196    292 ELLAELARLEQDIARLEERRRELEERLEELEEE-------------------------------------LAE----LEE 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2008 RIQELEAQMGVMREELghKELEGDVAALQEKYQRdfeslkatcergfaamEETHQKKIEDLQRQHQRELEKLREEKDRLL 2087
Cdd:COG1196    331 ELEELEEELEELEEEL--EEAEEELEEAEAELAE----------------AEEALLEAEAELAEAEEELEELAEELLEAL 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2088 AEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQAL 2167
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081929 2168 EAERQALRQCQRENQELNA-----HNQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVLLR 2233
Cdd:COG1196    473 ALLEAALAELLEELAEAAArllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
737-947 1.11e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.87  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRL--LQDQLRVALGREQSAREGYV-LQTEVAtspsGAWQRLHRVNQDLQSELEAQcrRQEL 813
Cdd:COG3206    187 LRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAeARAELA----EAEARLAALRAQLGSGPDAL--PELL 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  814 ITQQIQTLKHSYGEAkdairhhEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLE-EWQHSKAMLSgQL 892
Cdd:COG3206    261 QSPVIQQLRAQLAEL-------EAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREA-SL 332

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929  893 RASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKE-VQRLQEciAELSQQLGTS 947
Cdd:COG3206    333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEE--ARLAEALTVG 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
737-1109 1.17e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSARegyvLQTEVATSPSG---------AWQRLHRVNQDLQSEL-EA 806
Cdd:COG4717    100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEA----LEAELAELPERleeleerleELRELEEELEELEAELaEL 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  807 QCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLkgELKMEQGKVREQLEEWQHSKA 886
Cdd:COG4717    176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLL 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  887 MLSGQL------------------------------RASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQEC 936
Cdd:COG4717    254 IAAALLallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  937 I--AELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQ-----NLKEVEDKASAYED--QLQGHVQQVEALQKE 1007
Cdd:COG4717    334 LspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAeagveDEEELRAALEQAEEyqELKEELEELEEQLEE 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1008 KLSETCKGSEQVHKLE--EELEAREASIRQLAQHVQSLHDERDLIKHQFQELMErvatsDGDVAELQEKLRGKEVDYQNL 1085
Cdd:COG4717    414 LLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELREL 488

                          410       420
                   ....*....|....*....|....
gi 1907081929 1086 EHSHHRVSVQLQSVRTLLREKEEE 1109
Cdd:COG4717    489 AEEWAALKLALELLEEAREEYREE 512
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 852-1153 1.52e-06

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: 53.82  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  852 ELAIKEQALAKL------KGELKMEQGKVREQL--EEWQHSKAMLSGQLRASEQKLRSTEARLLEKT---QELRDLETQQ 920
Cdd:pfam02463  167 LKRKKKEALKKLieetenLAELIIDLEELKLQElkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKlneERIDLLQELL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  921 ALQRDRQKEVQRLQECIAELSQQ----LGTSEQAQRLMEKKLKRNYTLL------LESCEQEKQALLQNLKEVEDKASAY 990
Cdd:pfam02463  247 RDEQEEIESSKQEIEKEEEKLAQvlkeNKEEEKEKKLQEEELKLLAKEEeelkseLLKLERRKVDDEEKLKESEKEKKKA 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  991 EDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQ---FQELMERVATSDGD 1067
Cdd:pfam02463  327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAaklKEEELELKSEEEKE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1068 VAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEI 1147
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486


                   ....*.
gi 1907081929 1148 KLQEKE 1153
Cdd:pfam02463  487 ELLLSR 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 693-1158 1.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  693 EIEQRWHQVETTPLREEKQvpIAPLHLSLEDRSERL-STHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQS 771
Cdd:COG1196    285 EAQAEEYELLAELARLEQD--IARLEERRRELEERLeELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  772 AREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAA 851
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  852 ELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSgQLRASEQKLRSTEARLLE--KTQELRDLETQQALQRDRQKE 929
Cdd:COG1196    443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEaeADYEGFLEGVKAALLLAGLRG 521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  930 VQR---------------LQECIAELSQQLGT------SEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKAS 988
Cdd:COG1196    522 LAGavavligveaayeaaLEAALAAALQNIVVeddevaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  989 AYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELME---RVATSD 1065
Cdd:COG1196    602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAallEAEAEL 681

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1066 GDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEET 1145
Cdd:COG1196    682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761

                          490
                   ....*....|...
gi 1907081929 1146 EIKLQEKEECLRR 1158
Cdd:COG1196    762 LEELERELERLER 774
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 737-1154 2.37e-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: 53.10  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLRVaLGREQSAREGYVLQTEvatspsgaWQRLhRVNQDLqSELEAQCRRQELITQ 816
Cdd:TIGR04523  150 KEKELEKLNNKYNDLKKQKEELENELNL-LEKEKLNIQKNIDKIK--------NKLL-KLELLL-SNLKKKIQKNKSLES 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  817 QIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAikeqalaklkgELKMEQGKVREQLEEWQHskamlsgQLRASE 896
Cdd:TIGR04523  219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN-----------QLKDEQNKIKKQLSEKQK-------ELEQNN 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  897 QKLRSTEARLLEKTQELRDL--ETQQALQRDRQKEVQRLQECIAELSQQLGTSEQA-QRLMEK--KLKRNytllLESCEQ 971
Cdd:TIGR04523  281 KKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIiSQLNEQisQLKKE----LTNSES 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  972 EKQALLQNLKEVEDKASAYEDQLQGHVQQVEAL--QKEKLSETCKGSEQVHKleeeleareasirQLAQHVQSLHDERDL 1049
Cdd:TIGR04523  357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLesQINDLESKIQNQEKLNQ-------------QKDEQIKKLQQEKEL 423

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1050 IKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNL--------------EHSHHRVSVQLQSVRTLLREKEEELKHIKE 1115
Cdd:TIGR04523  424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlSRSINKIKQNLEQKQKELKSKEKELKKLNE 503

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1907081929 1116 tHERVLEKKDQDLN----EALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:TIGR04523  504 -EKKELEEKVKDLTkkisSLKEKIEKLESEKKEKESKISDLED 545
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 849-1079 2.55e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  849 AAAELAIKEQALAKLKGELKmeqgKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-QALQRDRQ 927
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIA----ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElAELEKEIA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  928 KEVQRLQECIAELSQQLgtseqaqRLMEKKLKRNYTLLLESCEQEKQAL--LQNLKEVEDKASAYEDQLQGHVQQVEALQ 1005
Cdd:COG4942     94 ELRAELEAQKEELAELL-------RALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081929 1006 KEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKE 1079
Cdd:COG4942    167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 816-1146 2.56e-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: 53.10  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  816 QQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAI---KEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQL 892
Cdd:TIGR04523  117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  893 RASEQKLRSTEA-----RLLEKtqELRDLETQQA-LQRDRQKEVQRLQECIAELSQqlgTSEQAQRLMEKKLKRNYTLll 966
Cdd:TIGR04523  197 LKLELLLSNLKKkiqknKSLES--QISELKKQNNqLKDNIEKKQQEINEKTTEISN---TQTQLNQLKDEQNKIKKQL-- 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  967 esceQEKQallQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKG--------SEQVHKLEEELEAREASIRQLAQ 1038
Cdd:TIGR04523  270 ----SEKQ---KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselknqEKKLEEIQNQISQNNKIISQLNE 342

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1039 HVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKhIKETHE 1118
Cdd:TIGR04523  343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK-KLQQEK 421

                          330       340
                   ....*....|....*....|....*...
gi 1907081929 1119 RVLEKKDQDLNEALVKMIALGSSLEETE 1146
Cdd:TIGR04523  422 ELLEKEIERLKETIIKNNSEIKDLTNQD 449
PH_Gab-like cd13324
Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are ...
 45-141 2.92e-06

Grb2-associated binding protein family Pleckstrin homology (PH) domain; Gab proteins are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. There are 3 families: Gab1, Gab2, and Gab3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270133  Cd Length: 112  Bit Score: 48.18  E-value: 2.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   45 IYGGWLLLAPdgtdfdnPVHR--SRKWQRRFFILYEHGL------LRYALDEMPTTlPQGTINMNQCTDVVDGEARTGQK 116
Cdd:cd13324      2 VYEGWLTKSP-------PEKKiwRAAWRRRWFVLRSGRLsggqdvLEYYTDDHCKK-LKGIIDLDQCEQVDAGLTFEKKK 73

                           90       100
                   ....*....|....*....|....*....
gi 1907081929  117 FS----LCILTPDKEHFIRAETKEIISGW 141
Cdd:cd13324     74 FKnqfiFDIRTPKRTYYLVAETEEEMNKW 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1699-2301 3.09e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1699 QEPLQALHQSPEVLAAIQDELAQQLREKASILEEISAALPVLppTEPLGGCQ------RLLRMSQHLSYESCLEGLGQYS 1772
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL--KEELESLEaeleelEAELEELESRLEELEEQLETLR 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1773 S----LLVQDAIIQAQVCYAACRI-RLEYEKELRFYKKACQEAKGASGQKraQAVGALKEEYEELLHKQKSEYQKVITLI 1847
Cdd:TIGR02168  386 SkvaqLELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEAL 463

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1848 EKENTELKAKVSQMDHQQRCLQEAENKhSESMFALQGRYEEEIRcMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEq 1927
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAIE- 540

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1928 hhvqqmKMLEDRFQ-LKVRELQAVhqeelRALQEHYIWSLRG-----ALSLYQPSHPDSSLAPG-PSEPRAVPAAKDEAE 2000
Cdd:TIGR02168  541 ------AALGGRLQaVVVENLNAA-----KKAIAFLKQNELGrvtflPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVK 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2001 SMSGLRERIQELEAQMGV---------MREELGHKE----LEGDVAAlqekyqrdfeslkatceRGFAAMEETHQKKIED 2067
Cdd:TIGR02168  610 FDPKLRKALSYLLGGVLVvddldnaleLAKKLRPGYrivtLDGDLVR-----------------PGGVITGGSAKTNSSI 672

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2068 LQRQhqRELEKLREEKDRLLAEETAATISAIEAMKNahREEMERELEKSQRsQISSINSDIEALRRQYLEELQSVQR--- 2144
Cdd:TIGR02168  673 LERR--REIEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRK-ELEELSRQISALRKDLARLEAEVEQlee 747

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2145 ELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTL-----LTGDGGGESTGLPL 2219
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLRERLE 827

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2220 TQGKDAYELEVLLRVKESEIQYLKQEISSLKDElqtaLRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEAL 2299
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAE----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903


                   ..
gi 1907081929 2300 GE 2301
Cdd:TIGR02168  904 RE 905
PH_PLEKHD1 cd13281
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH ...
 64-145 3.69e-06

Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain; Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, , dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270099  Cd Length: 139  Bit Score: 48.47  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   64 HRSRKWQRRFFILYEHGLLRYALDEMPT--------TLPQGTINMNQCTDVVDGEarTGQKFSLCILTPD--KEHFIRAE 133
Cdd:cd13281     25 HQSAKWSKRFFIIKEGFLLYYSESEKKDfektrhfnIHPKGVIPLGGCSIEAVED--PGKPYAISISHSDfkGNIILAAD 102

                           90
                   ....*....|..
gi 1907081929  134 TKEIISGWLEML 145
Cdd:cd13281    103 SEFEQEKWLDML 114
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 722-1051 4.32e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  722 EDRSERLSTheLTSLLEKELEQSQKEASDLLEQNRLLqdqlrvalgREQSAREGYVLqtevatspSGAWQRLHRVNQDLQ 801
Cdd:TIGR02169  183 EENIERLDL--IIDEKRQQLERLRREREKAERYQALL---------KEKREYEGYEL--------LKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  802 SELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQ--------TLQTRLGNAAAELAIKEQALAKLKGELKMEQGK 873
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  874 VR---EQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-----QALQRDRQKEVQRlQECIAELSQQLG 945
Cdd:TIGR02169  324 LAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdKEFAETRDELKDY-REKLEKLKREIN 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  946 TSEQAQ-RLMEKKLKRNYTLL-----LESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKL---SETCKGS 1016
Cdd:TIGR02169  403 ELKRELdRLQEELQRLSEELAdlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYdlkEEYDRVE 482

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1907081929 1017 EQVHKLEEELEAREASIRQLAQHVQSLHDERDLIK 1051
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 736-983 5.32e-06

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: 51.43  E-value: 5.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  736 LLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQ----CRRQ 811
Cdd:pfam07888   31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykelSASS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  812 ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAikeqalaklkgELKMEQGKVREQLEEWQHSKAMLSGQ 891
Cdd:pfam07888  111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-----------RMKERAKKAGAQRKEEEAERKQLQAK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  892 LRASEQKLRSTEARLlektQELRDLETQQALQrdrqkeVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTL--LLESC 969
Cdd:pfam07888  180 LQQTEEELRSLSKEF----QELRNSLAQRDTQ------VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLqeRLNAS 249

                          250
                   ....*....|....
gi 1907081929  970 EQEKQALLQNLKEV 983
Cdd:pfam07888  250 ERKVEGLGEELSSM 263
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
875-1111 6.74e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  875 REQLEEWQHSKAMLSgQLRASEQKLRSTEARLlEKTQELRD----------LETQQALQRDRQKEVQRLQECIAELSQQL 944
Cdd:COG4913    241 HEALEDAREQIELLE-PIRELAERYAAARERL-AELEYLRAalrlwfaqrrLELLEAELEELRAELARLEAELERLEARL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  945 GTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQghvqqvealqkeKLSETCKGSEQVHKLEE 1024
Cdd:COG4913    319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA------------ALGLPLPASAEEFAALR 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1025 eleareasiRQLAQHVQSLHDERDlikhqfqELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLR 1104
Cdd:COG4913    387 ---------AEAAALLEALEEELE-------ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450

                          250
                   ....*....|.
gi 1907081929 1105 E----KEEELK 1111
Cdd:COG4913    451 EalglDEAELP 461
PH_Gab2_2 cd13384
Grb2-associated binding protein family pleckstrin homology (PH) domain; The Gab subfamily ...
 45-141 7.07e-06

Grb2-associated binding protein family pleckstrin homology (PH) domain; The Gab subfamily includes several Gab proteins, Drosophila DOS and C. elegans SOC-1. They are scaffolding adaptor proteins, which possess N-terminal PH domains and a C-terminus with proline-rich regions and multiple phosphorylation sites. Following activation of growth factor receptors, Gab proteins are tyrosine phosphorylated and activate PI3K, which generates 3-phosphoinositide lipids. By binding to these lipids via the PH domain, Gab proteins remain in proximity to the receptor, leading to further signaling. While not all Gab proteins depend on the PH domain for recruitment, it is required for Gab activity. Members here include insect, nematodes, and crustacean Gab2s. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241535  Cd Length: 115  Bit Score: 47.05  E-value: 7.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   45 IYGGWLLLAPdgtdfdnPVHR--SRKWQRRFFILY-----EHGLLRYALDEMPTTLpQGTINMNQCTDV-----VDGEAR 112
Cdd:cd13384      4 VYEGWLTKSP-------PEKRiwRAKWRRRYFVLRqseipGQYFLEYYTDRTCRKL-KGSIDLDQCEQVdagltFETKNK 75

                           90       100
                   ....*....|....*....|....*....
gi 1907081929  113 TGQKFSLCILTPDKEHFIRAETKEIISGW 141
Cdd:cd13384     76 LKDQHIFDIRTPKRTYYLVADTEDEMNKW 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2032-2341 7.22e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 7.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2032 VAALQEKYQRDFESLKATCERgfaamEETHQKKIEDLQRQhqreLEKLREEKDRLL--------AEETAATI--SAIEAM 2101
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEEN-----IERLDLIIDEKRQQ----LERLRREREKAEryqallkeKREYEGYEllKEKEAL 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2102 K------NAHREEMERELEKSQRsQISSINSDIEALRRqyleELQSVQRELEVLSEQYSQKCLENAHLAQA-LEAERQAL 2174
Cdd:TIGR02169  236 ErqkeaiERQLASLEEELEKLTE-EISELEKRLEEIEQ----LLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSI 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2175 RQCQRENQELNAHNQELN---NRLAAEITRLRTLLtgdgggESTGLPLTQGKDAY-ELEVLLRVKESEIQYLKQEISSLK 2250
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEaeiDKLLAEIEELEREI------EEERKRRDKLTEEYaELKEELEDLRAELEEVDKEFAETR 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2251 DELQTALRDKKYASDKYKDIYTELSI---AKAKADCDISRLKEQLKAATEALGEkSPEGTTVSGYDIMKSKSNPDFLKKD 2327
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELDRlqeELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAAD 463

                          330
                   ....*....|....
gi 1907081929 2328 RSCVTRQLRNIRSK 2341
Cdd:TIGR02169  464 LSKYEQELYDLKEE 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1816-2249 1.32e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1816 QKRAQAVGALKEEYEELLHKQKSEYQKVITLIEKENTELKAKVSQMDHQQRCLQEAEN--KHSESMFALQGRYEEEIRCM 1893
Cdd:COG1196    347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEEL 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1894 VEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKmLEDRFQLKVRELQAVHQEELRALQEHyiWSLRGALSLY 1973
Cdd:COG1196    427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAARL--LLLLEAEADY 503

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1974 QPSHPDSSLAPGPSEPRAVPAAKDEAesMSGLRERIQELEAQMGVMREELGHKELEgdVAALQEKYQRDFESLKAT---- 2049
Cdd:COG1196    504 EGFLEGVKAALLLAGLRGLAGAVAVL--IGVEAAYEAALEAALAAALQNIVVEDDE--VAAAAIEYLKAAKAGRATflpl 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2050 --CERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRL---LAEETAATISAIEAMKNAHREEMERELEKSQRSQISSI 2124
Cdd:COG1196    580 dkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2125 NSDIEALRRQYLEELQSVQRELEVLSEQ--YSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRL 2202
Cdd:COG1196    660 GSLTGGSRRELLAALLEAEAELEELAERlaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907081929 2203 RTLltgdgggESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSL 2249
Cdd:COG1196    740 ELL-------EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1838-2307 1.42e-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: 50.50  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1838 SEYQKVITLIEKENTELKAKVSQMDHQQRCLQ-EAENK-------HSESMFALQGRYEEEIRCMVEQLSHTENTLQAERS 1909
Cdd:pfam15921  220 SAISKILRELDTEISYLKGRIFPVEDQLEALKsESQNKielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1910 RvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEHYIWSlrgalslyqpshpDSSLAPGPSEp 1989
Cdd:pfam15921  300 Q-LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLA-------------NSELTEARTE- 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1990 ravpaaKDEAESMSG-LRERIQELEAQMGVMREELG---------------------HKELEGDVAALQ-EKYQRDFESL 2046
Cdd:pfam15921  365 ------RDQFSQESGnLDDQLQKLLADLHKREKELSlekeqnkrlwdrdtgnsitidHLRRELDDRNMEvQRLEALLKAM 438

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2047 KATC----ERGFAAMEETHQ--KKIEDLQRQHQRELEKLREEKDRLLA-----EETAATISAIeamkNAHREEMERELEK 2115
Cdd:pfam15921  439 KSECqgqmERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtlESSERTVSDL----TASLQEKERAIEA 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2116 SQrSQISSINS--DIEALRRQYL----EELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQ 2189
Cdd:pfam15921  515 TN-AEITKLRSrvDLKLQELQHLknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2190 ELNNRLAAEITRLRTLLTgdgggestglpLTQGKDAYELEVLLRVKESEIQY----------------LKQEISSLKDEL 2253
Cdd:pfam15921  594 QLEKEINDRRLELQEFKI-----------LKDKKDAKIRELEARVSDLELEKvklvnagserlravkdIKQERDQLLNEV 662

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081929 2254 QTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGE-----KSPEGT 2307
Cdd:pfam15921  663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlKSMEGS 721
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 798-1154 1.64e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  798 QDLQSELEAQCRRQELITQQIQTLKHSYGEAKDA-------IRHHEAEIQTLQTRLGNAAAELAI----KEQALAK-LKG 865
Cdd:TIGR04523  235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlsekqkeLEQNNKKIKELEKQLNQLKSEISDlnnqKEQDWNKeLKS 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  866 ELKMEQGKVRE---QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQ-QALQRDRQ---KEVQRLQECIA 938
Cdd:TIGR04523  315 ELKNQEKKLEEiqnQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEiEKLKKENQsykQEIKNLESQIN 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  939 ELSQQLGTSEQAQRLME---KKLKRNYTLLLESCEQEKQALLQN---LKEVEDKASAYEDQLQGHVQQVEAlQKEKLSEt 1012
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDeqiKKLQQEKELLEKEIERLKETIIKNnseIKDLTNQDSVKELIIKNLDNTRES-LETQLKV- 472

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1013 ckgseqvhkleeeleaREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRV 1092
Cdd:TIGR04523  473 ----------------LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081929 1093 SVQLQSVRTLLREKEEELKhiKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:TIGR04523  537 ESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
mukB PRK04863
chromosome partition protein MukB;
721-1061 2.13e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.96  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  721 LEDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQtevatspsgawQRLHRVNQDL 800
Cdd:PRK04863   289 LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ-----------EKIERYQADL 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  801 QsELEAQCRRQELITQQIQTLKHSYGEAKDAIrhhEAEIQTLQTRLGNAAAELAIKE----------QALAKLKGELK-- 868
Cdd:PRK04863   358 E-ELEERLEEQNEVVEEADEQQEENEARAEAA---EEEVDELKSQLADYQQALDVQQtraiqyqqavQALERAKQLCGlp 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  869 -MEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEA--RLLEKTQEL-----------------RDLETQQALQRDRQK 928
Cdd:PRK04863   434 dLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahSQFEQAYQLvrkiagevsrseawdvaRELLRRLREQRHLAE 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  929 EVQRLQECIAELSQQLGTSEQAQRLM---EKKLKRNYTL--LLESCEQEKQALLQNLKE----VEDKASAYEDQLQGHVQ 999
Cdd:PRK04863   514 QLQQLRMRLSELEQRLRQQQRAERLLaefCKRLGKNLDDedELEQLQEELEARLESLSEsvseARERRMALRQQLEQLQA 593

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081929 1000 QVEALQK---------EKLSETCkgsEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERV 1061
Cdd:PRK04863   594 RIQRLAArapawlaaqDALARLR---EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 797-1153 2.15e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  797 NQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGElkmEQGKvRE 876
Cdd:TIGR04523  309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSY-KQ 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  877 QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQ----ALQRDRQKEVQRLQECIAELSQQLGTSEQAQR 952
Cdd:TIGR04523  385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIerlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  953 LMEKKLKrnytLLLESCEQEKQALLQNLKEVEDKASAYeDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREAS 1032
Cdd:TIGR04523  465 SLETQLK----VLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1033 IRQLAQHVQSLHDE--RDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEEL 1110
Cdd:TIGR04523  540 ISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1907081929 1111 KHIKETHERVLEKKDqDLNEALVKMIALGSSLEETEIKLQEKE 1153
Cdd:TIGR04523  620 EKAKKENEKLSSIIK-NIKSKKNKLKQEVKQIKETIKEIRNKW 661
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
812-1123 2.27e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 48.75  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  812 ELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQtrlgNAAAELAIKEQALAKLKGELKMEQGKVREQLEEwqhskamLSGQ 891
Cdd:COG1340      4 DELSSSLEELEEKIEELREEIEELKEKRDELN----EELKELAEKRDELNAQVKELREEAQELREKRDE-------LNEK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  892 LRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTS----EQAQRLMEK--KLKRNYTLL 965
Cdd:COG1340     73 VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEvlspEEEKELVEKikELEKELEKA 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  966 LESCEQEKQallqnLKEVEDKASAYEDQLQGHVQQVEALQKEklsetckgSEQVHKleeeleareaSIRQLAQHVQSLHD 1045
Cdd:COG1340    153 KKALEKNEK-----LKELRAELKELRKEAEEIHKKIKELAEE--------AQELHE----------EMIELYKEADELRK 209

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081929 1046 ERDLIKHQFQELMERvatsdgdVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRtllreKEEELKHIKETHERVLEK 1123
Cdd:COG1340    210 EADELHKEIVEAQEK-------ADELHEEIIELQKELRELRKELKKLRKKQRALK-----REKEKEELEEKAEEIFEK 275
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
904-1154 2.76e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  904 ARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKklkrnytlllescEQEKQALLQNLKEV 983
Cdd:COG4913    194 LRLLHKTQSFKPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALED-------------AREQIELLEPIREL 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  984 EDKASAYEDQLQGHVQQVEALQKEKlsetckGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVAT 1063
Cdd:COG4913    261 AERYAAARERLAELEYLRAALRLWF------AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1064 SDGD-VAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSL 1142
Cdd:COG4913    335 NGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414

                          250
                   ....*....|..
gi 1907081929 1143 EETEIKLQEKEE 1154
Cdd:COG4913    415 RDLRRELRELEA 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 737-950 3.00e-05

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: 48.99  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLrvalgrEQSAREGYVLQTEVATspsgAWQRLHRVNQDLQSELEAQCRRQELITQ 816
Cdd:COG4942     39 LEKELAALKKEEKALLKQLAALERRI------AALARRIRALEQELAA----LEAELAELEKEIAELRAELEAQKEELAE 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  817 QIQTL----KHSY-------GEAKDAIRHHEAeIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSK 885
Cdd:COG4942    109 LLRALyrlgRQPPlalllspEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081929  886 AMLSGQLRASEQKLRSTEARLLEKTQELRDLetqqalqrdrQKEVQRLQECIAELSQQLGTSEQA 950
Cdd:COG4942    188 AALEALKAERQKLLARLEKELAELAAELAEL----------QQEAEELEALIARLEAEAAAAAER 242
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
722-1154 3.19e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  722 EDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYvlqTEVATSPSGAWQRLHRVNQDLQ 801
Cdd:PRK02224   293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL---REDADDLEERAEELREEAAELE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  802 SELEAqCRRQelitqqiqtlkhsYGEAKDAIRHHEAEIQTLQTRLGNAAAELaikeQALAKLKGELKMEQGKVREQLEEw 881
Cdd:PRK02224   370 SELEE-AREA-------------VEDRREEIEELEEEIEELRERFGDAPVDL----GNAEDFLEELREERDELREREAE- 430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  882 qhskamLSGQLRASEQKLRSTEaRLLEK------TQELRDLETQQALQRDRQKevqrlqecIAELSQQLGTSEQAQRLME 955
Cdd:PRK02224   431 ------LEATLRTARERVEEAE-ALLEAgkcpecGQPVEGSPHVETIEEDRER--------VEELEAELEDLEEEVEEVE 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  956 KKLKRNYTllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQvhklEEELEAREASIRQ 1035
Cdd:PRK02224   496 ERLERAED--LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK----REAAAEAEEEAEE 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1036 LAQHVQSLHDERDLIKHQFQELmERVATSDGDVAELQ---EKLRGKEVDYQNLE-HSHHRVSVQLQSVRTLLREKE---- 1107
Cdd:PRK02224   570 AREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEdeiERLREKREALAELNdERRERLAEKRERKRELEAEFDeari 648

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907081929 1108 EELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEE 1154
Cdd:PRK02224   649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 696-1151 3.32e-05

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 49.36  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  696 QRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLE-KELEQSQKEASDLLEQNRLLQDQLRVALGREQSARE 774
Cdd:pfam07111  146 QRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEaKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRK 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  775 gYVLQTEVATSPSGAWqrlhrvnqdlqsELEaqcrRQELItQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELA 854
Cdd:pfam07111  226 -YVGEQVPPEVHSQTW------------ELE----RQELL-DTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELT 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  855 IKEQALAKLKGELKMeqgKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQA-----LQR---DR 926
Cdd:pfam07111  288 RKIQPSDSLEPEFPK---KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSqeqaiLQRalqDK 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  927 QKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLL------LESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQ 1000
Cdd:pfam07111  365 AAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLkfvvnaMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRK 444

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1001 V---EALQKEKLS------ETCKGSEqvhKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERvATSDGDVAEL 1071
Cdd:pfam07111  445 VhtiKGLMARKVAlaqlrqESCPPPP---PAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGR-AREQGEAERQ 520

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1072 Q--EKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKM-IALGSSLEETEIK 1148
Cdd:pfam07111  521 QlsEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVeTRLREQLSDTKRR 600


                   ...
gi 1907081929 1149 LQE 1151
Cdd:pfam07111  601 LNE 603
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 702-1168 3.57e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 3.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  702 ETTPLREEkQVPIAPLHLSLEDRSERLSTHELTSLLEKELEQ-----SQKEASDLLEQNRLLQDQLRVALGREQSAREGY 776
Cdd:TIGR00618  401 ELDILQRE-QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  777 VLQTEVATSPSGAWQRLHRVnQDLQSELEAQCRRQELITQQIQTL------------KHSY-GEAKDAIRHHEAEIQTLQ 843
Cdd:TIGR00618  480 QIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNPARQDIDNPgpltrrmqrgeqTYAQlETSEEDVYHQLTSERKQR 558

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  844 TRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSgqlraseqklRSTEARLLEKTQELRDLETQQALQ 923
Cdd:TIGR00618  559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----------EAEDMLACEQHALLRKLQPEQDLQ 628

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  924 RDRQKEvqrlQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQN-LKEVEDKASAYEDQLQGHVQQVE 1002
Cdd:TIGR00618  629 DVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLaLQKMQSEKEQLTYWKEMLAQCQT 704

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1003 ALQKEKLSETcKGSEQVHKLEEELEAREASIR-QLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVD 1081
Cdd:TIGR00618  705 LLRELETHIE-EYDREFNEIENASSSLGSDLAaREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1082 YQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECLRRFVS 1161
Cdd:TIGR00618  784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863


                   ....*..
gi 1907081929 1162 DSPKDAK 1168
Cdd:TIGR00618  864 LTQEQAK 870
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1982-2212 6.22e-05

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: 47.84  E-value: 6.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1982 LAPGPSEPRAVPAAKDEAEsMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQRDFESLKATcERGFAAMEeth 2061
Cdd:COG4942     10 LLALAAAAQADAAAEAEAE-LEQLQQEIAELEKELAALKKE--EKALLKQLAALERRIAALARRIRAL-EQELAALE--- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2062 qKKIEDLQRQH---QRELEKLREEKDRLLA--------EETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEA 2130
Cdd:COG4942     83 -AELAELEKEIaelRAELEAQKEELAELLRalyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2131 LRR------QYLEELQSVQRELE----VLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEIT 2200
Cdd:COG4942    162 LAAlraeleAERAELEALLAELEeeraALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

                          250
                   ....*....|..
gi 1907081929 2201 RLRTLLTGDGGG 2212
Cdd:COG4942    242 RTPAAGFAALKG 253
PH_DOCK-D cd13267
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also ...
 48-145 8.05e-05

Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270087  Cd Length: 126  Bit Score: 44.24  E-value: 8.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   48 GWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHG----LLRYALDEMPTTlPQGTINMNQCTDVVDGEARTGQKFSLCILT 123
Cdd:cd13267     10 GYLYKGPENSSDSFISLAMKSFKRRFFHLKQLVdgsyILEFYKDEKKKE-AKGTIFLDSCTGVVQNSKRRKFCFELRMQD 88

                           90       100
                   ....*....|....*....|..
gi 1907081929  124 PdKEHFIRAETKEIISGWLEML 145
Cdd:cd13267     89 K-KSYVLAAESEAEMDEWISKL 109
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2005-2203 8.88e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 8.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2005 LRERIQELEAQMGVMREELghKELEGDVAALQEKYQrdfeslkatcERGFAAMEETHQKKIEDLQRQhqreLEKLREEKD 2084
Cdd:COG3206    173 ARKALEFLEEQLPELRKEL--EEAEAALEEFRQKNG----------LVDLSEEAKLLLQQLSELESQ----LAEARAELA 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2085 RLLAEETAATiSAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEE---LQSVQRELEVLSEQYSQkclENA 2161
Cdd:COG3206    237 EAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQ---EAQ 312

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907081929 2162 HLAQALEAERQALRQCQRE-NQELNAHNQELN--NRLAAEITRLR 2203
Cdd:COG3206    313 RILASLEAELEALQAREASlQAQLAQLEARLAelPELEAELRRLE 357
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 914-1162 9.00e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 9.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  914 RDLETQQALqRDRQKEVQRLQECIAELSQQLGT----SEQAQRLMEKKLKRNytlllescEQEKQALLQNLKEVEDKASA 989
Cdd:TIGR02168  173 RRKETERKL-ERTRENLDRLEDILNELERQLKSlerqAEKAERYKELKAELR--------ELELALLVLRLEELREELEE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  990 YEDQLQGHVQQVEALQKEKlsetckgseqvhkleeelEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVA 1069
Cdd:TIGR02168  244 LQEELKEAEEELEELTAEL------------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1070 ELQEKLRgkevdyqNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHErVLEKKDQDLNEALVKMIALgssLEETEIKL 1149
Cdd:TIGR02168  306 ILRERLA-------NLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAE---LEELESRL 374

                          250
                   ....*....|...
gi 1907081929 1150 QEKEECLRRFVSD 1162
Cdd:TIGR02168  375 EELEEQLETLRSK 387
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 798-1003 9.48e-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: 9.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  798 QDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLkgelkmeqgkvREQ 877
Cdd:COG3883     19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER-----------REE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  878 LEEWQHSKAMLSGQLRASEQKLRSTE-ARLLEKTQELRDL-ETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLME 955
Cdd:COG3883     88 LGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907081929  956 KKLKRnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEA 1003
Cdd:COG3883    168 AAKAE-----LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2000-2265 1.05e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2000 ESMSGLRERIQELEAQMGVMREELGH------KELEGDVAALQEKYqRDFESLKATCERGFAAMEEtHQKKIEDLQRQHQ 2073
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEQLRVKEKI-GELEAEIASLERSIAEKER-ELEDAEERLAKLE 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2074 RELEKLREEKDRL---LAEETAATISAIEAMKNAHREEMEReleksqRSQISSINSDIEALRR---QYLEELQSVQRELE 2147
Cdd:TIGR02169  329 AEIDKLLAEIEELereIEEERKRRDKLTEEYAELKEELEDL------RAELEEVDKEFAETRDelkDYREKLEKLKREIN 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2148 VLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTlltgdgggestglpLTQGKDAYE 2227
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ--------------LAADLSKYE 468

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907081929 2228 LEvlLRVKESEIQYLKQEISSLKDELQTALRDKKYASD 2265
Cdd:TIGR02169  469 QE--LYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 2007-2183 1.11e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2007 ERIQELEA-QMGVMRE-ELGHKELEG--DVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKLREE 2082
Cdd:pfam17380  375 SRMRELERlQMERQQKnERVRQELEAarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2083 KdrLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISS---INSDIEALRRQYLEELQS---VQRELE-----VLSE 2151
Cdd:pfam17380  455 E--QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkiLEKELEERKQAMIEEERKrklLEKEMEerqkaIYEE 532

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907081929 2152 QYSQKCLENAHLAQALEAERQALRQCQRENQE 2183
Cdd:pfam17380  533 ERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
PH_TBC1D2A cd01265
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1 ...
 67-145 1.16e-04

TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269966  Cd Length: 102  Bit Score: 43.47  E-value: 1.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081929   67 RKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQkFSlcILTPDKEHFIRAETKEIISGWLEML 145
Cdd:cd01265     17 KGWKRRWFVLDESKCQLYYYRSPQDATPLGSIDLSGAAFSYDPEAEPGQ-FE--IHTPGRVHILKASTRQAMLYWLQAL 92
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 1806-2290 1.17e-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: 47.41  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1806 ACQEAKGASGQKRAQAVGALKEEYEELLHKQKsEYQKVITLIEKENTELKAKVSqmdhqqrclqEAENKHSESMFALqgr 1885
Cdd:pfam05483  198 AFEELRVQAENARLEMHFKLKEDHEKIQHLEE-EYKKEINDKEKQVSLLLIQIT----------EKENKMKDLTFLL--- 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1886 yeEEIRCMVEQLSHtENTLQAERSRVLSQ----LDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEH 1961
Cdd:pfam05483  264 --EESRDKANQLEE-KTKLQDENLKELIEkkdhLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEEL 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1962 YIWSLRGALSLYQPSHPDSSLAPG-PSEPRAVPAAKD-------EAESMSGLRERIQELEAQMGVMREELgHKELEGDVA 2033
Cdd:pfam05483  341 NKAKAAHSFVVTEFEATTCSLEELlRTEQQRLEKNEDqlkiitmELQKKSSELEEMTKFKNNKEVELEEL-KKILAEDEK 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2034 ALQEKYQRD--FESLKATcERGFAAMEETHQKKIEDLQRQ----------HQRELEKLREE--KDRLLAEETAATISAIE 2099
Cdd:pfam05483  420 LLDEKKQFEkiAEELKGK-EQELIFLLQAREKEIHDLEIQltaiktseehYLKEVEDLKTEleKEKLKNIELTAHCDKLL 498

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2100 AMKNAHREE---MERELEKSQRSQISSINSDIEALRR-QYLEELQSVQR-ELEVLSEQYSQ-----KCLENAHLAQALEA 2169
Cdd:pfam05483  499 LENKELTQEasdMTLELKKHQEDIINCKKQEERMLKQiENLEEKEMNLRdELESVREEFIQkgdevKCKLDKSEENARSI 578

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2170 ERQALRQCQRENQELNAHNQ-----ELNNRLAAEITRLRTLLTGDGGGESTGLpltqgkDAYELEVllRVKESEIQYLKQ 2244
Cdd:pfam05483  579 EYEVLKKEKQMKILENKCNNlkkqiENKNKNIEELHQENKALKKKGSAENKQL------NAYEIKV--NKLELELASAKQ 650

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1907081929 2245 EISSLKDELQTALRDKKYASDKykdIYTELSIAKAKADCDISRLKE 2290
Cdd:pfam05483  651 KFEEIIDNYQKEIEDKKISEEK---LLEEVEKAKAIADEAVKLQKE 693
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 707-1156 1.22e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 47.73  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  707 REEKQVPIAPLHLSLEDRSERlSTHELTSLLEKELEQSQKEASDLLEQNRLLQdqlrVALGREQSARegyVLQTEVAtsp 786
Cdd:TIGR00606  724 RRDEMLGLAPGRQSIIDLKEK-EIPELRNKLQKVNRDIQRLKNDIEEQETLLG----TIMPEEESAK---VCLTDVT--- 792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  787 sgawqrlhrVNQDLQSELEAQCRRqelITQQIQTLKHSygeakDAIRHHEAEIQTLQTrlgnaaaelaiKEQALAKLKGE 866
Cdd:TIGR00606  793 ---------IMERFQMELKDVERK---IAQQAAKLQGS-----DLDRTVQQVNQEKQE-----------KQHELDTVVSK 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  867 LKMEQGKVREQLEEWQHskamlsgqLRASEQKLRStearllEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGT 946
Cdd:TIGR00606  845 IELNRKLIQDQQEQIQH--------LKSKTNELKS------EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  947 SEQAQRLMEKKLKRNYTLLLESCEQEKQAL--LQNLKEVEDKASAYEDQLQGHVQQ-VEALQKEKLSETCKGSEQVHKLE 1023
Cdd:TIGR00606  911 DSPLETFLEKDQQEKEELISSKETSNKKAQdkVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECE 990

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1024 EELEAREASIRQLAQHVQSLHDERDLIKHQF---------QELMERVATSDGDVAELQekLRGKEVDYQNLEHSHHRVSV 1094
Cdd:TIGR00606  991 KHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlrkrenelKEVEEELKQHLKEMGQMQ--VLQMKQEHQKLEENIDLIKR 1068

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081929 1095 QLQSVRTLLREKEEELKHIKethERVLEKKDQDLNEALVKMIALGSSLEETEIKLQEKEECL 1156
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFK---KELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTL 1127
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 67-142 1.36e-04

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 43.07  E-value: 1.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081929   67 RKWQRRFFILYEHGLLRY-ALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWL 142
Cdd:cd13276     13 KTWRRRWFVLKQGKLFWFkEPDVTPYSKPRGVIDLSKCLTVKSAEDATNKENAFELSTPEETFYFIADNEKEKEEWI 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1824-2305 1.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1824 ALKEEYEELLhKQKSEYQKVITLIEKENTELKAKVSQmdhqqrcLQEAENKHSESMFALQGRYE--EEIRCMVEQLSHTE 1901
Cdd:PRK03918   176 RRIERLEKFI-KRTENIEELIKEKEKELEEVLREINE-------ISSELPELREELEKLEKEVKelEELKEEIEELEKEL 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1902 NTLQAErsrvLSQLDASVKDRQAMEQHHVQQMKMLEDrfqlKVRELqavhqEELRALQEHYIwSLRGALSLY--QPSHPD 1979
Cdd:PRK03918   248 ESLEGS----KRKLEEKIRELEERIEELKKEIEELEE----KVKEL-----KELKEKAEEYI-KLSEFYEEYldELREIE 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1980 SSLAPGPSEPRAVPAAKDEAESMSglrERIQELEAQMGVMREELGhkELEGDVAALQEKYQRDFESLKATCERGFAAMEE 2059
Cdd:PRK03918   314 KRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRLE--ELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2060 ThQKKIEDLQRQH---QRELEKLREEKDRLLAEEtAATISAIEAMKNAHR----------EEMERELEKSQRSQISSINS 2126
Cdd:PRK03918   389 L-EKELEELEKAKeeiEEEISKITARIGELKKEI-KELKKAIEELKKAKGkcpvcgreltEEHRKELLEEYTAELKRIEK 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2127 DIEALRRQyLEELQSVQRELEVLSEQYSQkclenahlaqaLEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLL 2206
Cdd:PRK03918   467 ELKEIEEK-ERKLRKELRELEKVLKKESE-----------LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2207 TGDGGgESTGLpLTQGKDAYELEVLLRVKESEIQYLKQEISSLK-----------DELQTALRDKKYASDKY---KDIYT 2272
Cdd:PRK03918   535 IKLKG-EIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEYlelKDAEK 612

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1907081929 2273 ELSIAKAKadcdISRLKEQLKAATEALGEKSPE 2305
Cdd:PRK03918   613 ELEREEKE----LKKLEEELDKAFEELAETEKR 641
PTZ00121 PTZ00121
MAEBL; Provisional
 1795-2199 1.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1795 EYEKELRFYKKACQEAKGASGQKRAQAVGALKEE---YEELlhKQKSEYQKVITLIEKENTELKAKVSQMdhqqRCLQEA 1871
Cdd:PTZ00121  1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkADEA--KKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEA 1508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1872 ENKHSESMFALQGRYEEEIRcMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRElqavh 1951
Cdd:PTZ00121  1509 KKKADEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK----- 1582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1952 QEELRALQEHYIwslrgalslyqpshpdsslapgpsepravpaakdeaesmsglrERIQELEAQMGVMREELGHKELEGD 2031
Cdd:PTZ00121  1583 AEEAKKAEEARI-------------------------------------------EEVMKLYEEEKKMKAEEAKKAEEAK 1619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2032 VAALQEKYQrdfESLKATCERgFAAMEETHQKKIEDLQRQHqrELEKLREEKDRLLAEETAATISAIEAMKNAHREEMER 2111
Cdd:PTZ00121  1620 IKAEELKKA---EEEKKKVEQ-LKKKEAEEKKKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2112 ELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQEL 2191
Cdd:PTZ00121  1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773


                   ....*...
gi 1907081929 2192 NNRLAAEI 2199
Cdd:PTZ00121  1774 RKEKEAVI 1781
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
897-1100 1.53e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  897 QKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQ-QLGTSEQAQRLMEKKLKRNyTLLLESCEQEKQA 975
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL-RAELARLEAELER 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  976 LLQNLKEVEDKASAYEDQLQGH-VQQVEALQKEklsetckgseqVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQF 1054
Cdd:COG4913    314 LEARLDALREELDELEAQIRGNgGDRLEQLERE-----------IERLERELEERERRRARLEALLAALGLPLPASAEEF 382

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1055 QEL----MERVATSDGDVAELQEKLRGKEVDYQNLEHSHHRVSVQLQSVR 1100
Cdd:COG4913    383 AALraeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1888-2300 1.58e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.14  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1888 EEIRCMVEQLSHTENTLQAERSRvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALQEHyIWSLR 1967
Cdd:pfam12128  237 MKIRPEFTKLQQEFNTLESAELR-LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGE-LSAAD 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1968 GALSLYQpSHPDSSlapgpsEPRAVPAAKDEAESMSGLRERIQELEAQMGVMREElgHKELEGDVAALQEKYQRDFESLK 2047
Cdd:pfam12128  315 AAVAKDR-SELEAL------EDQHGAFLDADIETAAADQEQLPSWQSELENLEER--LKALTGKHQDVTAKYNRRRSKIK 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2048 ATCERGFAAMEEthqkkiedlqrqhqrELEKLREEKDRLLAEETAatisAIEAMKNAHREEME------RELEKSQRSQI 2121
Cdd:pfam12128  386 EQNNRDIAGIKD---------------KLAKIREARDRQLAVAED----DLQALESELREQLEagklefNEEEYRLKSRL 446

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2122 SSIN---------SDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELN 2192
Cdd:pfam12128  447 GELKlrlnqatatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2193 NRLAAEITRLRTLLTGDGGG--ESTG----------------LPLTQGKDAYEL-EVLLRVKESEIQ---YLKQEISSLK 2250
Cdd:pfam12128  527 LQLFPQAGTLLHFLRKEAPDweQSIGkvispellhrtdldpeVWDGSVGGELNLyGVKLDLKRIDVPewaASEEELRERL 606

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907081929 2251 DELQTALRDkkyASDKYKDIYTELSIAKA---KADCDISRLKEQLKAATEALG 2300
Cdd:pfam12128  607 DKAEEALQS---AREKQAAAEEQLVQANGeleKASREETFARTALKNARLDLR 656
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
792-966 1.88e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  792 RLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKE--QALAKLKGELKM 869
Cdd:COG4717     64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAE 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  870 EQGKVRE------QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQE-----LRDLETQQALQRDRQKEVQRLQECIA 938
Cdd:COG4717    144 LPERLEEleerleELRELEEELEELEAELAELQEELEELLEQLSLATEEelqdlAEELEELQQRLAELEEELEEAQEELE 223

                          170       180       190
                   ....*....|....*....|....*....|
gi 1907081929  939 ELSQQLGTSEQAQRL--MEKKLKRNYTLLL 966
Cdd:COG4717    224 ELEEELEQLENELEAaaLEERLKEARLLLL 253
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1994-2151 1.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1994 AAKDEAES-MSGLRERIQELEAQM---GVMREElghkELEGDVAALQEKY---QRDFESLKATCER-GFAAmeETHQKKI 2065
Cdd:COG4913    309 AELERLEArLDALREELDELEAQIrgnGGDRLE----QLEREIERLERELeerERRRARLEALLAAlGLPL--PASAEEF 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2066 EDLQRQHQRELEKLREEKDRLLAEETAAtISAIEAMKNAHREeMERELEkSQRSQISSINSDIEALRRQYLEELQSVQRE 2145
Cdd:COG4913    383 AALRAEAAALLEALEEELEALEEALAEA-EAALRDLRRELRE-LEAEIA-SLERRKSNIPARLLALRDALAEALGLDEAE 459


                   ....*.
gi 1907081929 2146 LEVLSE 2151
Cdd:COG4913    460 LPFVGE 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
721-1151 2.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  721 LEDRSERLSTheltslLEKELEQSQKEASDLLEQNRLLQD--QLRVALGREQSAREGYVLQtevatspsgawqrlhrvnq 798
Cdd:PRK03918   333 LEEKEERLEE------LKKKLKELEKRLEELEERHELYEEakAKKEELERLKKRLTGLTPE------------------- 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  799 DLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNA---AAELAikEQALAKLKGELKMEQGKVR 875
Cdd:PRK03918   388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcGRELT--EEHRKELLEEYTAELKRIE 465

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  876 EQLEEWQHSKAMLSGQLRASEQKLR--STEARLLEKTQELRDLETQqaLQRDRQKEVQRLQECIAELSQQLGTSEQAQRL 953
Cdd:PRK03918   466 KELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  954 MEKKLKRnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEalqkEKLSETCKGSEQVHKLEEELEAREASI 1033
Cdd:PRK03918   544 LKKELEK-----LEELKKKLAELEKKLDELEEELAELLKELEELGFESV----EELEERLKELEPFYNEYLELKDAEKEL 614

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1034 RQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAEL-----QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEE 1108
Cdd:PRK03918   615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1907081929 1109 ELKHIKETHERVLEKKD--QDLNEALVKMIALGSSLEETEIKLQE 1151
Cdd:PRK03918   695 TLEKLKEELEEREKAKKelEKLEKALERVEELREKVKKYKALLKE 739
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1860-2278 2.18e-04

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: 46.65  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1860 QMDHQQRCLQEAENKHSESMFAlqgRYEEEIRCMVEQLSHTeNTLQAERSRVLSQldaSVKDRQAmeqhHVQQMKMLEDR 1939
Cdd:pfam15921   60 ELDSPRKIIAYPGKEHIERVLE---EYSHQVKDLQRRLNES-NELHEKQKFYLRQ---SVIDLQT----KLQEMQMERDA 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1940 FqLKVRELQAVHQEELRALQEHYIWSLRGALSLYQPSHPDSSLAPGP------------SEPRAVPAAKDEAESmsglrE 2007
Cdd:pfam15921  129 M-ADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQlrkmmlshegvlQEIRSILVDFEEASG-----K 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2008 RIQELEAQMGVMREELGH------KELEGDVAALQEK---YQRDFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEK 2078
Cdd:pfam15921  203 KIYEHDSMSTMHFRSLGSaiskilRELDTEISYLKGRifpVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITG 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2079 LREEKdrllaeetaatiSAIEAMKNAHREEME--RELEKSQRSQISSINSDIEALRRQYLEELQSVQRELE-VLSEQYSQ 2155
Cdd:pfam15921  283 LTEKA------------SSARSQANSIQSQLEiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdKIEELEKQ 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2156 KCLENAHLAQAlEAERQALRQ----CQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYELEVl 2231
Cdd:pfam15921  351 LVLANSELTEA-RTERDQFSQesgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEV- 428

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1907081929 2232 lRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAK 2278
Cdd:pfam15921  429 -QRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2001-2358 2.25e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2001 SMSGLRERIQELEAQMGVMREELghKELEGDVAALQE------------KYQRDFESLKATCERGFAAMEETH---QKKI 2065
Cdd:PRK03918   253 SKRKLEEKIRELEERIEELKKEI--EELEEKVKELKElkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEIngiEERI 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2066 EDLQRQHQR--ELEKLREEKDRLLA--EETAATISAIEAMKnahrEEMERELEKSQRSQISSINSDIEALRRQYLEelqs 2141
Cdd:PRK03918   331 KELEEKEERleELKKKLKELEKRLEelEERHELYEEAKAKK----EELERLKKRLTGLTPEKLEKELEELEKAKEE---- 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2142 VQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNA-HNQELNNRLAAEITRLRTLLTGDGGGESTGLplt 2220
Cdd:PRK03918   403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEeHRKELLEEYTAELKRIEKELKEIEEKERKLR--- 479

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2221 qgKDAYELEVLLRvKESEIQYLKQ---EISSLKDELqtalrdKKYASDKYKDIYTELSIAKAKAD---CDISRLKEQLKA 2294
Cdd:PRK03918   480 --KELRELEKVLK-KESELIKLKElaeQLKELEEKL------KKYNLEELEKKAEEYEKLKEKLIklkGEIKSLKKELEK 550

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081929 2295 ATEALGEKSpegttvsgydimKSKSNPDFLKKDRSCVTRQLRNIRSKSLKEgltVQERLKLFES 2358
Cdd:PRK03918   551 LEELKKKLA------------ELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELEP 599
PH_3BP2 cd13308
SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes ...
 66-145 2.36e-04

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270118  Cd Length: 113  Bit Score: 42.78  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   66 SRKWQRRFFILYEHGLLrYALDEMPTTlPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEH---FIRAETKEIISGWL 142
Cdd:cd13308     25 LQNWQLRYVIIHQGCVY-YYKNDQSAK-PKGVFSLNGYNRRAAEERTSKLKFVFKIIHLSPDHrtwYFAAKSEDEMSEWM 102


                   ...
gi 1907081929  143 EML 145
Cdd:cd13308    103 EYI 105
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 737-1158 2.73e-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: 46.50  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSA-------REGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCR 809
Cdd:TIGR00618  227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqlrariEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  810 RQ-ELITQQIQTLKHSYGEAKDAIRHHEAEIQTL--QTRLGN---AAAELAIKEQALAKLKGELKMEQGKVREQLEEWQH 883
Cdd:TIGR00618  307 QQaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIeeQRRLLQtlhSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  884 SKAMLSGQLRASEQ---KLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKR 960
Cdd:TIGR00618  387 QKTTLTQKLQSLCKeldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  961 NYTLLLEScEQEKQALLQNLKEVEDKASAYEDQLQG------------HVQQVEALQKEKLSETCKGSEQVHKLEEELEA 1028
Cdd:TIGR00618  467 SLKEREQQ-LQTKEQIHLQETRKKAVVLARLLELQEepcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1029 REASIRQ-LAQHVQSLHDERDLIKHQFQELmervATSDGDVAELQEKLRGKEVDYQNL--EHSHHRVSVQLQSVRTLLRE 1105
Cdd:TIGR00618  546 DVYHQLTsERKQRASLKEQMQEIQQSFSIL----TQCDNRSKEDIPNLQNITVRLQDLteKLSEAEDMLACEQHALLRKL 621

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907081929 1106 KEEELKHIKETHERVLEKKDQDLNEALVKmialgsslEETEIKLQEKEECLRR 1158
Cdd:TIGR00618  622 QPEQDLQDVRLHLQQCSQELALKLTALHA--------LQLTLTQERVREHALS 666
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 693-995 2.74e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  693 EIEQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLEK--ELEQSQKEASDLLEQNRLLQDQLRVALGREQ 770
Cdd:TIGR02169  699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLE 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  771 SAREGyvLQTEVATSPsgaWQRLhrvnQDLQSELEAQCRRQELITQQIQ------TLKHSYgeAKDAIRHHEAEIQTLQT 844
Cdd:TIGR02169  779 EALND--LEARLSHSR---IPEI----QAELSKLEEEVSRIEARLREIEqklnrlTLEKEY--LEKEIQELQEQRIDLKE 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  845 RLGNAAAELAIKEQALAKLKGELKMEQGKVRE---QLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQA 921
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081929  922 LQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRnytllLESCEQEKQALLQNLKEVEDKASAYEDQLQ 995
Cdd:TIGR02169  928 ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE-----IRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 462-540 2.78e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 42.15  E-value: 2.78e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929   462 RKRPDLLNFKKGW---------LTKQYEDGQAADLDGEINLSTC---YDVTEYPVQRNYGFQIHTKEGE-FTLSAMTSGI 528
Cdd:smart00233   10 KSGGGKKSWKKRYfvlfnstllYYKSKKDKKSYKPKGSIDLSGCtvrEAPDPDSSKKPHCFEIKTSDRKtLLLQAESEEE 89

                            90
                    ....*....|..
gi 1907081929   529 RRNWIQTIMKHV 540
Cdd:smart00233   90 REKWVEALRKAI 101
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2074-2341 3.16e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2074 RELEKLREEKDRLLAEEtaatiSAIEAMKnahrEEMERELEKSQRsQISSINSDIEALRRQyLEELQSVQRELEVLSEQY 2153
Cdd:PRK03918   172 KEIKRRIERLEKFIKRT-----ENIEELI----KEKEKELEEVLR-EINEISSELPELREE-LEKLEKEVKELEELKEEI 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2154 SQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRlAAEITRLRTLltgdgggestglpltqgKDAY-ELEVLL 2232
Cdd:PRK03918   241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEK-----------------AEEYiKLSEFY 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2233 RVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIyTELSIAKAKADCDISRLKEQLKAATEA---LGEKSPEGTTV 2309
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEERHELYEEAkakKEELERLKKRL 381

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907081929 2310 SGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSK 2341
Cdd:PRK03918   382 TGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1996-2176 4.04e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 4.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1996 KDEAESMSGLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFESLKATCERgfaameethqkkIEDLQRQHQrE 2075
Cdd:COG4717     91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER------------LEELEERLE-E 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2076 LEKLREEKDRLLAEetaatisaiEAMKNAHREEMERELEKSQRSQISSINSDIEALR---RQYLEELQSVQRELEVLSEQ 2152
Cdd:COG4717    158 LRELEEELEELEAE---------LAELQEELEELLEQLSLATEEELQDLAEELEELQqrlAELEEELEEAQEELEELEEE 228

                          170       180
                   ....*....|....*....|....
gi 1907081929 2153 YSQkcLENAHLAQALEAERQALRQ 2176
Cdd:COG4717    229 LEQ--LENELEAAALEERLKEARL 250
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 853-1109 4.77e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  853 LAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQrdrQKEVQR 932
Cdd:COG4942     11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  933 LQECIAELSQQLGTSEQ--AQRL--MEKKLKRNYTLLLESCEqekqallqNLKEVEDKASAYEDQLQGHVQQVEALqkek 1008
Cdd:COG4942     88 LEKEIAELRAELEAQKEelAELLraLYRLGRQPPLALLLSPE--------DFLDAVRRLQYLKYLAPARREQAEEL---- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1009 lsetckgseqvhklEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHS 1088
Cdd:COG4942    156 --------------RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                          250       260
                   ....*....|....*....|.
gi 1907081929 1089 HHRVSVQLQSVRTLLREKEEE 1109
Cdd:COG4942    222 AEELEALIARLEAEAAAAAER 242
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1994-2290 5.03e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.33  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1994 AAKDEAESMSGLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFESLKATCE-----RGFAAMEETHQKKIEDL 2068
Cdd:COG5185    269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeskRETETGIQNLTAEIEQG 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2069 QRQHQRELEKLREEKDRLLAEETAATisaieamknahREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEV 2148
Cdd:COG5185    349 QESLTENLEAIKEEIENIVGEVELSK-----------SSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKA 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2149 LSEQysqkclenahlaqaLEAERQALRQCQRENQElnahNQELNNRLAAEITRLRTLLTGDGggeSTGLPLTQGKDAYEL 2228
Cdd:COG5185    418 ADRQ--------------IEELQRQIEQATSSNEE----VSKLLNELISELNKVMREADEES---QSRLEEAYDEINRSV 476

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081929 2229 EVLLRVKESEIQYLKQEISSLKDELQT--ALRDKKYASDKYKDIYTELSIAKAKADCDISRLKE 2290
Cdd:COG5185    477 RSKKEDLNEELTQIESRVSTLKATLEKlrAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1795-2086 5.16e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1795 EYEKELRFYKKACQEAKGASGQKRaQAVGALKEEYEELLHKQKSEYQKvITLIEKENTELKAKVSQMDHQQRCLQEAENK 1874
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELS-RQISALRKDLARLEAEVEQLEER-IAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1875 HSESMFALQGRYEEeircMVEQLSHTENTLQAERSRvLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVREL--QAVHQ 1952
Cdd:TIGR02168  780 AEAEIEELEAQIEQ----LKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIeeLSEDI 854

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1953 EELRALQEHYiWSLRGALSlyqpSHPDSSLAPGPSEPRAVPAAKDEAESMSG----LRERIQELEAQMGVMREELGH--- 2025
Cdd:TIGR02168  855 ESLAAEIEEL-EELIEELE----SELEALLNERASLEEALALLRSELEELSEelreLESKRSELRRELEELREKLAQlel 929

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081929 2026 --KELEGDVAALQEK----YQRDFEslkatcergfaaMEETHQKKIEDLQRQHQRELEKLREEKDRL 2086
Cdd:TIGR02168  930 rlEGLEVRIDNLQERlseeYSLTLE------------EAEALENKIEDDEEEARRRLKRLENKIKEL 984
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 686-1111 5.22e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.48  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  686 KTQNVHVEIEQRWHQVETT--PLREEKQVPIAPLHLSLEDRSERLstHELTSLLEKELEQSQKEASDLLEQNRLLQDQLR 763
Cdd:pfam05483  180 ETRQVYMDLNNNIEKMILAfeELRVQAENARLEMHFKLKEDHEKI--QHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  764 VALGREQSAREGyVLQTEVATSpsgawqrlhrvnqdLQSE-LEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTL 842
Cdd:pfam05483  258 DLTFLLEESRDK-ANQLEEKTK--------------LQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  843 QTRLGNAAAELAIKEQALAKLKGELKMeqgkvreQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELR----DLET 918
Cdd:pfam05483  323 TKTICQLTEEKEAQMEELNKAKAAHSF-------VVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQkkssELEE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  919 QQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKklkrnytllLESCEQEKQALLQNL-KEVED---KASAYEDQL 994
Cdd:pfam05483  396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE---------LKGKEQELIFLLQAReKEIHDleiQLTAIKTSE 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  995 QGHVQQVEALQKEKLSETCKGSEqvhkleeeleareasirqLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEK 1074
Cdd:pfam05483  467 EHYLKEVEDLKTELEKEKLKNIE------------------LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1907081929 1075 LRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELK 1111
Cdd:pfam05483  529 EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK 565
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 737-1156 5.29e-04

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: 45.49  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNrllQDQLRVALGREQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRRQelITQ 816
Cdd:pfam15921  247 LEALKSESQNKIELLLQQH---QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ--LSD 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  817 QIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQAlaklKGELKMEQGKVREQLEEwqhskamLSGQLRASE 896
Cdd:pfam15921  322 LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNLDDQLQK-------LLADLHKRE 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  897 QKLRstearlLEKTQELR--DLETQQA-----LQR---DRQKEVQRLQ--------ECIAELSQQLGTSEQAQRLMEKkl 958
Cdd:pfam15921  391 KELS------LEKEQNKRlwDRDTGNSitidhLRReldDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEK-- 462

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  959 krnYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSE--QVHKLEEELEAREASIRQL 1036
Cdd:pfam15921  463 ---VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNE 539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1037 AQHVQSLHDERDLIKHQFQELMERVatsdgdvaelqEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLrEKE--------E 1108
Cdd:pfam15921  540 GDHLRNVQTECEALKLQMAEKDKVI-----------EILRQQIENMTQLVGQHGRTAGAMQVEKAQL-EKEindrrlelQ 607

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907081929 1109 ELKHIKETHE---RVLEKKDQDLNEALVKMIALGSS-LEETEIKLQEKEECL 1156
Cdd:pfam15921  608 EFKILKDKKDakiRELEARVSDLELEKVKLVNAGSErLRAVKDIKQERDQLL 659
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 702-1117 5.61e-04

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: 45.49  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  702 ETTPLREEKQVPIAPLH-----LSLE-DRSERLSTHELTSL-----LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQ 770
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHkrekeLSLEkEQNKRLWDRDTGNSitidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQM 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  771 SAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGnaa 850
Cdd:pfam15921  451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD--- 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  851 aelaIKEQALAKLKGE---------------LKM-EQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLlEKTQELR 914
Cdd:pfam15921  528 ----LKLQELQHLKNEgdhlrnvqtecealkLQMaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL-EKEINDR 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  915 DLETQQ--ALQRDRQKEVQRLQECIAEL-----------SQQLGT-----SEQAQRLMEKKLKRNYtllLESCEQEKQAL 976
Cdd:pfam15921  603 RLELQEfkILKDKKDAKIRELEARVSDLelekvklvnagSERLRAvkdikQERDQLLNEVKTSRNE---LNSLSEDYEVL 679

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  977 LQNLKEVEDKASAYEDQLQGHVQ--QVEALQKEKLSETCKGSE------------QVHKLEEELEAREASIRQLAQHVQS 1042
Cdd:pfam15921  680 KRNFRNKSEEMETTTNKLKMQLKsaQSELEQTRNTLKSMEGSDghamkvamgmqkQITAKRGQIDALQSKIQFLEEAMTN 759

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1043 LHDERDLIKHQFQEL---MERVATSDGDVAELQEKLRGKEVDYQ----NLEHSHHRVSVQLQSVRTLLREKEEELKHIKE 1115
Cdd:pfam15921  760 ANKEKHFLKEEKNKLsqeLSTVATEKNKMAGELEVLRSQERRLKekvaNMEVALDKASLQFAECQDIIQRQEQESVRLKL 839


                   ..
gi 1907081929 1116 TH 1117
Cdd:pfam15921  840 QH 841
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1699-2176 5.62e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1699 QEPLQALHQSPEVLAAIQDELAQQLREKASILEEISAALPVLPPTEPLGGCQRLLRMSQHlSYESCLEGLGQYSSLLVQd 1778
Cdd:COG4717     87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE-RLEELEERLEELRELEEE- 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1779 aiiqaqvcyaacriRLEYEKELRFYKKACQEAKGASGQKRAQAVGALKEEYEELlHKQKSEYQKVITLIEKENTELKAKV 1858
Cdd:COG4717    165 --------------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL-QQRLAELEEELEEAQEELEELEEEL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1859 SQMDHQQRCLQEAENKHSESMFALqgryeeeIRCMVEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLED 1938
Cdd:COG4717    230 EQLENELEAAALEERLKEARLLLL-------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1939 RFQlkvrelQAVHQEELRALQEHYIWSLRGALSLyqpshpdsslaPGPSEPRAVPAAKDEAESMSGLRERIQELEAQMgv 2018
Cdd:COG4717    303 EAE------ELQALPALEELEEEELEELLAALGL-----------PPDLSPEELLELLDRIEELQELLREAEELEEEL-- 363

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2019 mreelghkelegDVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQR--QHQRELEKLREEKDRLLAEETAATIS 2096
Cdd:COG4717    364 ------------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEELE 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2097 AIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQY-----LEELQSVQRELEVLSEQYSQKCLenahLAQALEAER 2171
Cdd:COG4717    432 EELEELEEELEELEEELEE-LREELAELEAELEQLEEDGelaelLQELEELKAELRELAEEWAALKL----ALELLEEAR 506


                   ....*
gi 1907081929 2172 QALRQ 2176
Cdd:COG4717    507 EEYRE 511
46 PHA02562
endonuclease subunit; Provisional
 793-1018 7.19e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.62  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  793 LHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKlkgeLKMEQG 872
Cdd:PHA02562   190 IDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK----LNTAAA 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  873 KVREQLEEWQHSKAMLS--GQLRASEQKLRSTEARLLEKTQELRDLETQ-QALQRDRQKEVQRLQEcIAELSQQLgtseq 949
Cdd:PHA02562   266 KIKSKIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSlEKLDTAIDELEEIMDE-FNEQSKKL----- 339

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081929  950 aqrlmeKKLKRNYtlllESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKE--KLSETCKGSEQ 1018
Cdd:PHA02562   340 ------LELKNKI----STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEldKIVKTKSELVK 400
PRK09039 PRK09039
peptidoglycan -binding protein;
2056-2208 7.27e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2056 AMEETHQKKIEDLQRQHQRELEKLREEKDRL--LAEETAATISAIEAMKNAHREEM--ERELEKSQRSQISSINSDIEAL 2131
Cdd:PRK09039    70 SLERQGNQDLQDSVANLRASLSAAEAERSRLqaLLAELAGAGAAAEGRAGELAQELdsEKQVSARALAQVELLNQQIAAL 149

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081929 2132 RRQyleeLQSVQRELEVlSEQYSQkclenahlaqalEAERQALRQCQRENQELNAHNQELnNRLAAE-ITRLRTLLTG 2208
Cdd:PRK09039   150 RRQ----LAALEAALDA-SEKRDR------------ESQAKIADLGRRLNVALAQRVQEL-NRYRSEfFGRLREILGD 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 793-1158 7.54e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.81  E-value: 7.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  793 LHRVNQDLQSELEAQCRRQELITQQIQT--------------LKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAE------ 852
Cdd:pfam10174  245 LERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevykshskfMKNKIDQLKQELSKKESELLALQTKLETLTNQnsdckq 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  853 --------LAIKEQALAKLKGE-----LKMEQ-----GKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELR 914
Cdd:pfam10174  325 hievlkesLTAKEQRAAILQTEvdalrLRLEEkesflNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  915 DLETQqalQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDkasaYEDQL 994
Cdd:pfam10174  405 NLQEQ---LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELES----LKKEN 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  995 QGHVQQVEALQKEKLSETCKGS---EQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDvAEL 1071
Cdd:pfam10174  478 KDLKEKVSALQPELTEKESSLIdlkEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTN-PEI 556

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1072 QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEElKHIKETHERVLEK------KDQDLNEALVKMialgSSLEET 1145
Cdd:pfam10174  557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE-KNDKDKKIAELESltlrqmKEQNKKVANIKH----GQQEMK 631

                          410
                   ....*....|...
gi 1907081929 1146 EIKLQEKEECLRR 1158
Cdd:pfam10174  632 KKGAQLLEEARRR 644
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1994-2256 7.67e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1994 AAKDEAEsmsgLRERIQELEAQMGVMREELGHKELEGDVAALQ-----------EKYQRDFESLKATCERGFAAMEETHQ 2062
Cdd:PRK02224   197 EEKEEKD----LHERLNGLESELAELDEEIERYEEQREQARETrdeadevleehEERREELETLEAEIEDLRETIAETER 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2063 KK--IEDLQRQHQRELEKLREEKDRLLAEE--TAATISAIEAMKN---AHREEMERELEKsQRSQISSINSDIEALRrqy 2135
Cdd:PRK02224   273 EReeLAEEVRDLRERLEELEEERDDLLAEAglDDADAEAVEARREeleDRDEELRDRLEE-CRVAAQAHNEEAESLR--- 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2136 leelqsvqRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAaeitrlrtlltgdgggest 2215
Cdd:PRK02224   349 --------EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG------------------- 401

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907081929 2216 GLPLTQGKDAYELEVLLrvkeSEIQYLKQEISSLKDELQTA 2256
Cdd:PRK02224   402 DAPVDLGNAEDFLEELR----EERDELREREAELEATLRTA 438
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1818-2280 8.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1818 RAQAVGALKEEYEELLHKQKSEYQKVITLIEKENTELKAKVSQMDHQQRcLQEAENKHSESMFALQGRYEE---EIRCMV 1894
Cdd:COG4717     44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEElreELEKLE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1895 EQLSHTENTLQAER-SRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQlKVRELQAVHQEELRALQEHYIWSLRGALSLY 1973
Cdd:COG4717    123 KLLQLLPLYQELEAlEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEEL 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1974 QpshpdsslapgpsepravpAAKDEAESmsgLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFESLKATCER- 2052
Cdd:COG4717    202 E-------------------ELQQRLAE---LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALl 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2053 GFAAMEETHQKKIEDLQRQHQ-----RELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSD 2127
Cdd:COG4717    260 ALLGLGGSLLSLILTIAGVLFlvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2128 IEALRRqyLEELQSVQRELEVLSEQYSQKCLE---NAHLAQALEAERQALRQCQRENQELnahnQELNNRLAAEITRLRT 2204
Cdd:COG4717    340 LELLDR--IEELQELLREAEELEEELQLEELEqeiAALLAEAGVEDEEELRAALEQAEEY----QELKEELEELEEQLEE 413

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929 2205 LLTGDGGGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYAsdkykDIYTELSIAKAK 2280
Cdd:COG4717    414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA-----ELLQELEELKAE 484
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 849-1124 9.13e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 9.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  849 AAAELAIKEQALAK---LKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRD 925
Cdd:TIGR00618  182 ALMEFAKKKSLHGKaelLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  926 RQKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQ 1005
Cdd:TIGR00618  262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1006 KEKLSETCKGSEQVH------------KLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSD-------- 1065
Cdd:TIGR00618  342 EQRRLLQTLHSQEIHirdahevatsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtsafrd 421

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081929 1066 --GDVAEL-------QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKK 1124
Cdd:TIGR00618  422 lqGQLAHAkkqqelqQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1999-2199 9.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 9.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1999 AESMSGLRERIQELEAQMGVMR--------------EELGHKELEGDVAALQEKYQR------DFESLK---ATCERGFA 2055
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQerrealqrlaeyswDEIDVASAEREIAELEAELERldassdDLAALEeqlEELEAELE 702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2056 AMEEtHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAI------------EAMKNAHREEMERELEKSQ---RSQ 2120
Cdd:COG4913    703 ELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelralleerfaAALGDAVERELRENLEERIdalRAR 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2121 ISSINSDIEALRRQYLEE----LQSVQRELEVLSEqYSQKC--LENAHLAQALEAERQALRQCQRENQElnahnqELNNR 2194
Cdd:COG4913    782 LNRAEEELERAMRAFNREwpaeTADLDADLESLPE-YLALLdrLEEDGLPEYEERFKELLNENSIEFVA------DLLSK 854


                   ....*
gi 1907081929 2195 LAAEI 2199
Cdd:COG4913    855 LRRAI 859
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 735-904 9.79e-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: 9.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  735 SLLEKELEQSQKEAS----DLLEQNRLLQDQLRVALGREQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEAQCRR 810
Cdd:COG4942     79 AALEAELAELEKEIAelraELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  811 QELITQQIQTLKhsygEAKDAIRHHEAEIQTLQTRLgnaAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSG 890
Cdd:COG4942    159 LAELAALRAELE----AERAELEALLAELEEERAAL---EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231

                          170
                   ....*....|....
gi 1907081929  891 QLRASEQKLRSTEA 904
Cdd:COG4942    232 LEAEAAAAAERTPA 245
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2115-2322 9.99e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 9.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2115 KSQRSQISSINSDIEALRrqylEELQSVQRELEVLSEQYSQKcleNAHLAQALEAERQALRQCQRENQELNAHNQELNNR 2194
Cdd:COG3883     19 QAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2195 LAA------EITRLRTLLTGDGGGE--------STGLPLTQG--KDAYELEVLLRVKESEIQYLKQEISSLKDELQTALR 2258
Cdd:COG3883     92 ARAlyrsggSVSYLDVLLGSESFSDfldrlsalSKIADADADllEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081929 2259 DKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPEGTTVSGYDIMKSKSNPD 2322
Cdd:COG3883    172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
COG5022 COG5022
Myosin heavy chain [General function prediction only];
797-1263 1.33e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.30  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  797 NQDLQSELEAQCRRQELITQQI----QTLKHSYGEAkdAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKmEQG 872
Cdd:COG5022    819 IIKLQKTIKREKKLRETEEVEFslkaEVLIQKFGRS--LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVK-SIS 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  873 KVREQLEEWQHSKAMLSGQLRASEQ---KLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLgtseq 949
Cdd:COG5022    896 SLKLVNLELESEIIELKKSLSSDLIenlEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETS----- 970

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  950 aqrlmekklkrnytlllesceQEKQALLqnlkeveDKASAYEDQLQGHVQQVEALQKEkLSETCKGSEQVHKLEEELEAR 1029
Cdd:COG5022    971 ---------------------EEYEDLL-------KKSTILVREGNKANSELKNFKKE-LAELSKQYGALQESTKQLKEL 1021

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1030 EASIRQLAQHVQSLHDERDlIKHQFQELMERVATSDGDVAELQEKLrgKEVDYQN-LEHSHHRVSVQLQSVRTLlrEKEE 1108
Cdd:COG5022   1022 PVEVAELQSASKIISSEST-ELSILKPLQKLKGLLLLENNQLQARY--KALKLRReNSLLDDKQLYQLESTENL--LKTI 1096

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1109 ELKHIKETHERVLEKKdqdlnEALVKMIALGSSLEEteikLQEKEECLRRFVSDSPkDAKEPLSTTEPTEEGSGILPLGS 1188
Cdd:COG5022   1097 NVKDLEVTNRNLVKPA-----NVLQFIVAQMIKLNL----LQEISKFLSQLVNTLE-PVFQKLSVLQLELDGLFWEANLE 1166

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1189 VTRVFPGFpHSQPEDEDPSAGLGEEGSSGS-------------LSREENTILPKSADMPE--REG-HLQSTSKSDPGapI 1252
Cdd:COG5022   1167 ALPSPPPF-AALSEKRLYQSALYDEKSKLSssevndlkneliaLFSKIFSGWPRGDKLKKliSEGwVPTEYSTSLKG--F 1243

                          490
                   ....*....|.
gi 1907081929 1253 KRPRIRFSTIQ 1263
Cdd:COG5022   1244 NNLNKKFDTPA 1254
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1999-2184 1.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1999 AESMSGLRERIQELEAQMGVMREELGHKELEGDVAALQekyQRDFESLKATCERgfaAMEETHQKkiedlQRQHQRELEK 2078
Cdd:PRK02224   278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR---REELEDRDEELRD---RLEECRVA-----AQAHNEEAES 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2079 LREEKDRLlaEETAATISAIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQY---LEELQSVQRELEVLSEQysq 2155
Cdd:PRK02224   347 LREDADDL--EERAEELREEAAELESELEEAREAVED-RREEIEELEEEIEELRERFgdaPVDLGNAEDFLEELREE--- 420

                          170       180       190
                   ....*....|....*....|....*....|
gi 1907081929 2156 kcLENAHLAQA-LEAERQALRQCQRENQEL 2184
Cdd:PRK02224   421 --RDELREREAeLEATLRTARERVEEAEAL 448
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1809-2196 1.33e-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: 44.01  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1809 EAKGASGQKRAQAVGALKEEYEELLHKQKSEYQKVITLIEKEN------TELKAkVSQMDHQQRCLQEAENKHSESMFAL 1882
Cdd:pfam01576  562 EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqmlAEEKA-ISARYAEERDRAEAEAREKETRALS 640

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1883 QGRYEEEIRCMVEQLSHTENTLQAERSRVLSQLDASVKD-------RQAMEQhHVQQMKM----LEDrfqlkvrELQAVH 1951
Cdd:pfam01576  641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhelersKRALEQ-QVEEMKTqleeLED-------ELQATE 712

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1952 QEELR------ALQEHYIWSLRgalslyqpshpdsslapgpsepravpaAKDEA--ESMSGLRERIQELEAQMGVMREEl 2023
Cdd:pfam01576  713 DAKLRlevnmqALKAQFERDLQ---------------------------ARDEQgeEKRRQLVKQVRELEAELEDERKQ- 764

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2024 ghkelEGDVAALQEKYQRDFESLKATCERGFAAMEET--HQKKIEDLQRQHQRELEKLREEKDRLLA--EETAATISAIE 2099
Cdd:pfam01576  765 -----RAQAVAAKKKLELDLKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASRDEILAqsKESEKKLKNLE 839

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2100 A-----------------MKNAHREEMERELEK--SQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLEN 2160
Cdd:pfam01576  840 AellqlqedlaaserarrQAQQERDELADEIASgaSGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQV 919

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1907081929 2161 AHLAQALEAERQALRQCQRENQELNAHNQELNNRLA 2196
Cdd:pfam01576  920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ 955
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1658-2293 1.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1658 ERVIQQILetlrhptgREDQVQTSWDQnpLGEILRPgTDGSQEPLQALHQSPEvlaAIQDELAQQLREKASILEEISAAL 1737
Cdd:PRK03918   148 EKVVRQIL--------GLDDYENAYKN--LGEVIKE-IKRRIERLEKFIKRTE---NIEELIKEKEKELEEVLREINEIS 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1738 PVLPPT-EPLGGCQRLLRmsqhlSYESCLEGLgqySSLLVQDAIIQAQVCYAACRIRlEYEKELRFYKKACQEAKgaSGQ 1816
Cdd:PRK03918   214 SELPELrEELEKLEKEVK-----ELEELKEEI---EELEKELESLEGSKRKLEEKIR-ELEERIEELKKEIEELE--EKV 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1817 KRAQAVGALKEEYEElLHKQKSEYQKVITLIEKENTELKAKVSQMdhqQRCLQEAENKHSEsMFALQGRyEEEIRCMVEQ 1896
Cdd:PRK03918   283 KELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGI---EERIKELEEKEER-LEELKKK-LKELEKRLEE 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1897 LSHTENTLQAERsRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEELRALqEHYIWSLRGALSLYQPS 1976
Cdd:PRK03918   357 LEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAIEELKKA 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1977 HPDSSL--APGPSEPRAVPAAKDEAEsMSGLRERIQELEAQMGVMREELghKELEGDVaalqeKYQRDFESLKATCERGF 2054
Cdd:PRK03918   435 KGKCPVcgRELTEEHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKEL--RELEKVL-----KKESELIKLKELAEQLK 506

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2055 AAMEETHQKKIEDLQRQhQRELEKLREEKDRLLAE--ETAATISAIEAMKNaHREEMERELEKSQRsQISSINSDIEALR 2132
Cdd:PRK03918   507 ELEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKGEikSLKKELEKLEELKK-KLAELEKKLDELEE-ELAELLKELEELG 583

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2133 RQYLEELQSVQRELEVLSEQYsqkcLENAHLAQALEAERQALRQCQRENQELNAHNQELNNR---LAAEITRLRTLLTGD 2209
Cdd:PRK03918   584 FESVEELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRleeLRKELEELEKKYSEE 659

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2210 GGGESTGLPLtqgkdayELEVLLRVKESEIQYLKqeisSLKDELQTALRDKKYASDKYKDIYTEL-SIAKAKAdcDISRL 2288
Cdd:PRK03918   660 EYEELREEYL-------ELSRELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELeKLEKALE--RVEEL 726


                   ....*
gi 1907081929 2289 KEQLK 2293
Cdd:PRK03918   727 REKVK 731
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1999-2168 1.46e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1999 AESMSGLRERIQELEAQMGVMREELghKELEGDVAALQEKYQRDFESLKATCErgfAAMEETHQKKIEDLQRQHQRELEK 2078
Cdd:COG3206    211 SEEAKLLLQQLSELESQLAEARAEL--AEAEARLAALRAQLGSGPDALPELLQ---SPVIQQLRAQLAELEAELAELSAR 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2079 LREEKDRL--LAEETAATISAIEAMKNAHREEMERELEkSQRSQISSINSDIEALRRQYLE------ELQSVQRELEVLS 2150
Cdd:COG3206    286 YTPNHPDViaLRAQIAALRAQLQQEAQRILASLEAELE-ALQAREASLQAQLAQLEARLAElpeleaELRRLEREVEVAR 364

                          170       180
                   ....*....|....*....|
gi 1907081929 2151 EQYSQ--KCLENAHLAQALE 2168
Cdd:COG3206    365 ELYESllQRLEEARLAEALT 384
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 737-1000 1.49e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 44.02  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLRvalgREQSAREGYVLQTEVATSpsgAWQRL-------HRVNQDLQSELEAQCR 809
Cdd:PRK10246   535 LEKEVKKLGEEGAALRGQLDALTKQLQ----RDESEAQSLRQEEQALTQ---QWQAVcaslnitLQPQDDIQPWLDAQEE 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  810 RQELITQ--QIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIK------EQA-LAKLKGELKMEQGKVREQ--L 878
Cdd:PRK10246   608 HERQLRLlsQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTlpqedeEASwLATRQQEAQSWQQRQNELtaL 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  879 EEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRD----LETQ-QALQRDRQKEVQRLQECIAELSQQLGTSEQAQR- 952
Cdd:PRK10246   688 QNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEqclsLHSQlQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQq 767

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907081929  953 ------LMEKKLKRnytlllesCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQ 1000
Cdd:PRK10246   768 aflaalLDEETLTQ--------LEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1791-2184 1.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1791 RIRLEYEKELRFYKKACQEAKGASGQKRAQAvgALKEEYEELLHKQKSEYQKVITLIEKENTELKAKVSQMDHQQRcLQE 1870
Cdd:COG1196    380 ELEELAEELLEALRAAAELAAQLEELEEAEE--ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE-LEE 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1871 AENKHSESMFALQGRYEEEIrcmvEQLSHTENTLQAERSRVLSQLDASVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAV 1950
Cdd:COG1196    457 EEEALLELLAELLEEAALLE----AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1951 HQEELRALQEhyiwsLRGALSLYQPSHPDSSLAPGPSEPRAVPAAKDEAESMSGLRERIQELEAQMGVMREElGHKELEG 2030
Cdd:COG1196    533 EAAYEAALEA-----ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA-AVDLVAS 606

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2031 DVAALQEKYQRDFESL------KATCERGFAAMEETHQKKIE---DLQRQHQRELEKLREEKDRLLAEETAATISAIEAM 2101
Cdd:COG1196    607 DLREADARYYVLGDTLlgrtlvAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2102 KNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAE----------R 2171
Cdd:COG1196    687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdleelE 766

                          410
                   ....*....|...
gi 1907081929 2172 QALRQCQRENQEL 2184
Cdd:COG1196    767 RELERLEREIEAL 779
mukB PRK04863
chromosome partition protein MukB;
1808-2205 1.74e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1808 QEAKGASGQ-KRAQA-VGALKEEYEE------LLHKQKSEYQKVITLIEKENTELKAKVSqmDHQQRcLQEAENKhsesm 1879
Cdd:PRK04863   341 QTALRQQEKiERYQAdLEELEERLEEqnevveEADEQQEENEARAEAAEEEVDELKSQLA--DYQQA-LDVQQTR----- 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1880 fALQGRyeeeircmveqlshteNTLQA-ERSRVLSQLDA----SVKDRQAMEQHHVQQMKMLEDRFQLKVRELQAVHQEE 1954
Cdd:PRK04863   413 -AIQYQ----------------QAVQAlERAKQLCGLPDltadNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1955 LRALQehyiwSLRgalslyqpshpdsSLAPGPSEPRAVPAAKD---EAESMSGLRERIQELEAQmgvmreelgHKELEGD 2031
Cdd:PRK04863   476 EQAYQ-----LVR-------------KIAGEVSRSEAWDVAREllrRLREQRHLAEQLQQLRMR---------LSELEQR 528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2032 VAAlqekyQRDFESLKATCERGFAAMEEThQKKIEDLQRQHQRELEKLREEKDRLlaeetaatisaieamkNAHREEMER 2111
Cdd:PRK04863   529 LRQ-----QQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEA----------------RERRMALRQ 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2112 ELEKsqrsqissINSDIEALRRQYLEELQSvQRELEVLSEQY------SQKCLEnaHLAQALEAERQALR---QCQRENQ 2182
Cdd:PRK04863   587 QLEQ--------LQARIQRLAARAPAWLAA-QDALARLREQSgeefedSQDVTE--YMQQLLERERELTVerdELAARKQ 655

                          410       420
                   ....*....|....*....|...
gi 1907081929 2183 ELNAHNQELNNRLAAEITRLRTL 2205
Cdd:PRK04863   656 ALDEEIERLSQPGGSEDPRLNAL 678
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 791-945 1.81e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  791 QRLHRVNQDLQSELEA-QCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQtRLGNAAAELAIKEQALAKLKGELKM 869
Cdd:TIGR00618  725 NASSSLGSDLAAREDAlNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA-ELSHLAAEIQFFNRLREEDTHLLKT 803

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929  870 EQGKVREQLEewqHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLG 945
Cdd:TIGR00618  804 LEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2069-2341 1.89e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2069 QRQHQRELEKLREEKDRLLAEEtAATISAIEAMKNaHREEMERELEKSQRsQISSINSDIEALrrqyLEELQSVQRELEV 2148
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKREL-SSLQSELRRIEN-RLDELSQELSDASR-KIGEIEKEIEQL----EQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2149 LSEQYSQkclenahLAQALEAERQALRQCQRENQELnahnQELNNRLAAEITRLRTLLTGDGGGESTGLPLTQGKDAYEL 2228
Cdd:TIGR02169  742 LEEDLSS-------LEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2229 EVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKadcdISRLKEQLKAATEALgekspegtt 2308
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK----KEELEEELEELEAAL--------- 877

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907081929 2309 vsgYDIMKSKSNpdfLKKDRSCVTRQLRNIRSK 2341
Cdd:TIGR02169  878 ---RDLESRLGD---LKKERDELEAQLRELERK 904
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 2062-2205 1.95e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2062 QKKIEDLQRQHQRELEKLREEKDRL--LAEETAATISA--------------IEAMKNAH-REEMER--ELEkSQRSQIS 2122
Cdd:pfam10174  400 QKKIENLQEQLRDKDKQLAGLKERVksLQTDSSNTDTAlttleealsekeriIERLKEQReREDRERleELE-SLKKENK 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2123 SINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQR-ENQELNAHNQELNNRLAAEIT- 2200
Cdd:pfam10174  479 DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKlENQLKKAHNAEEAVRTNPEINd 558


                   ....*
gi 1907081929 2201 RLRTL 2205
Cdd:pfam10174  559 RIRLL 563
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 2004-2292 2.46e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2004 GLRERIQELEAQMGVMREElgHKELEGDVAALQE----------KYQRDFESLKATceRGFAAMEETHQKKIEDLQRQHQ 2073
Cdd:COG3096    372 EAAEQLAEAEARLEAAEEE--VDSLKSQLADYQQaldvqqtraiQYQQAVQALEKA--RALCGLPDLTPENAEDYLAAFR 447

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2074 RELEKLREEkdrLLAEETAATISaiEAMKNAHREEME------------------RELEKSQRSQiSSINSDIEALRRQY 2135
Cdd:COG3096    448 AKEQQATEE---VLELEQKLSVA--DAARRQFEKAYElvckiageversqawqtaRELLRRYRSQ-QALAQRLQQLRAQL 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2136 --LEELQSVQRELEVLSEQYSQ---KCLENA----HLAQALEAERQAL-----------RQCQRENQELNAHNQELNNRL 2195
Cdd:COG3096    522 aeLEQRLRQQQNAERLLEEFCQrigQQLDAAeeleELLAELEAQLEELeeqaaeaveqrSELRQQLEQLRARIKELAARA 601

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2196 AAEIT---RLRTLltgdggGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRdkkyasdkykdiyt 2272
Cdd:COG3096    602 PAWLAaqdALERL------REQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIE-------------- 661

                          330       340
                   ....*....|....*....|
gi 1907081929 2273 ELSIAKAKADCDISRLKEQL 2292
Cdd:COG3096    662 RLSQPGGAEDPRLLALAERL 681
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1997-2261 2.51e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1997 DEAESMSGLRERIQELEAQMGVMREELG-----HKELEGDVAALQ------EKYQRDFESLKATcERGFAAME-ETHQKK 2064
Cdd:TIGR02168  162 EEAAGISKYKERRKETERKLERTRENLDrlediLNELERQLKSLErqaekaERYKELKAELREL-ELALLVLRlEELREE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2065 IEDLQRQhQRELEKLREEKDRLLAEETAAtisaIEAMKNAHREeMERELEKSQRS--QISSINSDIEALRRQYLEELQSV 2142
Cdd:TIGR02168  241 LEELQEE-LKEAEEELEELTAELQELEEK----LEELRLEVSE-LEEEIEELQKElyALANEISRLEQQKQILRERLANL 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2143 QRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRtlltgdgggestglpltqg 2222
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE------------------- 375

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1907081929 2223 kdayELEVLLRVKESEIQYLKQEISSLKDELQTALRDKK 2261
Cdd:TIGR02168  376 ----ELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
PRK11281 PRK11281
mechanosensitive channel MscK;
798-1006 2.66e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.36  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  798 QDLQSELEAQCRRQELITQQ---IQTLKHSYgEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKG--------- 865
Cdd:PRK11281    39 ADVQAQLDALNKQKLLEAEDklvQQDLEQTL-ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdndeetret 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  866 -------ELKMEQGKVREQLEEWQHSKAMLSGQL--------RASEQkLRSTEARLLEKTQELRDLETQQALQRDRQKev 930
Cdd:PRK11281   118 lstlslrQLESRLAQTLDQLQNAQNDLAEYNSQLvslqtqpeRAQAA-LYANSQRLQQIRNLLKGGKVGGKALRPSQR-- 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  931 QRLQECIAELSQQ-------LGTSEQAQRLMEKklKRNYTLLLESCEQEKQALLQNLkeVEDKasaYEDQLQGHVQQVEA 1003
Cdd:PRK11281   195 VLLQAEQALLNAQndlqrksLEGNTQLQDLLQK--QRDYLTARIQRLEHQLQLLQEA--INSK---RLTLSEKTVQEAQS 267


                   ...
gi 1907081929 1004 LQK 1006
Cdd:PRK11281   268 QDE 270
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 2000-2176 2.66e-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: 41.10  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2000 ESMSGLRERIQELEAQMGVMREELgHKELEGDVAALQEKYQRDFESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKL 2079
Cdd:pfam01442    4 DSLDELSTYAEELQEQLGPVAQEL-VDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEEL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2080 ReekdrllaEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLE 2159
Cdd:pfam01442   83 R--------KRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQ 154

                          170
                   ....*....|....*...
gi 1907081929 2160 NA-HLAQALEAERQALRQ 2176
Cdd:pfam01442  155 RLqELREKLEPQAEDLRE 172
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
891-1061 3.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  891 QLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTSEQAQRLMEKK---LKRNYTL--- 964
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerlDASSDDLaal 690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  965 --LLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQS 1042
Cdd:COG4913    691 eeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770

                          170
                   ....*....|....*....
gi 1907081929 1043 LHDERDLIKHQFQELMERV 1061
Cdd:COG4913    771 LEERIDALRARLNRAEEEL 789
PRK09039 PRK09039
peptidoglycan -binding protein;
838-980 3.42e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  838 EIQTLQTRLGNAAAELAIKEQALA---KLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELr 914
Cdd:PRK09039    47 EISGKDSALDRLNSQIAELADLLSlerQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL- 125

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081929  915 DLETQQALQRDRQkeVQRLQECIAELSQQLGTSEQAQRLMEKKlkrnytlllescEQEKQALLQNL 980
Cdd:PRK09039   126 DSEKQVSARALAQ--VELLNQQIAALRRQLAALEAALDASEKR------------DRESQAKIADL 177
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
 69-145 3.77e-03

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 38.84  E-value: 3.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081929   69 WQRRFFILYEHgLLRYALDEMPTTlPQGTINMNQCTDVvDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEML 145
Cdd:cd10573     19 WKTRWFVLRRN-ELKYFKTRGDTK-PIRVLDLRECSSV-QRDYSQGKVNCFCLVFPERTFYMYANTEEEADEWVKLL 92
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1816-2256 3.95e-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: 42.47  E-value: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1816 QKRAQAVGALKEEYEELlHKQKSEYQKVITLIEKENTELKAKV-----SQMDHQQR------CLQEAENKHSESMFALQG 1884
Cdd:pfam01576  352 QKHTQALEELTEQLEQA-KRNKANLEKAKQALESENAELQAELrtlqqAKQDSEHKrkklegQLQELQARLSESERQRAE 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1885 RYEEEIRCMVEQLSHTENTLQAER-----SRVLSQLDASVKDRQAMEQHHVQQMKMLEDRfqlkVRELQavhqEELRALQ 1959
Cdd:pfam01576  431 LAEKLSKLQSELESVSSLLNEAEGkniklSKDVSSLESQLQDTQELLQEETRQKLNLSTR----LRQLE----DERNSLQ 502

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1960 EHYiwslrgalslyqpshpdsslapgpsepravpaaKDEAESMSGLRERIQELEAQMGVMREELghKELEGDVAALQE-- 2037
Cdd:pfam01576  503 EQL---------------------------------EEEEEAKRNVERQLSTLQAQLSDMKKKL--EEDAGTLEALEEgk 547

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2038 -KYQRDFESLKATCERGFAAMEETH------QKKIEDL------QRQHQRELEKLREEKDRLLAEETAATISAIEAMKNA 2104
Cdd:pfam01576  548 kRLQRELEALTQQLEEKAAAYDKLEktknrlQQELDDLlvdldhQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRA 627

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2105 HREEMERELEksqrsqissinsdiealrrqyleelqsvqreleVLSeqysqkclenahLAQALEAERQALRQCQRENQEL 2184
Cdd:pfam01576  628 EAEAREKETR---------------------------------ALS------------LARALEEALEAKEELERTNKQL 662

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081929 2185 NAHNQELNNRLAAeitrlrtlltgdgggestglpltQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTA 2256
Cdd:pfam01576  663 RAEMEDLVSSKDD-----------------------VGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 2008-2152 4.53e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2008 RIQELEAQMGVMREELghKELEGDVAALQ---EKYQRDFESLKATCERgFAAMEETHQKKIEDLQRQH-----QRELEKL 2079
Cdd:COG1579     18 ELDRLEHRLKELPAEL--AELEDELAALEarlEAAKTELEDLEKEIKR-LELEIEEVEARIKKYEEQLgnvrnNKEYEAL 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081929 2080 REEKDRLLAEETAATISAIEAMKNahREEMERELEKSQrSQISSINSDIEALRRQYLEELQSVQRELEVLSEQ 2152
Cdd:COG1579     95 QKEIESLKRRISDLEDEILELMER--IEELEEELAELE-AELAELEAELEEKKAELDEELAELEAELEELEAE 164
PTZ00121 PTZ00121
MAEBL; Provisional
 851-1128 4.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  851 AELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMlsgQLRASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEV 930
Cdd:PTZ00121  1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM---ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  931 QRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQLQGHVQQVEALQKEKLS 1010
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1011 ETCKGSEQVHKLEEELEAREASIRQlaqhvqslHDERDLIKhqfQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHH 1090
Cdd:PTZ00121  1699 EEAKKAEELKKKEAEEKKKAEELKK--------AEEENKIK---AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907081929 1091 RVSVQLQSVRTLLreKEEELKHIKETHERVLEKKDQDL 1128
Cdd:PTZ00121  1768 KKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDI 1803
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 737-1011 4.95e-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: 42.25  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVA--TSPSGAWQRlhrvnqdlQSELEAQCRRQELI 814
Cdd:COG3096    439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeVERSQAWQT--------ARELLRRYRSQQAL 510

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  815 TQQIQTLKHSYGEA-KDAIRHHEAEiqtlqtrlgnaaaelaikeqalaKLKGELKMEQGKVREQLEEWQHSKAMLSGQLR 893
Cdd:COG3096    511 AQRLQQLRAQLAELeQRLRQQQNAE-----------------------RLLEEFCQRIGQQLDAAEELEELLAELEAQLE 567

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  894 ASEQKLRSTEARLLEKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLGTS--------EQAQRLMEKklKRNYTLL 965
Cdd:COG3096    568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAladsqevtAAMQQLLER--EREATVE 645

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907081929  966 LESCEQEKQALLQNLKEVEDKASAYEDQLqghVQQVEALQKEKLSE 1011
Cdd:COG3096    646 RDELAARKQALESQIERLSQPGGAEDPRL---LALAERLGGVLLSE 688
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 828-1009 5.50e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 42.05  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  828 AKDAIRHHEAEIQTLQTRlGNAAAELAIKEQALAKLKGELKmeqgkVREQLEEwqhskamlsgQLRASEQKLRSTEARLL 907
Cdd:pfam09731  292 AHREIDQLSKKLAELKKR-EEKHIERALEKQKEELDKLAEE-----LSARLEE----------VRAADEAQLRLEFERER 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  908 EKTQELRDLETQQALQRDRQKEVQRLQECIAELSQQLgtseqaQRLMEKKLKrnytlllESCEQEKQALLQNLKEVEDKA 987
Cdd:pfam09731  356 EEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIEL------QREFLQDIK-------EKVEEERAGRLLKLNELLANL 422

                          170       180
                   ....*....|....*....|...
gi 1907081929  988 SAYEDQLQGHVQQV-EALQKEKL 1009
Cdd:pfam09731  423 KGLEKATSSHSEVEdENRKAQQL 445
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
 1995-2140 5.62e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 41.09  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1995 AKDEAESMSGLRERIQELEAQMGVMREELG----HKELEGDVAALQ-EKYQRDFESLKatcergfaameETHQKKIEDLQ 2069
Cdd:pfam15397   76 EEKEESKLNKLEQQLEQLNAKIQKTQEELNflstYKDKEYPVKAVQiANLVRQLQQLK-----------DSQQDELDELE 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081929 2070 RQHQRELEKL----REEKDRLL---AEETAATISAIEAMKNAHREEMERELEKsQRSQISSINSDIEALRRQyLEELQ 2140
Cdd:pfam15397  145 EMRRMVLESLsrkiQKKKEKILsslAEKTLSPYQESLLQKTRDNQVMLKEIEQ-FREFIDELEEEIPKLKAE-VQQLQ 220
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
737-902 5.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGY---VLQTEVAtspsgAWQ-RLHRVNQD------LQSELEA 806
Cdd:COG4913    622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIA-----ELEaELERLDASsddlaaLEEQLEE 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  807 QCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKA 886
Cdd:COG4913    697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776

                          170
                   ....*....|....*.
gi 1907081929  887 MLSGQLRASEQKLRST 902
Cdd:COG4913    777 ALRARLNRAEEELERA 792
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1716-2301 5.80e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1716 QDELAQQLREKASILEEISAALPVLPPTEPLGgcqrLLRMSQHLSYESCLEGLGQYSSLLVQDAIIQAQVCYAACRIRLE 1795
Cdd:TIGR00618  151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLA----LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEK 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1796 YEKELRFYKKACQEAKGASGQKRAQAVGALKEEYE-ELLHKQKSEYQKVITLIEKENTELK------------AKVSQMD 1862
Cdd:TIGR00618  227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLlKQLRARIEELRAQEAVLEETQERINrarkaaplaahiKAVTQIE 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1863 HQ-QRCLQEAENKHSESMFALQGRYE-EEIRCMVEQLSHTENTLQAERSRVLSQLDA-----SVKDRQAMEQHHV----Q 1931
Cdd:TIGR00618  307 QQaQRIHTELQSKMRSRAKLLMKRAAhVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVatsirEISCQQHTLTQHIhtlqQ 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1932 QMKMLEDRFQLKVRELQAVHQE---------ELRALQEHYIwSLRGALSLYQPSHPDSSLAPGPSEPRAVPAAKDEAESM 2002
Cdd:TIGR00618  387 QKTTLTQKLQSLCKELDILQREqatidtrtsAFRDLQGQLA-HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2003 SGLRERIQELEAQMGVMREELGHKELEGDVAALQEKYQRDFE--SLKATCERGFAAMEETHQKK---IEDLQRQHQRELE 2077
Cdd:TIGR00618  466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCgsCIHPNPARQDIDNPGPLTRRmqrGEQTYAQLETSEE 545

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2078 KLREEKDRLLaeETAATISAieamknahREEMERELEKSQRSQISSINSDIEALRRqyleELQSVQRELEVLSEQYSQKC 2157
Cdd:TIGR00618  546 DVYHQLTSER--KQRASLKE--------QMQEIQQSFSILTQCDNRSKEDIPNLQN----ITVRLQDLTEKLSEAEDMLA 611

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2158 LENAHL------AQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTgdgggestglplTQGKDAYELEVL 2231
Cdd:TIGR00618  612 CEQHALlrklqpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI------------RVLPKELLASRQ 679

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081929 2232 LrvKESEIQYLKQEISSLKDEL---QTALRDKKYASDKYKDIYTELSIAKAKAdcdISRLKEQLKAATEALGE 2301
Cdd:TIGR00618  680 L--ALQKMQSEKEQLTYWKEMLaqcQTLLRELETHIEEYDREFNEIENASSSL---GSDLAAREDALNQSLKE 747
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
836-1154 5.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 5.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  836 EAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRD 915
Cdd:COG4372     12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  916 LETQQALQRDR----QKEVQRLQECIAELSQQLGTSEQAQRLMEKKLKRNYTLLLEScEQEKQALLQNLKEVEDKASAYE 991
Cdd:COG4372     92 AQAELAQAQEEleslQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-EEELKELEEQLESLQEELAALE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  992 DQLQGHVQQVEALQKEKLSETCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAEL 1071
Cdd:COG4372    171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1072 QEKLRGKEVDYQNLEHSHHRVSVQLQSVRTLLREKEEELKHIKETHERVLEKKDQDLNEALVKMIALGSSLEETEIKLQE 1151
Cdd:COG4372    251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330


                   ...
gi 1907081929 1152 KEE 1154
Cdd:COG4372    331 ALA 333
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 737-912 6.46e-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: 6.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  737 LEKELEQSQKEASDLLEQNRLLQ---DQLRVALGR------EQSAREGYVLQTEVATSPSGAWQRLHRVNQDLQSELEaq 807
Cdd:COG3883     56 LQAELEALQAEIDKLQAEIAEAEaeiEERREELGEraralyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADAD-- 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  808 crrqelITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNAAAELAIKEQALAKLKGELKMEQGKVREQLEEWQHSKAM 887
Cdd:COG3883    134 ------LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207

                          170       180
                   ....*....|....*....|....*
gi 1907081929  888 LSGQLRASEQKLRSTEARLLEKTQE 912
Cdd:COG3883    208 AEAAAAAAAAAAAAAAAAAAAAAAA 232
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 2094-2207 7.58e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 2094 TISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQA 2173
Cdd:pfam09787   43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907081929 2174 LRQCQRENQELNAHNQELNNRLAAEITRLRTLLT 2207
Cdd:pfam09787  123 LRYLEEELRRSKATLQSRIKDREAEIEKLRNQLT 156
Yuri_gagarin pfam15934
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
 695-923 8.67e-03

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 40.33  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  695 EQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLstheltslleKELEQSQKEASDLLEQNRLlqdqlrvalgreqsARE 774
Cdd:pfam15934   45 EQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQI----------KQLQSMITGYSDISENNRL--------------KEE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  775 GYVLQTEVATspsgawqrLHRVNQDLQSELEAQCRRQELITQQIQTLKHSYGEAKDAIRHHEAEIQTLQTRLGNaaaela 854
Cdd:pfam15934  101 IHDLKQKNCV--------QARVVRKMGLELKGQEEQRVELCDKYESLLGSFEEQCQELKRANRRVQSLQTRLSQ------ 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081929  855 ikeqaLAKLKGELKMEQGKVREQLEEWQHSKAMLSGQLRASEQKLRSTEARLLEKTQELRDLETQQALQ 923
Cdd:pfam15934  167 -----VEKLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIEKSRTLIRNMQSHLQLE 230
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 1990-2086 8.91e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 40.80  E-value: 8.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  1990 RAVPaaKDEAESMSGLRERIQELEAQMGVMREELGHKELEGDV-AALQEKYQRDFESLKATCERGFAAM--EETHQKKIE 2066
Cdd:smart00435  269 RTVS--KTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLkRKLKSKFERDNEKLDAEVKEKKKEKkkEEKKKKQIE 346

                            90       100
                    ....*....|....*....|
gi 1907081929  2067 DLQRQHQReLEKLREEKDRL 2086
Cdd:smart00435  347 RLEERIEK-LEVQATDKEEN 365
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 932-1144 9.14e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 9.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929  932 RLQECIAELSQQLGTSEQAQRLMEKKlKRNYTLLLESCEQEKQALLQNLKEVEDKASAYEDQlqghVQQVEALQKEKLSE 1011
Cdd:pfam07888   35 RLEECLQERAELLQAQEAANRQREKE-KERYKRDREQWERQRRELESRVAELKEELRQSREK----HEELEEKYKELSAS 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081929 1012 TCKGSEQVHKLEEELEAREASIRQLAQHVQSLHDERDLIKHQFQELMERVATSDGDVAELQEKLRGKEVDYQNLEHSHHR 1091
Cdd:pfam07888  110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907081929 1092 VSVQLQSVRTLLREKEEELKHIKEThervLEKKDQDLNEALVKMIALGSSLEE 1144
Cdd:pfam07888  190 LSKEFQELRNSLAQRDTQVLQLQDT----ITTLTQKLTTAHRKEAENEALLEE 238
 
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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