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Conserved domains on  [gi|564335600|ref|XP_006232125|]
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ankycorbin isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-248 2.30e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666  195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                 ....*...
gi 564335600 241 ISQDADLK 248
Cdd:COG0666  275 LLLLAAAL 282
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
607-867 1.32e-11

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 68.94  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   607 MVDELNKQVSELsqlyREAQAELEDYRK-RKSLEDATEYIHRAEHErlmhlsnlsrtKAEESLSDMRSQYSKVLNELTQL 685
Cdd:TIGR02169  192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELLKEKE-----------ALERQKEAIERQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   686 KQLVDAHKENSVSITEHLEVITtlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyEKLQASL 765
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA-------EERLAKL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   766 ESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKL 845
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
                          250       260
                   ....*....|....*....|..
gi 564335600   846 EEDKDEKINEMTKEVLKLKEAL 867
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAI 429
MukB super family cl34550
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
401-694 8.05e-05

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


The actual alignment was detected with superfamily member COG3096:

Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.87  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtDTTCLNNTEISENGS---DLSQKLKDTQSK---YEEAMKEVLSVQK 474
Cdd:COG3096   349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  475 QMKLGLLSHESADG---DSRLREVRVTDEdVDALKQDLQRAlEESKRDKARVQELETKLV-EKEKAEATKPSSEVCEEMR 550
Cdd:COG3096   428 LCGLPDLTPENAEDylaAFRAKEQQATEE-VLELEQKLSVA-DAARRQFEKAYELVCKIAgEVERSQAWQTARELLRRYR 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  551 nSYCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 626
Cdd:COG3096   506 -SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600  627 AELEDYR-KRKSLEdATEYIHRAEHERLMHLSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKE 694
Cdd:COG3096   585 QQLEQLRaRIKELA-ARAPAWLAAQDALERLREQSGEALADSqeVTAAMQQLLEREREATVERDELAARKQ 654
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-248 2.30e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666  195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                 ....*...
gi 564335600 241 ISQDADLK 248
Cdd:COG0666  275 LLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 3.11e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   90 LHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKsPINLKDlDGNIPLLVAIQNGHSEACH 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 564335600  170 FLLDHGADVNSRD 182
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
23-239 3.48e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 3.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLKVMVTHGVDVTAQDSSGHSALHIAA--K 95
Cdd:PHA03100  39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  96 NGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGS--LQAVQVLCEHKSPINLKDldgNIPLLvaiqnghseachflLD 173
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYL--------------LS 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600 174 HGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
607-867 1.32e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 68.94  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   607 MVDELNKQVSELsqlyREAQAELEDYRK-RKSLEDATEYIHRAEHErlmhlsnlsrtKAEESLSDMRSQYSKVLNELTQL 685
Cdd:TIGR02169  192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELLKEKE-----------ALERQKEAIERQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   686 KQLVDAHKENSVSITEHLEVITtlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyEKLQASL 765
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA-------EERLAKL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   766 ESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKL 845
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
                          250       260
                   ....*....|....*....|..
gi 564335600   846 EEDKDEKINEMTKEVLKLKEAL 867
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAI 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
608-888 2.06e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 608 VDELNKQVSELS------QLYREAQAELEDYRKR---KSLEDATEYIHRAEHERlmHLSNLSRTKAEESLSDMRSQYSKV 678
Cdd:COG1196  195 LGELERQLEPLErqaekaERYRELKEELKELEAElllLKLRELEAELEELEAEL--EELEAELEELEAELAELEAELEEL 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 679 LNELTQLKQLVDAHKEN----SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvp 754
Cdd:COG1196  273 RLELEELELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA--- 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 755 kasyEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAG 834
Cdd:COG1196  350 ----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564335600 835 LKrcsETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLE 888
Cdd:COG1196  426 LE---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
401-867 6.62e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.24  E-value: 6.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKqlqdELQSQRTDTTCLNNTEISENGS--DLSQKLKDTQSKYEEAMKEVLSVQKQMK- 477
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKe 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 478 ----------LGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE-KEKAEATKPSSEVC 546
Cdd:PRK03918 285 lkelkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELY 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 547 EEMRnsycSVIENMNKEKAFL----FEKYQQAQEEIMKLKDTLksqmpQEAPDDSGDMKETMNRMVDELNKQVSEL---- 618
Cdd:PRK03918 365 EEAK----AKKEELERLKKRLtgltPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELkkak 435
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 619 ---------------SQLYREAQAELEDYRKR-KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSD----MRSQYSKV 678
Cdd:PRK03918 436 gkcpvcgrelteehrKELLEEYTAELKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeLEEKLKKY 515
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 679 -LNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-------------- 743
Cdd:PRK03918 516 nLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlk 595
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 744 -------EKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQakREKENIQTLLKSKEQ 816
Cdd:PRK03918 596 elepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSR 673
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564335600 817 EVTELVQKFQRAQEELAGLKRCSEtssKLEEDKdEKINEMTKEVLKLKEAL 867
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKAL 720
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
88-223 1.49e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.03  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  88 SALHIAAKNGHPEYIKKLLQYKSpaesVDN-----LGKTALHYAAAQGSLQAVQVLCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPS----CDLfqrgaLGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 158 VAIQNGHSEACHFLLDHGADVNS----------RDKN----GRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALY 223
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
51-275 5.14e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   51 SEGKTAFHLAAAKGHVECLKVMVTHG--VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVdnlGKTALHyAAA 128
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AIS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  129 QGSLQAVQVLCEHKSPINLKDLD--------------GNIPLLVAIQNGHSEACHFLLDHGADVNSRDK----------- 183
Cdd:TIGR00870  91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvd 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  184 ---NGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKL-SENA--------GIQSLLLSKISQDADLktpt 251
Cdd:TIGR00870 171 sfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMeNEFKaeyeelscQMYNFALSLLDKLRDS---- 246
                         250       260
                  ....*....|....*....|....
gi 564335600  252 kaKQLSDVSSPRSITSTPLSGKES 275
Cdd:TIGR00870 247 --KELEVILNHQGLTPLKLAAKEG 268
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
403-864 5.90e-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: 53.58  E-value: 5.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   403 QLQDTLHDLQKRLETSEAEKKQLQ-------------DELQSQRTDttclNNTEISENGSDLSQKLKDTQSKYEEAMKEV 469
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitiDHLRRELDD----RNMEVQRLEALLKAMKSECQGQMERQMAAI 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   470 LSvqKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELEtKLVEKEKAEATKPSSEVCEEM 549
Cdd:pfam15921  454 QG--KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKL 530
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   550 RNsycsvIENMNKEKAFLfeKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAEL 629
Cdd:pfam15921  531 QE-----LQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   630 EDYRKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVIT-T 708
Cdd:pfam15921  604 LELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrN 682
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   709 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 788
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600   789 EVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLK 864
Cdd:pfam15921  763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
184-213 6.57e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 6.57e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 564335600   184 NGRTALMLACETGSANTVEALIKKGADLNL 213
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
401-694 8.05e-05

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: 46.87  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtDTTCLNNTEISENGS---DLSQKLKDTQSK---YEEAMKEVLSVQK 474
Cdd:COG3096   349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  475 QMKLGLLSHESADG---DSRLREVRVTDEdVDALKQDLQRAlEESKRDKARVQELETKLV-EKEKAEATKPSSEVCEEMR 550
Cdd:COG3096   428 LCGLPDLTPENAEDylaAFRAKEQQATEE-VLELEQKLSVA-DAARRQFEKAYELVCKIAgEVERSQAWQTARELLRRYR 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  551 nSYCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 626
Cdd:COG3096   506 -SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600  627 AELEDYR-KRKSLEdATEYIHRAEHERLMHLSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKE 694
Cdd:COG3096   585 QQLEQLRaRIKELA-ARAPAWLAAQDALERLREQSGEALADSqeVTAAMQQLLEREREATVERDELAARKQ 654
PRK09039 PRK09039
peptidoglycan -binding protein;
402-530 1.59e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 402 QQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDtqskyeeaMKEVLSVQKQmklglL 481
Cdd:PRK09039  77 QDLQDSVANLRASLSAAEAERSRLQALL------------AELAGAGAAAEGRAGE--------LAQELDSEKQ-----V 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600 482 SHESadgdsrLREVRVTDEDVDALKQ---DLQRALEES-KRDK---ARVQELETKL 530
Cdd:PRK09039 132 SARA------LAQVELLNQQIAALRRqlaALEAALDASeKRDResqAKIADLGRRL 181
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
670-836 2.26e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.20  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 670 DMRSQYSKVLNELTQLKQLVDAhKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMS 749
Cdd:cd22656   88 TIDSYYAEILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 750 D------AMVPKASYEKLQASLESEVNALAAKLKESVKEKEKahsEVAQVRSEVSQAKRekenIQTLLKSKEQEVTELVQ 823
Cdd:cd22656  167 DlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA---LIADDEAKLAAALR----LIADLTAADTDLDNLLA 239
                        170
                 ....*....|...
gi 564335600 824 KFQRAQEELAGLK 836
Cdd:cd22656  240 LIGPAIPALEKLQ 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-653 5.50e-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: 40.81  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   314 ADQQDLLVLLQAKVASLtlhNKELQDKLQAKSPKETEADLSFQSFHSTQTDLAPSPSKSSDIPSSDAKSSPPVEhpagts 393
Cdd:TIGR02168  687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT------ 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   394 taDRDVIIQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTtclnnTEISENGSDLSQKLKDTQSKYEeamkevlsvQ 473
Cdd:TIGR02168  758 --ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAA---------N 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   474 KQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQElETKLVEKEKAEATKPSSEVCEEMRNSY 553
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   554 cSVIENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYR 623
Cdd:TIGR02168  901 -EELRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564335600   624 E----------AQAELEDYRKR---------------KSLEDATEYIHRAEHERL 653
Cdd:TIGR02168  980 KikelgpvnlaAIEEYEELKERydfltaqkedlteakETLEEAIEEIDREARERF 1034
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-248 2.30e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666   35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666  115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666  195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                 ....*...
gi 564335600 241 ISQDADLK 248
Cdd:COG0666  275 LLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-246 5.37e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 5.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVT 80
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  81 AQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 161 QNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                 ....*.
gi 564335600 241 ISQDAD 246
Cdd:COG0666  242 GADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-222 1.86e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 1.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  17 NKNDDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKN 96
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  97 GHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGA 176
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564335600 177 DVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNAL 222
Cdd:COG0666  244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-240 6.12e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 6.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  33 EKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPA 112
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 113 ESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564335600 193 CETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-189 5.65e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 5.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  12 DTNEWNKNDDRLLQ-AVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSAL 90
Cdd:COG0666  112 DVNARDKDGETPLHlAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  91 HIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF 170
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                        170
                 ....*....|....*....
gi 564335600 171 LLDHGADVNSRDKNGRTAL 189
Cdd:COG0666  271 LLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 3.11e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   90 LHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKsPINLKDlDGNIPLLVAIQNGHSEACH 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 564335600  170 FLLDHGADVNSRD 182
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
23-239 3.48e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 3.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHV-----ECLKVMVTHGVDVTAQDSSGHSALHIAA--K 95
Cdd:PHA03100  39 LYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  96 NGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGS--LQAVQVLCEHKSPINLKDldgNIPLLvaiqnghseachflLD 173
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN---RVNYL--------------LS 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600 174 HGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
123-215 1.19e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  123 LHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHgADVNSRDkNGRTALMLACETGSANTVE 202
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 564335600  203 ALIKKGADLNLVD 215
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-149 4.83e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 4.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   57 FHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPaeSVDNLGKTALHYAAAQGSLQAVQ 136
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 564335600  137 VLCEHKSPINLKD 149
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
12-215 3.91e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.71  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  12 DTNEWNKNDDRLLQAVENGDA--EKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGH 87
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  88 SALHIAAKNGHP--EYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQV--LCEHKSPINLKDLDGNIPLLVAIQNG 163
Cdd:PHA03095 189 SLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFN 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564335600 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVD 215
Cdd:PHA03095 269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1-178 1.76e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 91.08  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKSDTNEWNKN---DDRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV 77
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDpnmASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC 582
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  78 DVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESvdNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLL 157
Cdd:PLN03192 583 NVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQ 660
                        170       180
                 ....*....|....*....|.
gi 564335600 158 VAIQNGHSEACHFLLDHGADV 178
Cdd:PLN03192 661 VAMAEDHVDMVRLLIMNGADV 681
PHA03095 PHA03095
ankyrin-like protein; Provisional
27-218 1.52e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  27 VENGDAEKVASLLGKKGASATKHDSEGKTAFH--LAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGH--PEYI 102
Cdd:PHA03095  91 LYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 103 KKLLQYKSPAESVDNLGKTALHYAA--AQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACH--FLLDHGADV 178
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLvlPLLIAGISI 250
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564335600 179 NSRDKNGRTALMLAceTGSANTV--EALIKKGADLNLVDSLG 218
Cdd:PHA03095 251 NARNRYGQTPLHYA--AVFNNPRacRRLIALGADINAVSSDG 290
PHA02874 PHA02874
ankyrin repeat protein; Provisional
43-222 1.85e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  43 GASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTA 122
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 123 LHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQngHSEACHFLLDHGADVNSRDKNGRTALMLACETG-SANTV 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDII 271
                        170       180
                 ....*....|....*....|.
gi 564335600 202 EALIKKGADLNLVDSLGHNAL 222
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPI 292
PHA02875 PHA02875
ankyrin repeat protein; Provisional
38-214 1.02e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  38 LLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGV---DVTAQDssGHSALHIAAKNGHPEYIKKLLQYKSPAES 114
Cdd:PHA02875  53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDI 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 115 VDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALM-LAC 193
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAI 210
                        170       180
                 ....*....|....*....|.
gi 564335600 194 ETGSANTVEALIKKGADLNLV 214
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-108 4.15e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 4.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHgVDVTAQDsSGHSALHIAAKNGHPEYI 102
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*.
gi 564335600  103 KKLLQY 108
Cdd:pfam12796  78 KLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-240 4.84e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 4.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  156 LLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKgADLNLVDSlGHNALYYSKLSENAGIQS 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                  ....*
gi 564335600  236 LLLSK 240
Cdd:pfam12796  79 LLLEK 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
29-230 6.87e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 6.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  29 NGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVE-CLKVMVTHGVDVTAQDSSGHSALHI--AAKNGHPEYIKKL 105
Cdd:PHA03095  59 SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 106 LQYKSPAESVDNLGKTALH-YAAAQG-SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF--LLDHGADVNSR 181
Cdd:PHA03095 139 LRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAAT 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564335600 182 DKNGRTALMLACETGS--ANTVEALIKKGADLNLVDSLGHNALYYSKLSEN 230
Cdd:PHA03095 219 DMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
PHA02874 PHA02874
ankyrin repeat protein; Provisional
3-250 2.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 2.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   3 SLKAKFRKSDTNEWNKNDDR----LLQAVENGDAeKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVD 78
Cdd:PHA02874  15 EAIEKIIKNKGNCINISVDEtttpLIDAIRSGDA-KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  79 VtaqdssghSALHIAAKNGhpEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLV 158
Cdd:PHA02874  94 T--------SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 159 AIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLG----HNALYYsklseNAGIQ 234
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplHNAIIH-----NRSAI 238
                        250
                 ....*....|....*....
gi 564335600 235 SLLLSKIS---QDADLKTP 250
Cdd:PHA02874 239 ELLINNASindQDIDGSTP 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
102-246 1.02e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 102 IKKLLQYKSPAESVDNLGKTALHY---AAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEAC-HFLLDHGAD 177
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAGAD 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335600 178 VNSRDKNGRTALMlACETG---SANTVEALIKKGADLNLVDSLGHNAL--YYSKLSENAGIQSLLLSKISQDAD 246
Cdd:PHA03095 110 VNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1-179 2.16e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKS-DTNEWNKNDDRLLQAVEN-----GDAEKVASLLGKKGASATKHDSEGKTAFHLAAAK--GHVECLKVM 72
Cdd:PHA03100  48 IDVVKILLDNGaDINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  73 VTHGVDVTAQDSSGHSALHIAAKNGHPEY------------------IKKLLQYKSPAESVDNLGKTALHYAAAQGSLQA 134
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564335600 135 VQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
67-225 2.36e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  67 ECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPIN 146
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335600 147 LKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACeTGSANTVEALIKKgADLNLVDSLGHNALYYS 225
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
17-225 5.65e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.79  E-value: 5.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  17 NKNDDRLLQAVENGDAEkVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECL-KVMVTHGVDVTAQDSSGHSALHIAAK 95
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAK 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  96 NGH-PEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQ-AVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLD 173
Cdd:PHA02876 317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564335600 174 HGADVNSRDKNGRTALMLA-CETGSANTVEALIKKGADLNLVDSLGHNALYYS 225
Cdd:PHA02876 397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02876 PHA02876
ankyrin repeat protein; Provisional
31-238 4.63e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  31 DAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKS 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 111 -----------------------------PAESVDNLGKTALHYAAAQGSL-QAVQVLCEHKSPINLKDLDGNIPLLVAI 160
Cdd:PHA02876 236 ninkndlsllkairnedletslllydagfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 161 QNGH-SEACHFLLDHGADVNSRDKNGRTALMLACETG-SANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLL 238
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-106 4.85e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 4.85e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564335600   55 TAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLL 106
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
607-867 1.32e-11

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 68.94  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   607 MVDELNKQVSELsqlyREAQAELEDYRK-RKSLEDATEYIHRAEHErlmhlsnlsrtKAEESLSDMRSQYSKVLNELTQL 685
Cdd:TIGR02169  192 IIDEKRQQLERL----RREREKAERYQAlLKEKREYEGYELLKEKE-----------ALERQKEAIERQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   686 KQLVDAHKENSVSITEHLEVITtlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyEKLQASL 765
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA-------EERLAKL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   766 ESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKL 845
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
                          250       260
                   ....*....|....*....|..
gi 564335600   846 EEDKDEKINEMTKEVLKLKEAL 867
Cdd:TIGR02169  408 LDRLQEELQRLSEELADLNAAI 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
608-888 2.06e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 608 VDELNKQVSELS------QLYREAQAELEDYRKR---KSLEDATEYIHRAEHERlmHLSNLSRTKAEESLSDMRSQYSKV 678
Cdd:COG1196  195 LGELERQLEPLErqaekaERYRELKEELKELEAElllLKLRELEAELEELEAEL--EELEAELEELEAELAELEAELEEL 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 679 LNELTQLKQLVDAHKEN----SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvp 754
Cdd:COG1196  273 RLELEELELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA--- 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 755 kasyEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAG 834
Cdd:COG1196  350 ----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564335600 835 LKrcsETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLE 888
Cdd:COG1196  426 LE---EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
401-867 6.62e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 66.24  E-value: 6.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKqlqdELQSQRTDTTCLNNTEISENGS--DLSQKLKDTQSKYEEAMKEVLSVQKQMK- 477
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSkrKLEEKIRELEERIEELKKEIEELEEKVKe 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 478 ----------LGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE-KEKAEATKPSSEVC 546
Cdd:PRK03918 285 lkelkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELY 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 547 EEMRnsycSVIENMNKEKAFL----FEKYQQAQEEIMKLKDTLksqmpQEAPDDSGDMKETMNRMVDELNKQVSEL---- 618
Cdd:PRK03918 365 EEAK----AKKEELERLKKRLtgltPEKLEKELEELEKAKEEI-----EEEISKITARIGELKKEIKELKKAIEELkkak 435
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 619 ---------------SQLYREAQAELEDYRKR-KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSD----MRSQYSKV 678
Cdd:PRK03918 436 gkcpvcgrelteehrKELLEEYTAELKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeLEEKLKKY 515
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 679 -LNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-------------- 743
Cdd:PRK03918 516 nLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlk 595
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 744 -------EKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQakREKENIQTLLKSKEQ 816
Cdd:PRK03918 596 elepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSR 673
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564335600 817 EVTELVQKFQRAQEELAGLKRCSEtssKLEEDKdEKINEMTKEVLKLKEAL 867
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLE---KLKEEL-EEREKAKKELEKLEKAL 720
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
401-915 1.10e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.86  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKqmklgl 480
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKEL------------EEVLREINEISSELPELREELEKLEKEVKELEE------ 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 481 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKrdkARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIENM 560
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK---KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 561 NKEKAFLFEKYQQAQEEIMKLkdtlkSQMPQEAPDDSGDMKETMNRmVDELNKQVsELSQLYREAQAELEDYRKRKS--- 637
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR-LEELEERH-ELYEEAKAKKEELERLKKRLTglt 385
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 638 ---LEDATEYIHRAEHERLMHLSNLSRTKAEesLSDMRSQYSKVLNELTQLK--------QLVDAHKENSvsITEHLEVI 706
Cdd:PRK03918 386 pekLEKELEELEKAKEEIEEEISKITARIGE--LKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKEL--LEEYTAEL 461
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 707 TTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAmsdamvpkasyeKLQASLESEVNAL-AAKLKESVKEKEK 785
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA------------EQLKELEEKLKKYnLEELEKKAEEYEK 529
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 786 AHSEVAQVRSEVSQAKREKENIQTLLKSKEqevtELVQKFQRAQEELAGL-KRCSETSSKLEEDKDEKINEMTKEVLKLK 864
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPFYNEYL 605
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564335600 865 EALNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQEVVSVY 915
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
88-223 1.49e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.03  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  88 SALHIAAKNGHPEYIKKLLQYKSpaesVDN-----LGKTALHYAAAQGSLQAVQVLCEH-----KSPINLKDLDGNIPLL 157
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPS----CDLfqrgaLGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 158 VAIQNGHSEACHFLLDHGADVNS----------RDKN----GRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALY 223
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVSpratgtffrpGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
601-834 6.51e-10

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 63.11  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 601 KETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyihraehERLMHLSNLSRtkAEESLSDMRSQYSKVLN 680
Cdd:COG3206  170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE-------EAKLLLQQLSE--LESQLAEARAELAEAEA 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 681 ELTQLKQLVDAHKENSVSITEHlEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMvpkasyEK 760
Cdd:COG3206  241 RLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA------QR 313
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335600 761 LQASLESEVNALAAK---LKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLkskeqevTELVQKFQRAQEELAG 834
Cdd:COG3206  314 ILASLEAELEALQAReasLQAQLAQLEARLAELPELEAELRRLEREVEVARELY-------ESLLQRLEEARLAEAL 383
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-172 6.63e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 6.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564335600  121 TALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLL 172
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
9-268 7.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   9 RKSDTNEWN-KNDDRLLQAVENG-DAEKVASLLgKKGASATKHDSEGKTAFHLAAA-KGHVECLKVMVTHGVDVTAQDSS 85
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLI-MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  86 GHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYA-AAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNG- 163
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 164 HSEACHFLLDHGADVNSRDKNGRTALMLACETGSanTVEALIKKGADLN----LVDSLGHNALYYSKLSENAGIQSLLLS 239
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAELRdsrvLHKSLNDNMFSFRYIIAHICIQDFIRH 532
                        250       260
                 ....*....|....*....|....*....
gi 564335600 240 KISQDADLKTPTKAKQLSDVSSPRSITST 268
Cdd:PHA02876 533 DIRNEVNPLKRVPTRFTSLRESFKEIIQS 561
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 1.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.76e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564335600   86 GHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
155-205 1.98e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.98e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564335600  155 PLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALI 205
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
608-903 2.41e-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: 61.61  E-value: 2.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   608 VDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNlSRTKAEESLSDMRSQYSKVLNELTQLKQ 687
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   688 LVDAHKEN-SVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLE 766
Cdd:TIGR02168  779 EAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   767 SEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLK-RCSETSSKL 845
Cdd:TIGR02168  859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRI 938
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 564335600   846 EEDKdEKINEmtKEVLKLKEALNSLSQLSYSTSSSKRQTQQLEmlqqqvkqlqNQLAE 903
Cdd:TIGR02168  939 DNLQ-ERLSE--EYSLTLEEAEALENKIEDDEEEARRRLKRLE----------NKIKE 983
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
403-852 4.20e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 4.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 403 QLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDttclnNTEISEngsdLSQKLKDTQSKYEEAMKEVLSVQ--KQMKLGL 480
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEK-----EERLEE----LKKKLKELEKRLEELEERHELYEeaKAKKEEL 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 481 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKA----RVQELETKLVEKEKAEATKP------SSEVCEEMR 550
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGelkkEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELL 454
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 551 NSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpqeapddsgDMKETMNRMVDELNKQVSELSQL-YREAQAEL 629
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE----------SELIKLKELAEQLKELEEKLKKYnLEELEKKA 524
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 630 EDYRKRKSLEDATEYIHRAEHERLMHLSNLSRTKA--EESLSDMRSQYSKVLNELTQ------------LKQLVDAHKE- 694
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAelEKKLDELEEELAELLKELEElgfesveeleerLKELEPFYNEy 604
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 695 NSVSITEHlEVITTLRTMAKEmEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLqaSLESEVNALAA 774
Cdd:PRK03918 605 LELKDAEK-ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRA 680
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 775 KLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEqEVTELVQKFQR--AQEELAGLKRCSETSSKL-EEDKDE 851
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKykALLKERALSKVGEIASEIfEELTEG 759

                 .
gi 564335600 852 K 852
Cdd:PRK03918 760 K 760
PHA02878 PHA02878
ankyrin repeat protein; Provisional
34-195 6.45e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 6.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  34 KVASLLGKKGASATKHD-SEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPA 112
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 113 ESVDNLGKTALHYAAAQ-GSLQAVQVLCEHKSPINLKD-LDGNIPLLVAIqngHSE-ACHFLLDHGADVNSRDKNGRTAL 189
Cdd:PHA02878 228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSI---KSErKLKLLLEYGADINSLNSYKLTPL 304

                 ....*.
gi 564335600 190 MLACET 195
Cdd:PHA02878 305 SSAVKQ 310
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
401-888 1.53e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtdttclnnTEISEngsdLSQKLKDTQSKYEEAMKEVLSVQKQMKLG- 479
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELR--------LELEE----LELELEEAQAEEYELLAELARLEQDIARLe 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 480 -LLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIE 558
Cdd:COG1196  309 eRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 559 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSL 638
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 639 EDATEYIHRAEHERLMHLSNL-SRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEME 717
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAaARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 718 EKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEV 797
Cdd:COG1196  549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 798 SQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEALNSLSQLSYST 877
Cdd:COG1196  629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
                        490
                 ....*....|.
gi 564335600 878 SSSKRQTQQLE 888
Cdd:COG1196  709 LAEAEEERLEE 719
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
488-865 1.86e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.51  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 488 GDSRLREVRVTDEDVDALKQ-DLQRALEESKRDKARVQELETKLVEkekaeaTKPSSEVCEEMRNSYCSVIENMNKekaf 566
Cdd:PRK02224 172 SDARLGVERVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAE------LDEEIERYEEQREQARETRDEADE---- 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 567 LFEKYQQAQEEIMKLKdtlksqmpqEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyih 646
Cdd:PRK02224 242 VLEEHEERREELETLE---------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--- 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 647 RAEHERLMHLSNlSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSvsitehleviTTLRTMAKEMEEKTVTLQEH 726
Cdd:PRK02224 310 EAVEARREELED-RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----------EELREEAAELESELEEAREA 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 727 LASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKE---SVKEKEKAHSEVAQVRSE------- 796
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAgkcpecg 458
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 797 -----------VSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE------ELAGLKRCSETSSKLEEDKDEKINEMTKE 859
Cdd:PRK02224 459 qpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRER 538

                 ....*.
gi 564335600 860 VLKLKE 865
Cdd:PRK02224 539 AEELRE 544
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
492-836 2.87e-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: 57.77  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   492 LREVRVTDEDVDA----LKQDLQRaLEESKRDKARVQELETklvEKEKAEATKPSSEVcEEMRNSycsvIENMNKEKAFL 567
Cdd:TIGR02169  179 LEEVEENIERLDLiideKRQQLER-LRREREKAERYQALLK---EKREYEGYELLKEK-EALERQ----KEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   568 FEKYQQAQEEIMKLKDTLksqmpqeapddsgdmkETMNRMVDELNKQVSELSqlyreaqaELEDYRKRKSLEDATEYIHR 647
Cdd:TIGR02169  250 EEELEKLTEEISELEKRL----------------EEIEQLLEELNKKIKDLG--------EEEQLRVKEKIGELEAEIAS 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   648 AehERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHL----EVITTLRTMAKEMEEKTVTL 723
Cdd:TIGR02169  306 L--ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDKEFAET 383
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   724 QEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 803
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
                          330       340       350
                   ....*....|....*....|....*....|...
gi 564335600   804 KENIQTLLKSKEQEVTELVQKFQRAQEELAGLK 836
Cdd:TIGR02169  464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-222 2.90e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 2.90e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564335600  171 LLDHG-ADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNAL 222
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
60-238 5.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  60 AAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLC 139
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 140 EHKSPINlkDL---DGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDS 216
Cdd:PHA02875  89 DLGKFAD--DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                        170       180
                 ....*....|....*....|..
gi 564335600 217 LGHNALYYSKLSENAGIQSLLL 238
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLL 188
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
19-207 8.05e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 8.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  19 NDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTH-----GVDVTAQDSSGHSALHIA 93
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  94 AKNGHPEYIKKLLQY----KSP-------AESVDNL---GKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPL-LV 158
Cdd:cd22192   97 VVNQNLNLVRELIARgadvVSPratgtffRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhIL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564335600 159 AIQNGHSEACH---FLLDHGADVNS------RDKNGRTALMLACETGSANTVEALIKK 207
Cdd:cd22192  177 VLQPNKTFACQmydLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00121 PTZ00121
MAEBL; Provisional
419-867 1.30e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  419 EAEKKQLQDELQSQRTDTTCLNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGLLSHESADGDSRLREVRVT 498
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  499 DEDVDALKQDLQ--RALEESKR---DKARVQELETKLVEKEKAEATKPSSEvceEMRNSYCSVIENMNKEKAflfEKYQQ 573
Cdd:PTZ00121 1417 KKKADEAKKKAEekKKADEAKKkaeEAKKADEAKKKAEEAKKAEEAKKKAE---EAKKADEAKKKAEEAKKA---DEAKK 1490
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  574 AQEEIMKLKDTLKSQMPQEAPDDSGDMKETmNRMVDELNK-----QVSELSQlyREAQAELEDYRKRKSLEDATEYIHRA 648
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE-AKKADEAKKaeeakKADEAKK--AEEKKKADELKKAEELKKAEEKKKAE 1567
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  649 EHERLMHLSNLSRTKAEEslsdMRSQYSKVLNELTQLKQLVDAHKENSVSITEHlEVITTLRTMAKEMEEKTVTLQEHLA 728
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEE----AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKKKE 1642
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  729 SKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENiq 808
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-- 1720
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564335600  809 tlLKSKEQEVTELVQKFQRAQEELaglKRCSETSSKLEEDKDeKINEMTKEVLKLKEAL 867
Cdd:PTZ00121 1721 --LKKAEEENKIKAEEAKKEAEED---KKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEI 1773
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
127-206 2.52e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 127 AAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIK 206
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02798 PHA02798
ankyrin-like protein; Provisional
131-240 3.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.07  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 131 SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQN----GHS-EACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEAL- 204
Cdd:PHA02798  50 STDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILl 129
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564335600 205 --IKKGADLNLVDSLGHNAL-YYSKLSENAGIQ--SLLLSK 240
Cdd:PHA02798 130 fmIENGADTTLLDKDGFTMLqVYLQSNHHIDIEiiKLLLEK 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
599-866 3.46e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 3.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   599 DMKETMNRMVD---ELNKQV------SELSQLYREAQAELEDYRKRKSLEDATEYihraeherlmhlsnlsrtkaeesls 669
Cdd:TIGR02168  183 RTRENLDRLEDilnELERQLkslerqAEKAERYKELKAELRELELALLVLRLEEL------------------------- 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   670 dmRSQYSKVLNELTQLKQLVDAHKENsvsITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMS 749
Cdd:TIGR02168  238 --REELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   750 DAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQ 829
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 564335600   830 EELAG----LKRCSETSSKLEEDKDEKINEMTKEVLKLKEA 866
Cdd:TIGR02168  393 LQIASlnneIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
Ank_5 pfam13857
Ankyrin repeats (many copies);
50-93 3.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 3.71e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 564335600   50 DSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIA 93
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
162-271 3.87e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 162 NGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSKI 241
Cdd:PTZ00322  92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
                         90       100       110
                 ....*....|....*....|....*....|
gi 564335600 242 SQDADLKTPTKAKQLSDVssPRSITSTPLS 271
Cdd:PTZ00322 172 QCHFELGANAKPDSFTGK--PPSLEDSPIS 199
PHA02878 PHA02878
ankyrin repeat protein; Provisional
100-229 4.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 100 EYIKKLLQYKSPAESVD-NLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADV 178
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564335600 179 NSRDKNGRTALMLAC-ETGSANTVEALIKKGADLNLVDS-LGHNALYYSKLSE 229
Cdd:PHA02878 228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-251 5.00e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 5.00e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335600  189 LMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSKISQDADLKTPT 251
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
51-275 5.14e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   51 SEGKTAFHLAAAKGHVECLKVMVTHG--VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVdnlGKTALHyAAA 128
Cdd:TIGR00870  15 SDEEKAFLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLH-AIS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  129 QGSLQAVQVLCEHKSPINLKDLD--------------GNIPLLVAIQNGHSEACHFLLDHGADVNSRDK----------- 183
Cdd:TIGR00870  91 LEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvd 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  184 ---NGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKL-SENA--------GIQSLLLSKISQDADLktpt 251
Cdd:TIGR00870 171 sfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMeNEFKaeyeelscQMYNFALSLLDKLRDS---- 246
                         250       260
                  ....*....|....*....|....
gi 564335600  252 kaKQLSDVSSPRSITSTPLSGKES 275
Cdd:TIGR00870 247 --KELEVILNHQGLTPLKLAAKEG 268
PHA02798 PHA02798
ankyrin-like protein; Provisional
35-240 5.45e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.30  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHV---ECLKVMVTHGVDVTAQDSSGHSALHIAAKNGHP---EYIKKLLQY 108
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 109 KSPAESVDN-LGKTALHyaaaqgslqavqvlCEHKSpiNLKDLDGNIpllvaiqnghseaCHFLLDHGADVNSRDKNGRT 187
Cdd:PHA02798 171 GVDINTHNNkEKYDTLH--------------CYFKY--NIDRIDADI-------------LKLFVDNGFIINKENKSHKK 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564335600 188 ALM------LACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSENAGIQSLLLSK 240
Cdd:PHA02798 222 KFMeylnslLYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-83 5.52e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 5.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600   23 LLQAVENGDAEKVASLLGKKgasATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQD 83
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
403-864 5.90e-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: 53.58  E-value: 5.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   403 QLQDTLHDLQKRLETSEAEKKQLQ-------------DELQSQRTDttclNNTEISENGSDLSQKLKDTQSKYEEAMKEV 469
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitiDHLRRELDD----RNMEVQRLEALLKAMKSECQGQMERQMAAI 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   470 LSvqKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELEtKLVEKEKAEATKPSSEVCEEM 549
Cdd:pfam15921  454 QG--KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKL 530
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   550 RNsycsvIENMNKEKAFLfeKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAEL 629
Cdd:pfam15921  531 QE-----LQHLKNEGDHL--RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   630 EDYRKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVIT-T 708
Cdd:pfam15921  604 LELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrN 682
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   709 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 788
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600   789 EVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLK 864
Cdd:pfam15921  763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
PHA02874 PHA02874
ankyrin repeat protein; Provisional
35-161 7.59e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  35 VASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSSGHSALHIAAKngHPEYIKKLLQYKSPAES 114
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASIND 249
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564335600 115 VDNLGKTALHYAAAQG-SLQAVQVLCEHKSPINLKDLDGNIPLLVAIQ 161
Cdd:PHA02874 250 QDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1-120 7.74e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 7.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   1 MKSLKAKFRKSDTNEWNKNDD-------------RLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVE 67
Cdd:PTZ00322  51 LEALEATENKDATPDHNLTTEevidpvvahmltvELCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQ 129
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564335600  68 CLKVMVTHGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGK 120
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
PTZ00121 PTZ00121
MAEBL; Provisional
456-886 8.30e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  456 KDTQSKYEEAMKEVLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQdlqRALEESKRDKARVQELETKLVEKEK 535
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEA 1361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  536 AEATKPSSEVCEEMRNSYCSVIENMNKEKAFLFEKYQQAqEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQV 615
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  616 SELSQLyREAQAELEDYRKRKSLEDATEYIHRAEHERL----MHLSNLSRTKAEESL--SDMRSQYSKVLNELTQLKQLV 689
Cdd:PTZ00121 1441 EEAKKA-DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaeeAKKADEAKKKAEEAKkkADEAKKAAEAKKKADEAKKAE 1519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  690 DAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSD------AMVPKASYEKLQA 763
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeaKKAEEARIEEVMK 1599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  764 SLESEVNALAAKLKESVKEKEKAHsevaqvrsEVSQAKREKENIQTLLKSKEQEVTElVQKFQRAQEElaGLKRCSETSS 843
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEE--NKIKAAEEAK 1668
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 564335600  844 KLEEDKD--EKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQ 886
Cdd:PTZ00121 1669 KAEEDKKkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-126 8.89e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 8.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600   72 MVTHG-VDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYA 126
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
401-868 9.00e-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: 53.15  E-value: 9.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTclnnteisengsDLSQKLKDTQSKYEEAMKEVLSVQKQMKLgl 480
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE------------ELEREIEEERKRRDKLTEEYAELKEELED-- 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   481 LSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEkaeatkpssevcEEMRNSYCSVIENM 560
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL------------ADLNAAIAGIEAKI 436
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   561 NK---EKAFLFEKYQQAQEEIMKLKDTLKSqmpqeAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKS 637
Cdd:TIGR02169  437 NEleeEKEDKALEIKKQEWKLEQLAADLSK-----YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   638 LEDATEYIHRAEHERLMHLSNLSR--TKAEESLSDMRSQYSKV-------------------------LNELTQLKQLVD 690
Cdd:TIGR02169  512 VEEVLKASIQGVHGTVAQLGSVGEryATAIEVAAGNRLNNVVVeddavakeaiellkrrkagratflpLNKMRDERRDLS 591
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   691 AHKENSVsITEHLEVIT---TLRTMAKEMEEKTVTLQEHLASKE--GEV--AKLEKQLAEEKAAMSDAMVPKASYEKLQA 763
Cdd:TIGR02169  592 ILSEDGV-IGFAVDLVEfdpKYEPAFKYVFGDTLVVEDIEAARRlmGKYrmVTLEGELFEKSGAMTGGSRAPRGGILFSR 670
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   764 SLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR-CSETS 842
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdLSSLE 750
                          490       500       510
                   ....*....|....*....|....*....|..
gi 564335600   843 SKLEEDKDE------KINEMTKEVLKLKEALN 868
Cdd:TIGR02169  751 QEIENVKSElkeleaRIEELEEDLHKLEEALN 782
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
91-185 1.46e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  91 HIAAkNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHF 170
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90
                 ....*....|....*
gi 564335600 171 LLDHGADVNSRDKNG 185
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
401-868 1.66e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTclnntEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQM--KL 478
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELE-----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeAE 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 479 GLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKA-EATKPSSEVCEEMRNSYCSVI 557
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEE 458
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 558 ENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQA 627
Cdd:COG1196  459 EALLELLAELLEEAALLEAALAELLeelaeaaarlLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 628 ELEDY-------RKRKSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNE---LTQLKQLVDAHKENSV 697
Cdd:COG1196  539 ALEAAlaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavdLVASDLREADARYYVL 618
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 698 SITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAmsdamvpkasyeKLQASLESEVNALAAKLK 777
Cdd:COG1196  619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR------------ELLAALLEAEAELEELAE 686
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 778 ESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMT 857
Cdd:COG1196  687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
                        490
                 ....*....|.
gi 564335600 858 KEVLKLKEALN 868
Cdd:COG1196  767 RELERLEREIE 777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
401-868 3.14e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   401 IQQLQDTLHDLQKRL-------ETSEAEKKQLQDELQSQRTDTTCLnNTEISENGS---DLSQKLKDTQSKYEEAMKEVL 470
Cdd:TIGR02168  276 VSELEEEIEELQKELyalaneiSRLEQQKQILRERLANLERQLEEL-EAQLEELESkldELAEELAELEEKLEELKEELE 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   471 SVQKQMK--------LGLLSHE--------SADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKE 534
Cdd:TIGR02168  355 SLEAELEeleaeleeLESRLEEleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   535 KAEATKPSSEVcEEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-QMPQEAPDDSGDMKETMNRMVDELNK 613
Cdd:TIGR02168  435 LKELQAELEEL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlQARLDSLERLQENLEGFSEGVKALLK 513
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   614 QVSELSQL-------------YREA-----QAELEDY--RKRKSLEDATEYIHRAEHERLMHLSnLSRTKAEESLSDMRS 673
Cdd:TIGR02168  514 NQSGLSGIlgvlselisvdegYEAAieaalGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLP-LDSIKGTEIQGNDRE 592
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   674 QYSKVLNELTQLKQLVDAHKENSVSIT---EHLEVITTLRT---MAKEMEEKT--VTLQEHLASKEG------------- 732
Cdd:TIGR02168  593 ILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNaleLAKKLRPGYriVTLDGDLVRPGGvitggsaktnssi 672
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   733 -----EVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENI 807
Cdd:TIGR02168  673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600   808 QTLLKSKEQEVTELVQKFQRAQEElagLKRCSETSSKLEEDkdekINEMTKEVLKLKEALN 868
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEE---LAEAEAEIEELEAQ----IEQLKEELKALREALD 806
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
410-832 5.31e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 410 DLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGllSHESAD 487
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAAELESELEEAREAVEDR--REEIEE 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 488 GDSRLREVRV----TDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRNSYC--------- 554
Cdd:PRK02224 389 LEEEIEELRErfgdAPVDLGNAEDFLEELREERDELREREAELEATL--RTARERVEEAEALLEAGKCPECgqpvegsph 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 555 -SVIENMNKEKAFLFEKYQQAQEEIMKLKDTLksqmpqeapDDSGDMKETMNRmVDELNKQVSELSQLYREAQAELEDYR 633
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERL---------ERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEKR 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 634 KR--KSLEDATEYIHRAEHERlmhlsnLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAH---KENSVSITEHLEVITT 708
Cdd:PRK02224 537 ERaeELRERAAELEAEAEEKR------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLLAAIADAEDEIER 610
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 709 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEekAAMSDAMVPKASYEKLQASLESEVNALAAklkesvkEKEKAHS 788
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELRE-------ERDDLQA 681
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 564335600 789 EVAQVRSEVSQAKREKENIQTL------LKSKEQEVTELVQKFQRAQEEL 832
Cdd:PRK02224 682 EIGAVENELEELEELRERREALenrveaLEALYDEAEELESMYGDLRAEL 731
Ank_5 pfam13857
Ankyrin repeats (many copies);
145-192 5.51e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 5.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 564335600  145 INLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLA 192
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
184-213 6.57e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 6.57e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 564335600   184 NGRTALMLACETGSANTVEALIKKGADLNL 213
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
402-829 9.06e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 402 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDttcLNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKlgll 481
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKL---LQLLPLYQELEALEAELAELPERLEELEERLEELRELEE---- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 482 shesaDGDSRLREVRVTDEDVDALKQDL-QRALEESKRDKARVQELETKLVEKEKAEATkpSSEVCEEMRNSYCSVIENM 560
Cdd:COG4717  164 -----ELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEE--AQEELEELEEELEQLENEL 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 561 NKEKafLFEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKETMNRMVDELnkqVSELSQLYREAQAELEDYRKRKSLED 640
Cdd:COG4717  237 EAAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALP 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 641 ATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLvdahkENSVSITEHLEVITTLRTMAK----EM 716
Cdd:COG4717  312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-----EEELQLEELEQEIAALLAEAGvedeEE 386
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 717 EEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVpkasyEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSE 796
Cdd:COG4717  387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 564335600 797 VSQAKREKE--NIQTLLKSKEQEVTELVQKFQRAQ 829
Cdd:COG4717  462 LEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
Ank_5 pfam13857
Ankyrin repeats (many copies);
105-159 9.46e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 9.46e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600  105 LLQYKSPA-ESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVA 159
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
401-740 1.01e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtdttclnnTEISENGSDLSQKlKDTQSKYEEAMKEVlsvqkqmklgl 480
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVK--------SELKELEARIEEL-EEDLHKLEEALNDL----------- 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   481 lshESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQeLETKLVEKEKAEATKPSSEvCEEMRNSYCSVIENM 560
Cdd:TIGR02169  785 ---EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT-LEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENL 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   561 NKEKAFLFEKYQQAQEEIMKLKDTLKSqmpqeapddsgdmketMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLED 640
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   641 ATEyihRAEHERLMHLSNLSRTKAEESLSDMrsQYSKVLNELTQLKQLVDAHKE-NSVSITEHLEVITTLrtmaKEMEEK 719
Cdd:TIGR02169  924 AKL---EALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRL----DELKEK 994
                          330       340
                   ....*....|....*....|.
gi 564335600   720 TVTLQEHLASKEGEVAKLEKQ 740
Cdd:TIGR02169  995 RAKLEEERKAILERIEEYEKK 1015
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
655-837 1.02e-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: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  655 HLSNLSRtkAEESLSDMRSQyskvLNELTQLKQLVDAHKENSVSITEHLEVITTLRtmAKEMEEKTVTLQEHLASKEGEV 734
Cdd:COG4913   233 HFDDLER--AHEALEDAREQ----IELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAEL 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  735 AKLEKQLAEEKAAMSDAmvpKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEV----------------- 797
Cdd:COG4913   305 ARLEAELERLEARLDAL---REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaee 381
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564335600  798 -----SQAKREKENIQTLLKSKEQEVTELVQKFQRAQE-------ELAGLKR 837
Cdd:COG4913   382 faalrAEAAALLEALEEELEALEEALAEAEAALRDLRRelreleaEIASLER 433
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
15-141 1.23e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  15 EWNKNDDRL--LQAVENGDAekvasllGKKGASATKHDSEGKTAFHLA------AAKGHVECLKVMVTHGVDVTAQDSSG 86
Cdd:PTZ00322  43 EIARIDTHLeaLEATENKDA-------TPDHNLTTEEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDG 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564335600  87 HSALHIAAKNGHPEYIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEH 141
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
402-868 1.32e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.40  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   402 QQLQDTLHDLQKRLETSEAEKKQLQDElqsqrtdttclnNTEISENGSDLSQKLKDtqskyEEAMKEVLSVQKqmklgll 481
Cdd:pfam01576   71 QELEEILHELESRLEEEEERSQQLQNE------------KKKMQQHIQDLEEQLDE-----EEAARQKLQLEK------- 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   482 shesADGDSRLREVrvtDEDVDALKQDLQRALEESKRDKARVQELETKLVEKE-----------KAEATKPSSEV----C 546
Cdd:pfam01576  127 ----VTTEAKIKKL---EEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEekakslsklknKHEAMISDLEErlkkE 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   547 EEMRNSYCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKS-----QMPQEAPDDSGDMKETMNRMVDELNKQVSELSQ- 620
Cdd:pfam01576  200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKkeeelQAALARLEEETAQKNNALKKIRELEAQISELQEd 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   621 --LYREAQAELEDYRK---------RKSLED-----ATEYIHRAEHERlmHLSNLSRTKAEES------LSDMRSQYSKV 678
Cdd:pfam01576  280 leSERAARNKAEKQRRdlgeelealKTELEDtldttAAQQELRSKREQ--EVTELKKALEEETrsheaqLQEMRQKHTQA 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   679 LNELT-QLKQLvdahKENSVSITEHLEvitTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKAS 757
Cdd:pfam01576  358 LEELTeQLEQA----KRNKANLEKAKQ---ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAE 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   758 YEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAK-------REKENIQTLLKSKEQEVTELVQKFQRAQE 830
Cdd:pfam01576  431 LAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 564335600   831 ELAGLKR--------CSETSSKLEEDKD--EKINEMTKEVLKLKEALN 868
Cdd:pfam01576  511 AKRNVERqlstlqaqLSDMKKKLEEDAGtlEALEEGKKRLQRELEALT 558
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
52-81 1.75e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.75e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 564335600    52 EGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
402-865 2.51e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  402 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKL- 478
Cdd:TIGR04523  36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNd 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  479 ----GLLSHESADGDSRLREVR----VTDEDVDALKQDLQRALEESKRDKARVQELETKL--VEKEKAEATKPSSEVCEE 548
Cdd:TIGR04523 116 keqkNKLEVELNKLEKQKKENKknidKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnlLEKEKLNIQKNIDKIKNK 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  549 MRNSY--CSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKsQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 626
Cdd:TIGR04523 196 LLKLEllLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE-KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  627 AELEDYRKRKSLEDATEYIHraeherlMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDahkENSVSITEHLEVI 706
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLK-------SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS---QNNKIISQLNEQI 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  707 TTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKA 786
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335600  787 HSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKE 865
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
184-215 3.16e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 3.16e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564335600  184 NGRTALMLACE-TGSANTVEALIKKGADLNLVD 215
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
151-183 3.42e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 3.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564335600  151 DGNIPLLVAI-QNGHSEACHFLLDHGADVNSRDK 183
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
591-803 5.10e-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: 46.68  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 591 QEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRksLEDATEYIHRAEHERLMHLSNLSRTKAEE---- 666
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIRALEQELAALEAELAELEKEIaelr 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 667 -SLSDMRSQYSKVLNELTQLKQ----LVDAHKENSVSITEHLEVITTL----RTMAKEMEEKTVTLQEHLASKEGEVAKL 737
Cdd:COG4942   97 aELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLaparREQAEELRADLAELAALRAELEAERAEL 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600 738 EKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 803
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
569-867 5.28e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 569 EKYQQAQEEIMKLKDTLKSQMPQ-----EAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKR-KSLEDAT 642
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvKELEELK 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 643 EYIHRAEHERLMHLSNLSRTKA-----EESLSDMRSQYS---KVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAK 714
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEkirelEERIEELKKEIEeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 715 EMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVR 794
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564335600 795 SEVSQAKREKENIQTLLKSKEQEVTELvqkfQRAQEELAGLKRCSETSSKL--EEDKDEKINEMTKEVLKLKEAL 867
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGREltEEHRKELLEEYTAELKRIEKEL 468
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
460-868 7.48e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 7.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 460 SKYEEAMKEVLSVQKQmKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEAT 539
Cdd:COG4717   49 ERLEKEADELFKPQGR-KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 540 KPSSEVCEEMRNSYCSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSQmpqeapddSGDMKETMNRMVDELNKQVSELS 619
Cdd:COG4717  128 LPLYQELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAEL--------QEELEELLEQLSLATEEELQDLA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 620 QLYREAQAELEDYRKRksLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDMRSQYsKVLNELTQLKQLVDAHKENSVSI 699
Cdd:COG4717  199 EELEELQQRLAELEEE--LEEAQEELEELEEELEQLENELEAAALEERLKEARLLL-LIAAALLALLGLGGSLLSLILTI 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 700 TEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEK-QLAEEKAAMSDAMVPkasyeklqaslESEVNALAAKLKE 778
Cdd:COG4717  276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP-----------PDLSPEELLELLD 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 779 SVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTK 858
Cdd:COG4717  345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
                        410
                 ....*....|.
gi 564335600 859 EVLK-LKEALN 868
Cdd:COG4717  425 LDEEeLEEELE 435
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
401-694 8.05e-05

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: 46.87  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRtDTTCLNNTEISENGS---DLSQKLKDTQSK---YEEAMKEVLSVQK 474
Cdd:COG3096   349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-ARLEAAEEEVDSLKSqlaDYQQALDVQQTRaiqYQQAVQALEKARA 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  475 QMKLGLLSHESADG---DSRLREVRVTDEdVDALKQDLQRAlEESKRDKARVQELETKLV-EKEKAEATKPSSEVCEEMR 550
Cdd:COG3096   428 LCGLPDLTPENAEDylaAFRAKEQQATEE-VLELEQKLSVA-DAARRQFEKAYELVCKIAgEVERSQAWQTARELLRRYR 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  551 nSYCSVIENMNKEKAFLFEKYQQA--QEEIMKLKDTLKSQMPQE--APDDSGDMKETMNRMVDELNKQVSELSQLYREAQ 626
Cdd:COG3096   506 -SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600  627 AELEDYR-KRKSLEdATEYIHRAEHERLMHLSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKE 694
Cdd:COG3096   585 QQLEQLRaRIKELA-ARAPAWLAAQDALERLREQSGEALADSqeVTAAMQQLLEREREATVERDELAARKQ 654
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
402-911 9.25e-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: 46.59  E-value: 9.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   402 QQLQDTLHDLQKRLetSEAEKKQLQDELQSQRTDTTCLNNTEisengSDLSQKLKDTQSKYEEAMKEVLSVQKQM----- 476
Cdd:TIGR02168  216 KELKAELRELELAL--LVLRLEELREELEELQEELKEAEEEL-----EELTAELQELEEKLEELRLEVSELEEEIeelqk 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   477 KLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRNSYCSV 556
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL--EEKLEELKEELESLEAELEELEAE 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   557 IENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMPQEApddsgDMKETMNRMVDELNKQVSELSQLYREAQ-AELEDYRKR 635
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   636 KSLEDATEYIHRAEHERLMH-LSNL--SRTKAEESLSDMRSQYSKVLNELTQLKQLVDAH----------KENSVSITEH 702
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEaLEELreELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvkalLKNQSGLSGI 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   703 LEVITTLRTMAKEME-EKTVTLQEHLAS----------------KEGEVAKL-----------------EKQLAEEKAAM 748
Cdd:TIGR02168  522 LGVLSELISVDEGYEaAIEAALGGRLQAvvvenlnaakkaiaflKQNELGRVtflpldsikgteiqgndREILKNIEGFL 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   749 SDAMVPKASYEKLQASLES------------EVNALAAKLKE-----------------SVKEKEKAHSEVAQVRSEVSQ 799
Cdd:TIGR02168  602 GVAKDLVKFDPKLRKALSYllggvlvvddldNALELAKKLRPgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEE 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   800 AKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKrcsetssKLEEDKDEKINEMTKEVLKL-KEALNSLSQLSYSTS 878
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLeAEVEQLEERIAQLSK 754
                          570       580       590
                   ....*....|....*....|....*....|...
gi 564335600   879 SSKRQTQQLEMLQQQVKQLQNQLAECKKQHQEV 911
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
402-863 1.10e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   402 QQLQDTLHDLQKRLETSEAEKKQLQDELQsqrTDTTCLNNTE-----ISENGSDLSQKLKDTQSKYEEamKEVLSVQKQM 476
Cdd:pfam01576   22 QKAESELKELEKKHQQLCEEKNALQEQLQ---AETELCAEAEemrarLAARKQELEEILHELESRLEE--EEERSQQLQN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   477 KLGLLSHESADGDSRLrevrvtdEDVDALKQDLQraLEESKRDkARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSV 556
Cdd:pfam01576   97 EKKKMQQHIQDLEEQL-------DEEEAARQKLQ--LEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   557 IENMNKEKAFLFEKYQQAQEEIM-----KLKDTLKSQMPQEApddsgdMKETMNRMVDELNKQVSELSQLYREAQAELEd 631
Cdd:pfam01576  167 NLAEEEEKAKSLSKLKNKHEAMIsdleeRLKKEEKGRQELEK------AKRKLEGESTDLQEQIAELQAQIAELRAQLA- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   632 yRKRKSLEDAteyIHRAEHErlmhlsNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEvitTLRT 711
Cdd:pfam01576  240 -KKEEELQAA---LARLEEE------TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE---ALKT 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   712 MAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEK----AAMSD------------------AMVPKASYEKLQASLESEV 769
Cdd:pfam01576  307 ELEDTLDTTAAQQELRSKREQEVTELKKALEEETrsheAQLQEmrqkhtqaleelteqleqAKRNKANLEKAKQALESEN 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   770 NALAAKLK-------ESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGL-KRCSET 841
Cdd:pfam01576  387 AELQAELRtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLsKDVSSL 466
                          490       500
                   ....*....|....*....|..
gi 564335600   842 SSKLeEDKDEKINEMTKEVLKL 863
Cdd:pfam01576  467 ESQL-QDTQELLQEETRQKLNL 487
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
507-866 1.19e-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: 46.26  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   507 QDLQRALEESKRDKAR--------VQELETKLVEKEK-----AEATKPSSEVCEEMRNSYCSVIENMNKEKAFLFEKYQQ 573
Cdd:pfam15921   88 KDLQRRLNESNELHEKqkfylrqsVIDLQTKLQEMQMerdamADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLED 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   574 AQEEIMKLKDTLKSQ--MPQEAPDDSGDMKETMNRMVDELNKQV--------SELSQLYREAQAELEDYRKRK-SLEDAT 642
Cdd:pfam15921  168 SNTQIEQLRKMMLSHegVLQEIRSILVDFEEASGKKIYEHDSMStmhfrslgSAISKILRELDTEISYLKGRIfPVEDQL 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   643 EYI--------------HRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQlvDAHKENSVSITEHLEVITT 708
Cdd:pfam15921  248 EALksesqnkielllqqHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLEST 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   709 LRTMAKEMEEKTVTLqehlaskEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKL----KESVKEKE 784
Cdd:pfam15921  326 VSQLRSELREAKRMY-------EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKE 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   785 KAHS----------EVAQVRSEVSQAKREKENIQTLLKSKEQEVT-ELVQKFQRAQEELAGLKRCSETSSKLEEDKD--- 850
Cdd:pfam15921  399 QNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSLTAQLESTKEmlr 478
                          410
                   ....*....|....*.
gi 564335600   851 EKINEMTKEVLKLKEA 866
Cdd:pfam15921  479 KVVEELTAKKMTLESS 494
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
595-813 1.30e-04

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 45.82  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  595 DDSGDMKETMNRMVDELNKQVSELSQLYreaQAELEDYRKRKSLEDATEYIHRAEHERLMHLSNLSRtKAEESLSDM--R 672
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESAISSLLAQL---PAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRR-ALEAKRKDPfkS 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  673 SQYSKVLNELTQLKQLVDAHKEnsvSITEHLEVITTLRTMAKEMEEKtvtlqehlaskegevakLEKQLAEEKAAMSDAm 752
Cdd:pfam13166 355 IELDSVDAKIESINDLVASINE---LIAKHNEITDNFEEEKNKAKKK-----------------LRLHLVEEFKSEIDE- 413
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600  753 vpkasYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKS 813
Cdd:pfam13166 414 -----YKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
605-825 1.32e-04

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 45.61  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  605 NRMVD-ELNKQVSELSQLYREAQAELEdyRKRKSLEDATEYIHRAEHERLMHLSNLS----RTKAEEslsDMRSQYSKVL 679
Cdd:pfam09726 414 SRQTEqELRSQISSLTSLERSLKSELG--QLRQENDLLQTKLHNAVSAKQKDKQTVQqlekRLKAEQ---EARASAEKQL 488
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  680 NELTQLKQLVDAHKENSVS--ITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKaamsdamvpkaS 757
Cdd:pfam09726 489 AEEKKRKKEEEATAARAVAlaAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELR-----------K 557
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335600  758 YEKLQASLESEVNALAAkLKESVKEKEKAHSEVAQVR----SEVSQAKREKENIQTLLKSKEQEVTELVQKF 825
Cdd:pfam09726 558 YKESEKDTEVLMSALSA-MQDKNQHLENSLSAETRIKldlfSALGDAKRQLEIAQGQIYQKDQEIKDLKQKI 628
Ank_4 pfam13637
Ankyrin repeats (many copies);
23-73 1.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564335600   23 LLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMV 73
Cdd:pfam13637   5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
mukB PRK04863
chromosome partition protein MukB;
494-847 1.42e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  494 EVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEAtkpssevceEMRNSYCSVIENMNKEKAFL--FEKY 571
Cdd:PRK04863  280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAES---------DLEQDYQAASDHLNLVQTALrqQEKI 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  572 QQAQEEIMKLKDTLKSQM-----PQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDYRKRKSLEDateyih 646
Cdd:PRK04863  351 ERYQADLEELEERLEEQNevveeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE------ 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  647 raEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSvsiTEHLEVITTLRTMAKEME--------- 717
Cdd:PRK04863  425 --RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAH---SQFEQAYQLVRKIAGEVSrseawdvar 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  718 ------EKTVTLQEHLASKEGEVAKLEKQLAEEKAA--MSDAMVPKASyekLQASLESEVNALAAKLKESVKEKEKAHSE 789
Cdd:PRK04863  500 ellrrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAerLLAEFCKRLG---KNLDDEDELEQLQEELEARLESLSESVSE 576
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335600  790 VAQVRSEVSQAKREkeniqtlLKSKEQEVTELVQKFQRAQEELAGLKRCS----ETSSKLEE 847
Cdd:PRK04863  577 ARERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALARLREQSgeefEDSQDVTE 631
PHA02741 PHA02741
hypothetical protein; Provisional
47-162 1.63e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.49  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  47 TKHDSEGKTAFHLAAAKGHVECLKVMV------THGVDVTAQDSSGHSALHIAAKNGHPEYIKKLLQYK-------SPAE 113
Cdd:PHA02741  15 AEKNSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAQLAAEIIDHLielgadiNAQE 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564335600 114 SVDnlGKTALHYAAAQGSLQAVQVLCEHKSpINLK--DLDGNIPLLVAIQN 162
Cdd:PHA02741  95 MLE--GDTALHLAAHRRDHDLAEWLCCQPG-IDLHfcNADNKSPFELAIDN 142
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
717-837 1.82e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  717 EEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAK-----LKESVKEKEKAHSEVA 791
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSDDLA 688
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564335600  792 QVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR 837
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-179 1.92e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 564335600   151 DGNIPLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
664-835 2.11e-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: 44.75  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 664 AEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEV----ITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEK 739
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerrIAALARRIRALEQELAALEAELAELEKEIAELRA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 740 QLAEEKAAMSDAMV------------------------------------PKASYEKLQASLEsEVNALAAKLKESVKEK 783
Cdd:COG4942   98 ELEAQKEELAELLRalyrlgrqpplalllspedfldavrrlqylkylapaRREQAEELRADLA-ELAALRAELEAERAEL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564335600 784 EKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGL 835
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
404-824 2.12e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  404 LQDTLHDLQKRLETSEAEKKQLQDELQSQRTD----TTCLNNTEI--SENGSDLS--QKLKDTQSKYEEAMKEVLSVQKQ 475
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSEleemTKFKNNKEVelEELKKILAedEKLLDEKKQFEKIAEELKGKEQE 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  476 MKLGLLSHESADGDSRLREVRVTDEDVDALKQ--DLQRALEESKRDKARVQELETKLVEKEKaEATKPSSEVCEEMRNSY 553
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHCDKLLLENK-ELTQEASDMTLELKKHQ 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  554 CSVIENMNKEKAFLfEKYQQAQEEIMKLKDTLKSqMPQEAPDDSGDMKETMNRmvDELNKQVSELSQLYREAQAELEDYR 633
Cdd:pfam05483 520 EDIINCKKQEERML-KQIENLEEKEMNLRDELES-VREEFIQKGDEVKCKLDK--SEENARSIEYEVLKKEKQMKILENK 595
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  634 ---KRKSLEDATEYIHRAEHERlmhlSNLSRTKAEES--LSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVitT 708
Cdd:pfam05483 596 cnnLKKQIENKNKNIEELHQEN----KALKKKGSAENkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKI--S 669
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  709 LRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpKASYEKLQASLESEVNALAAKLKESVKEKEKAHS 788
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH---KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 564335600  789 EVAQVRSEVSQAKR----EKENIQTLLKSKEQEVTELVQK 824
Cdd:pfam05483 747 ELSNIKAELLSLKKqleiEKEEKEKLKMEAKENTAILKDK 786
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
52-83 2.25e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564335600   52 EGKTAFHLAAAK-GHVECLKVMVTHGVDVTAQD 83
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
184-212 3.11e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 3.11e-04
                          10        20
                  ....*....|....*....|....*....
gi 564335600  184 NGRTALMLACETGSANTVEALIKKGADLN 212
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
102-247 3.56e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.49  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 102 IKKLLQYKSpAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLkdLDGNIPLLVAIQNGHSEACHFLLDHGADVNSR 181
Cdd:PHA02791  14 LKSFLSSKD-AFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQF 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335600 182 DKNGRTALMLACETGSANTVEALIKKGADLNLVDSLG-HNALYYSKLSENAGIQSLLLSKISQDADL 247
Cdd:PHA02791  91 DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDL 157
PHA02876 PHA02876
ankyrin repeat protein; Provisional
129-232 4.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 129 QGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKG 208
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
                         90       100
                 ....*....|....*....|....*....
gi 564335600 209 A-----DLNLVDSLGHNALYYSKLSENAG 232
Cdd:PHA02876 235 SninknDLSLLKAIRNEDLETSLLLYDAG 263
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
635-868 5.19e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.76  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 635 RKSLEDATEYIHRAEherLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHK-----ENSVSITEHLEVITTL 709
Cdd:PRK05771  15 KSYKDEVLEALHELG---VVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreeKKKVSVKSLEELIKDV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 710 RTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAE-----------------EKAAMSDAMVPKASYEKLQASLESEVNAL 772
Cdd:PRK05771  92 EEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 773 AAKLKESV-------KEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRcsetssKL 845
Cdd:PRK05771 172 ISTDKGYVyvvvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAK------KY 245
                        250       260
                 ....*....|....*....|...
gi 564335600 846 EEDKDEKINEMTKEVLKLKEALN 868
Cdd:PRK05771 246 LEELLALYEYLEIELERAEALSK 268
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
608-803 6.44e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 608 VDELNKQVSELSQLYREAQAELEDYRKR-----KSLEDATEYIHRAEHERLMHLSNLSRTKAEESLSDM---RSQYSKVL 679
Cdd:COG3883   39 LDALQAELEELNEEYNELQAELEALQAEidklqAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgSESFSDFL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 680 NELTQLKQLVDAHKEnsvSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYE 759
Cdd:COG3883  119 DRLSALSKIADADAD---LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564335600 760 KLQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE 803
Cdd:COG3883  196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
401-653 6.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  401 IQQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnteisengsDLSQKLKDtqskYEEAMKEVLSVQKQMklgl 480
Cdd:COG4913   619 LAELEEELAEAEERLEALEAELDALQERR--------------------EALQRLAE----YSWDEIDVASAEREI---- 670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  481 lshesADGDSRLREVRVTDEDVDALKQ---DLQRALEESKRDKARVQELETKLvEKEKAEATkpssEVCEEMRNSYCSVI 557
Cdd:COG4913   671 -----AELEAELERLDASSDDLAALEEqleELEAELEELEEELDELKGEIGRL-EKELEQAE----EELDELQDRLEAAE 740
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  558 ENMNKEKAFLFEKYQQAQeeimkLKDTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDyrkrkS 637
Cdd:COG4913   741 DLARLELRALLEERFAAA-----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA-----D 810
                         250
                  ....*....|....*.
gi 564335600  638 LEDATEYihRAEHERL 653
Cdd:COG4913   811 LESLPEY--LALLDRL 824
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
403-887 6.85e-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: 43.80  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   403 QLQDTLHDlqkRLETSEAEKKQLQDELQSQRtdttclnnteISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGLLS 482
Cdd:TIGR00618  212 CMPDTYHE---RKQVLEKELKHLREALQQTQ----------QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   483 HESADGDSRLR----EVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIE 558
Cdd:TIGR00618  279 LEETQERINRArkaaPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   559 NMNKEKAFLFEKYQQAQEEIMKLKdtlksqmpqeapddsgDMKETMNRMVDELNKQVSELSQLYRE-AQAELEDYRKrks 637
Cdd:TIGR00618  359 DAHEVATSIREISCQQHTLTQHIH----------------TLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAF--- 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   638 ledateyihRAEHERLMHLsnlsRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTMAKEME 717
Cdd:TIGR00618  420 ---------RDLQGQLAHA----KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   718 EKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESevnalAAKLKESVKEKEkahsevAQVRSEV 797
Cdd:TIGR00618  487 RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQLETSEEDVY------HQLTSER 555
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   798 SQAKREKENIQTLlkskEQEVTELVQKFQRAQEELAGLKRCSET----SSKLEEDKDEKINEMTKEVLKLKEALNSLSQL 873
Cdd:TIGR00618  556 KQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITVRlqdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
                          490
                   ....*....|....
gi 564335600   874 SYSTSSSKRQTQQL 887
Cdd:TIGR00618  632 LHLQQCSQELALKL 645
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
394-910 7.39e-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: 43.42  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   394 TADRDVIIQQLQDTLHDLQKrLETSEAEKKQLQDELQSQRTDTTCLNNTEISENGSDLSQKL-KDTQSKYEEAMKEVLSV 472
Cdd:TIGR00618  375 HTLTQHIHTLQQQKTTLTQK-LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQC 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   473 QKQMKLGLlsHESAdgdSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNS 552
Cdd:TIGR00618  454 EKLEKIHL--QESA---QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   553 YCSVIENMNKEKAFLFEKYQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEDY 632
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   633 RKRKSLEdateyihRAEHERLMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKENSVSITEHLEVITTLRTM 712
Cdd:TIGR00618  608 DMLACEQ-------HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   713 AKEMEEktvTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQ 792
Cdd:TIGR00618  681 ALQKMQ---SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK 757
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   793 VRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEA--LNSL 870
Cdd:TIGR00618  758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEqfLSRL 837
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 564335600   871 SQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLAECKKQHQE 910
Cdd:TIGR00618  838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
760-867 7.83e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 760 KLQAsLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE--------- 830
Cdd:COG1579   11 DLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnk 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564335600 831 -------ELAGLKRCSETSSKLEEDKDEKINEMTKEVLKLKEAL 867
Cdd:COG1579   90 eyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
106-196 8.42e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 106 LQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPLLVAIQNGHSEACHFLLDHGADVNSRDKNG 185
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANG 591
                         90
                 ....*....|.
gi 564335600 186 RTALMLACETG 196
Cdd:PLN03192 592 NTALWNAISAK 602
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
591-868 8.51e-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: 43.52  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   591 QEAPDDSGDMKETMNRMVDELNKQVSELSQLyreaqaeledyrkRKSLEDATEYIHRAEHERLMHLSNLSRTKAEesLSD 670
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDEL-------------SQELSDASRKIGEIEKEIEQLEQEEEKLKER--LEE 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   671 MRSQYSKVLNELTQLKQLVDahkENSVSITEHLEVITTLRTMAKEMEEKTvtLQEHLASKEGEVAKLEKQLAEEKAAMSD 750
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLRE 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   751 amvpkasyeklqasLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQE 830
Cdd:TIGR02169  817 --------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 564335600   831 ELAGLKR-CSETSSKLEEDKDeKINEMTKEVLKLKEALN 868
Cdd:TIGR02169  883 RLGDLKKeRDELEAQLRELER-KIEELEAQIEKKRKRLS 920
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
389-862 9.21e-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: 43.27  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  389 PAGTSTADRDVIIQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNTEISENGSDLsqklKDTQSKYEEAMKE 468
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEM----KDTKISSLERNIR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  469 VLSVQKQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVE--------KEKAEATK 540
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETltnqnsdcKQHIEVLK 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  541 PSSEVCEEMRNSYCSVIENMN---KEKAFLFEKYQQAQEEIMKLKDTLKSQMpqeapDDSGDMKETMNRMVDELNKQVSE 617
Cdd:pfam10174 331 ESLTAKEQRAAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEI-----RDLKDMLDVKERKINVLQKKIEN 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  618 LSQLYREAQAELEDYRKR-KSLEDATEYihraeherlmhlSNLSRTKAEESLSDMrsqySKVLNELTQLKQLVDahkens 696
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERvKSLQTDSSN------------TDTALTTLEEALSEK----ERIIERLKEQRERED------ 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  697 vsiTEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEkqlaEEKAAMSDAMVPKASYEKlqaSLESEVNALAAKL 776
Cdd:pfam10174 464 ---RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLK---SLEIAVEQKKEEC 533
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  777 KESVKEKEKAHsevaqvrsEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEM 856
Cdd:pfam10174 534 SKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL 605

                  ....*.
gi 564335600  857 TKEVLK 862
Cdd:pfam10174 606 ESLTLR 611
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
64-189 9.47e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 9.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  64 GHVECLKVMVTHgvDVTAQDSSGHSALHIAA---KNGHPEYIKKLLQYKSPAESVDNL-----------GKTALHYAAAQ 129
Cdd:cd21882    6 GLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIEN 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335600 130 GSLQAVQVLCEH--------------KSPINLKDLdGNIPLLVAIQNGHSEACHFLLDHGADVNS---RDKNGRTAL 189
Cdd:cd21882   84 RNLNLVRLLVENgadvsaratgrffrKSPGNLFYF-GELPLSLAACTNQEEIVRLLLENGAQPAAleaQDSLGNTVL 159
PTZ00121 PTZ00121
MAEBL; Provisional
484-910 1.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  484 ESADGDSRLREVRVTDEDVDAL---KQDLQRALEESKRDKARVQELETKLVEKEKA-EATKPSSEVCEEMRNSYCSVIEN 559
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNhegKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRAdEATEEAFGKAEEAKKTETGKAEE 1113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  560 MNKEKAFLfEKYQQAQ--EEIMKLKDTLKSQMPQEAPDDSgdMKETMNRMVDELNKQVSELSQLYREAQA---------- 627
Cdd:PTZ00121 1114 ARKAEEAK-KKAEDARkaEEARKAEDARKAEEARKAEDAK--RVEIARKAEDARKAEEARKAEDAKKAEAarkaeevrka 1190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  628 ----ELEDYRK-----RKSLEDATEYIHRAEHER---LMHLSNLSRTKAEESLSDMRSQYSKVLNELTQLKQLVDAHKEN 695
Cdd:PTZ00121 1191 eelrKAEDARKaeaarKAEEERKAEEARKAEDAKkaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  696 SVSITEHLEVITTLRTM-------AKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAMVPKASYEKLQASLESE 768
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEekkkadeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  769 VNALAAKLKESVKEKEKA---HSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEElagLKRCSETSSKL 845
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKA 1427
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335600  846 EE-DKDEKINEMTKEVLKLKEALNSLSQLSYSTSSSKRQTQQLEMLQQQVKQLQNQLA-ECKKQHQE 910
Cdd:PTZ00121 1428 EEkKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEE 1494
PHA02946 PHA02946
ankyin-like protein; Provisional
101-326 1.06e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 101 YIKKLLQYKSPAESVDNLGKTALHYAAAQGSLQAVQVLCEHKSPINLKDLDGNIPL--LVAIQNGHSEACHFLLDHGADV 178
Cdd:PHA02946  54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 179 NSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSEN------AGIQSLLLSKISQDADLKTPTK 252
Cdd:PHA02946 134 NNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkastiSWMMKLGISPSKPDHDGNTPLH 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 253 ---AKQLSDVSSPRSITSTPLSGKESVfFAEAPFKAEISSIQE----NKdRLSDSTAGADSLLDVSSEADQQDLLVLLQA 325
Cdd:PHA02946 214 ivcSKTVKNVDIINLLLPSTDVNKQNK-FGDSPLTLLIKTLSPahliNK-LLSTSNVITDQTVNICIFYDRDDVLEIIND 291

                 .
gi 564335600 326 K 326
Cdd:PHA02946 292 K 292
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
498-868 1.35e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  498 TDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKPSS------------EVCEEMRNSYCSVIENMNKEKA 565
Cdd:pfam06160  98 IEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSygpaidelekqlAEIEEEFSQFEELTESGDYLEA 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  566 flFEKYQQAQEEImklkDTLKSQMPqeapddsgDMKETMNRMVDELNKQVSELSQLYREAQAE---LEDYRKRKSLEDAT 642
Cdd:pfam06160 178 --REVLEKLEEET----DALEELME--------DIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVDKEIQQLE 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  643 EYIHRAeherLMHLSNLSRTKAEESLSDMRSQyskvLNEL-TQLKQLVDAHKEnsvsITEHLEVITTLRTMAKEMEEKTV 721
Cdd:pfam06160 244 EQLEEN----LALLENLELDEAEEALEEIEER----IDQLyDLLEKEVDAKKY----VEKNLPEIEDYLEHAEEQNKELK 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  722 TLQEHLaskegevaKLEKQLAEEKAamsdamvpkASYEKLQASLEsEVNALAAKLKESVKEKEKAHSEvaqVRSEVSQAK 801
Cdd:pfam06160 312 EELERV--------QQSYTLNENEL---------ERVRGLEKQLE-ELEKRYDEIVERLEEKEVAYSE---LQEELEEIL 370
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600  802 REKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKR-CSETSSKLE--------EDKDEKINEMTKEVLKLKEALN 868
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLeLREIKRLVEksnlpglpESYLDYFFDVSDEIEDLADELN 446
PRK09039 PRK09039
peptidoglycan -binding protein;
402-530 1.59e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 402 QQLQDTLHDLQKRLETSEAEKKQLQDELqsqrtdttclnnTEISENGSDLSQKLKDtqskyeeaMKEVLSVQKQmklglL 481
Cdd:PRK09039  77 QDLQDSVANLRASLSAAEAERSRLQALL------------AELAGAGAAAEGRAGE--------LAQELDSEKQ-----V 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564335600 482 SHESadgdsrLREVRVTDEDVDALKQ---DLQRALEES-KRDK---ARVQELETKL 530
Cdd:PRK09039 132 SARA------LAQVELLNQQIAALRRqlaALEAALDASeKRDResqAKIADLGRRL 181
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
507-865 1.81e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.02  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  507 QDLQRALEESkRDKARVQELETKLVEKEKAEATKPSSEVCEEMRNSYCSVIENMNKEKAfLFEKYQQAQEEIMKLKDTLK 586
Cdd:pfam05483 257 KDLTFLLEES-RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA-LEEDLQIATKTICQLTEEKE 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  587 SQMpqeapDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELED------------YRKRKSLEDATEYIHRAEHErlm 654
Cdd:pfam05483 335 AQM-----EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiitmelQKKSSELEEMTKFKNNKEVE--- 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  655 hLSNLSRTKAE-ESLSDMRSQYSKVLNEL------------TQLKQLVDAHKENSVSITEHLEVITTLRTMAKEMEEKTV 721
Cdd:pfam05483 407 -LEELKKILAEdEKLLDEKKQFEKIAEELkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  722 TLQEhLASKEGEVAKLEKQLAEEKAAMS--------DAMVPKASYEKL----------QASLESEVNALAAKLKESVKEK 783
Cdd:pfam05483 486 KNIE-LTAHCDKLLLENKELTQEASDMTlelkkhqeDIINCKKQEERMlkqienleekEMNLRDELESVREEFIQKGDEV 564
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  784 ----EKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSETSSKLEEDKDEKINEMTKE 859
Cdd:pfam05483 565 kcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644

                  ....*.
gi 564335600  860 VLKLKE 865
Cdd:pfam05483 645 LASAKQ 650
PHA02876 PHA02876
ankyrin repeat protein; Provisional
160-230 1.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600 160 IQNGHSEACHFLLDHGADVNSRDKNGRTALMLACETGSANTVEALIKKGADLNLVDSLGHNALYYSKLSEN 230
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
670-836 2.26e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.20  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 670 DMRSQYSKVLNELTQLKQLVDAhKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMS 749
Cdd:cd22656   88 TIDSYYAEILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALK 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 750 D------AMVPKASYEKLQASLESEVNALAAKLKESVKEKEKahsEVAQVRSEVSQAKRekenIQTLLKSKEQEVTELVQ 823
Cdd:cd22656  167 DlltdegGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKA---LIADDEAKLAAALR----LIADLTAADTDLDNLLA 239
                        170
                 ....*....|...
gi 564335600 824 KFQRAQEELAGLK 836
Cdd:cd22656  240 LIGPAIPALEKLQ 252
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
404-867 2.43e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 41.55  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  404 LQDTLHDLQKRLETSEAEKKQLQDELQSqrtdttclNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKqMKLGLLSH 483
Cdd:pfam05701  47 VQEEIPEYKKQSEAAEAAKAQVLEELES--------TKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEE-MEQGIADE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  484 ESADGDSRLR-----------EVRVTDEDVDALKQDLQRALEESKRDKARVQE--LETKLVEKEKAEATK---PSSEVCE 547
Cdd:pfam05701 118 ASVAAKAQLEvakarhaaavaELKSVKEELESLRKEYASLVSERDIAIKRAEEavSASKEIEKTVEELTIeliATKESLE 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  548 EMRNSYCSVIEN-----MNKEKAFL-FEK-YQQAQEEIMKLKDTLKSQMPQEAPDDSG-----DMK-ETMNRMVDELNK- 613
Cdd:pfam05701 198 SAHAAHLEAEEHrigaaLAREQDKLnWEKeLKQAEEELQRLNQQLLSAKDLKSKLETAsalllDLKaELAAYMESKLKEe 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  614 --QVSELSQLYREAQAELEdyRKRKSLEDATEYIHRAEHErlmhlSNLSRTKAEEslsdMRSQYSKVLNELTQLKQLVDA 691
Cdd:pfam05701 278 adGEGNEKKTSTSIQAALA--SAKKELEEVKANIEKAKDE-----VNCLRVAAAS----LRSELEKEKAELASLRQREGM 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  692 HKENSVSITEHLEV----ITTLRTMAKEMEEKTVTLQEHL--ASKEGEVAKLEKQLAEE--KAAMSDAMVPKASYEKLQA 763
Cdd:pfam05701 347 ASIAVSSLEAELNRtkseIALVQAKEKEAREKMVELPKQLqqAAQEAEEAKSLAQAAREelRKAKEEAEQAKAAASTVES 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  764 SLESevnalAAKLKESVKEKEKAHSEVAQV--RSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAqEELAGlKRCSET 841
Cdd:pfam05701 427 RLEA-----VLKEIEAAKASEKLALAAIKAlqESESSAESTNQEDSPRGVTLSLEEYYELSKRAHEA-EELAN-KRVAEA 499
                         490       500       510
                  ....*....|....*....|....*....|..
gi 564335600  842 SSKLEEDKD------EKINEMTKEVLKLKEAL 867
Cdd:pfam05701 500 VSQIEEAKEselrslEKLEEVNREMEERKEAL 531
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
755-862 2.75e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 39.61  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 755 KASYEKLQASLESEVNALAAKLKESVKEKEKAHSEVAQVrsevsqakreKENIQTLLKSKEQEVTELVQKF-QRAQEELA 833
Cdd:PRK08475  48 KNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEA----------KEKAELIVETAKKEAYILTQKIeKQTKDDIE 117
                         90       100
                 ....*....|....*....|....*....
gi 564335600 834 GLKRCSETSSKLEEDKDEKinEMTKEVLK 862
Cdd:PRK08475 118 NLIKSFEELMEFEVRKMER--EVVEEVLN 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
155-179 3.39e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 3.39e-03
                          10        20
                  ....*....|....*....|....*
gi 564335600  155 PLLVAIQNGHSEACHFLLDHGADVN 179
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
21-81 3.54e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335600  21 DRLLQAVENGDAEKVASLLgKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTA 81
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
CagA_N pfam18971
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...
611-854 3.63e-03

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.


Pssm-ID: 408741 [Multi-domain]  Cd Length: 876  Bit Score: 41.30  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  611 LNKQVSELSQL-----YREAQAELE-DYRKRKSLEDATEYIHRAEHerlmhlSNLSRTKAEESLSDMRSQYSKVLNELTQ 684
Cdd:pfam18971 596 FNKAVAEAKSTgnydeVKKAQKDLEkSLRKREHLEKEVEKKLESKS------GNKNKMEAKAQANSQKDEIFALINKEAN 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  685 LKQLVDAHKENSVSITEHLEviTTLRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpkasyeKLQAS 764
Cdd:pfam18971 670 RDARAIAYTQNLKGIKRELS--DKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDL--------GINPE 739
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  765 LESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKRE---KENIQTLLKSKEQEVT--ELVQKFQRAQEELAGLKRCS 839
Cdd:pfam18971 740 WISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDviiNQKVTDKVDNLNQAVSvaKAMGDFSRVEQVLADLKNFS 819
                         250
                  ....*....|....*
gi 564335600  840 ETSSKLEEDKDEKIN 854
Cdd:pfam18971 820 KEQLAQQAQKNEDFN 834
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
401-637 3.94e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTTCLNNT--EISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKL 478
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 479 GLLSHESADGDSRLrEVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLVEKEKAEATKpssevcEEMRNSYCSVIE 558
Cdd:COG4942  109 LLRALYRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL------EAERAELEALLA 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335600 559 NMNKEKAFLFEKYQQAQEEIMKLKDTLKSQmpqeapddsgdmketmNRMVDELNKQVSELSQLYREAQAELEDYRKRKS 637
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAEL----------------AAELAELQQEAEELEALIARLEAEAAAAAERTP 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
475-852 3.99e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  475 QMKLGLLSHESaDGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQELETKLveKEKAEATKPSSEVCEEMRnsyc 554
Cdd:COG4913   582 QVKGNGTRHEK-DDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEAL--EAELDALQERREALQRLA---- 654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  555 svienmnkEKAFLFEKYQQAQEEIMKLKDTLksqmpqEAPDDSGDMKETMNRMVDELNKQVSELSQLYREAQAELEdyRK 634
Cdd:COG4913   655 --------EYSWDEIDVASAEREIAELEAEL------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG--RL 718
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  635 RKSLEDATEYIHRAEhERLMHLSNLSRTKAEESLSDMRSQyskvlneltqlkQLVDAHkensvsitehlevittLRTMAK 714
Cdd:COG4913   719 EKELEQAEEELDELQ-DRLEAAEDLARLELRALLEERFAA------------ALGDAV----------------ERELRE 769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  715 EMEEKTVTLQEHLASKEGEVAKLEKQLAEE-KAAMSDAMVPKASYEKLQASLESEVN----ALAAKLKESVKEKEKAhsE 789
Cdd:COG4913   770 NLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLALLDRLEEdglpEYEERFKELLNENSIE--F 847
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  790 VAQVRSEVSQAKRE-KENIQTL----------------LKSKEQEVTElVQKFQRAqeelagLKRCSETSSKLEEDKDEK 852
Cdd:COG4913   848 VADLLSKLRRAIREiKERIDPLndslkripfgpgrylrLEARPRPDPE-VREFRQE------LRAVTSGASLFDEELSEA 920
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
86-109 4.12e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.12e-03
                           10        20
                   ....*....|....*....|....
gi 564335600    86 GHSALHIAAKNGHPEYIKKLLQYK 109
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKG 25
PRK09039 PRK09039
peptidoglycan -binding protein;
677-830 4.32e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 677 KVLNELT-QLKQLVDAHKensvsitehLEvittlRTMAKEMEEKTVTLQEHLASKEGEVAKLEKQLAEEKAAMSDAmvpk 755
Cdd:PRK09039  53 SALDRLNsQIAELADLLS---------LE-----RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA---- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 756 asyeklqaslESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLL-----KSKEQEVT--ELVQKF--- 825
Cdd:PRK09039 115 ----------EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekRDRESQAKiaDLGRRLnva 184

                 ....*..
gi 564335600 826 --QRAQE 830
Cdd:PRK09039 185 laQRVQE 191
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
510-832 4.36e-03

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: 40.88  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  510 QRALEESKRDKARVQELETKLVEKEKAEATKpssevceemrnsycsvienMNKEKAFLFEKYQQAQEEIMKLKDTLKSQM 589
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAE-------------------MDRQAAIYAEQERMAMERERELERIRQEER 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  590 PQEAPD-DSGDMKETMNRMvDELNKQVSELSQLYREAQAELEDYRKRKSLEDATEyihRAEHERLMHLSNLSRTKAEESL 668
Cdd:pfam17380 359 KRELERiRQEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQ---RKIQQQKVEMEQIRAEQEEARQ 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  669 SDMRSQYSKVLNELTQLKQlVDAHKENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKegevaKLEKQLAEEKAAM 748
Cdd:pfam17380 435 REVRRLEEERAREMERVRL-EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK-----ILEKELEERKQAM 508
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  749 SD-----AMVPKASYEKLQASLESEVNALAaklkESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLlkSKEQEVTELVQ 823
Cdd:pfam17380 509 IEeerkrKLLEKEMEERQKAIYEEERRREA----EEERRKQQEMEERRRIQEQMRKATEERSRLEAM--EREREMMRQIV 582

                  ....*....
gi 564335600  824 KFQRAQEEL 832
Cdd:pfam17380 583 ESEKARAEY 591
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
32-124 5.03e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600  32 AEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLKVMVTHGVDVTAQDSS--------------GHSALHIAAKNG 97
Cdd:cd22193   55 AEKTDNLKRFINAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTN 134
                         90       100       110
                 ....*....|....*....|....*....|
gi 564335600  98 HPEYIKKLLQ---YKSPAESVDNLGKTALH 124
Cdd:cd22193  135 QPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
401-628 5.45e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 401 IQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTtclNNTEISENGSDLSQKLKDTQSKYEEAMKEVLSVQKQMKLGL 480
Cdd:COG3206  177 LEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE---EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 481 LSHESADGDSRLREVRvtdEDVDALKQDLQRALEESKRDKARVQELETKL--VEKEKAEATKpssEVCEEMRNSYcsvie 558
Cdd:COG3206  254 DALPELLQSPVIQQLR---AQLAELEAELAELSARYTPNHPDVIALRAQIaaLRAQLQQEAQ---RILASLEAEL----- 322
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600 559 nmnkekaflfEKYQQAQEEIMKLKDTLKSQMpQEAPDDSGDMKEtMNRMVDELNKQVSELSQLYREAQAE 628
Cdd:COG3206  323 ----------EALQAREASLQAQLAQLEARL-AELPELEAELRR-LEREVEVARELYESLLQRLEEARLA 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-653 5.50e-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: 40.81  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   314 ADQQDLLVLLQAKVASLtlhNKELQDKLQAKSPKETEADLSFQSFHSTQTDLAPSPSKSSDIPSSDAKSSPPVEhpagts 393
Cdd:TIGR02168  687 EELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT------ 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   394 taDRDVIIQQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTDTtclnnTEISENGSDLSQKLKDTQSKYEeamkevlsvQ 473
Cdd:TIGR02168  758 --ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREALDELRAELTLLNEEAA---------N 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   474 KQMKLGLLSHESADGDSRLREVRVTDEDVDALKQDLQRALEESKRDKARVQElETKLVEKEKAEATKPSSEVCEEMRNSY 553
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   554 cSVIENMNKEKAFLFEKYQQAQEEIMKLK----------DTLKSQMPQEAPDDSGDMKETMNRMVDELNKQVSELSQLYR 623
Cdd:TIGR02168  901 -EELRELESKRSELRRELEELREKLAQLElrleglevriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 564335600   624 E----------AQAELEDYRKR---------------KSLEDATEYIHRAEHERL 653
Cdd:TIGR02168  980 KikelgpvnlaAIEEYEELKERydfltaqkedlteakETLEEAIEEIDREARERF 1034
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
52-79 6.42e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 6.42e-03
                          10        20
                  ....*....|....*....|....*...
gi 564335600   52 EGKTAFHLAAAKGHVECLKVMVTHGVDV 79
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
402-856 7.08e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 7.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   402 QQLQDTLHDLQKRLETSEAEKKQLQDELQSQRTD----TTCLNNTE-----ISENGSDLSQKLKDTQSKYEEAMKEVLSV 472
Cdd:pfam01576  408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEgknikLSKDVSSLESQLQDTQELLQEETRQKLNL 487
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   473 QKQMK---------LGLLSHESADGDSRLREVRVTDEDVDALKQDLQR------ALEESKRDKAR-----VQELETKLVE 532
Cdd:pfam01576  488 STRLRqledernslQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagtleALEEGKKRLQRelealTQQLEEKAAA 567
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   533 KEKAEATKpssevcEEMRNSYCSVIENMNKEKAFL--FEKYQQAQEEIMKLKDTLKSQMPQEAPDDSGDMKE------TM 604
Cdd:pfam01576  568 YDKLEKTK------NRLQQELDDLLVDLDHQRQLVsnLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREketralSL 641
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   605 NRMVDELNKQVSELSQLYREAQAELEDYRKRKslEDATEYIHRAEHerlmhlsnlSRTKAEESLSDMRsqyskvlnelTQ 684
Cdd:pfam01576  642 ARALEEALEAKEELERTNKQLRAEMEDLVSSK--DDVGKNVHELER---------SKRALEQQVEEMK----------TQ 700
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   685 LKQLVDahkENSVSITEHLEVITTLRTMAKEMEEKTVTLQEHLASKEGEVAK----LEKQLAEEKAAMSDAMVPKASYEK 760
Cdd:pfam01576  701 LEELED---ELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKqvreLEAELEDERKQRAQAVAAKKKLEL 777
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335600   761 LQASLESEVNALAAKLKESVKEKEKAHSEVAQVRSEVSQAKREKENIQTLLKSKEQEVTELVQKFQRAQEELAGLKRCSE 840
Cdd:pfam01576  778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARR 857
                          490
                   ....*....|....*.
gi 564335600   841 TSsklEEDKDEKINEM 856
Cdd:pfam01576  858 QA---QQERDELADEI 870
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
119-146 8.63e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 8.63e-03
                          10        20
                  ....*....|....*....|....*...
gi 564335600  119 GKTALHYAAAQGSLQAVQVLCEHKSPIN 146
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
86-108 8.71e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 8.71e-03
                          10        20
                  ....*....|....*....|...
gi 564335600   86 GHSALHIAAKNGHPEYIKKLLQY 108
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLEN 24
 
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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