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Conserved domains on  [gi|160358772|sp|Q6UB98|]
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RecName: Full=Ankyrin repeat domain-containing protein 12; AltName: Full=Ankyrin repeat-containing cofactor 2; AltName: Full=GAC-1 protein

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];
173-291 6.88e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  173 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160358772  253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
PTZ00121 super family cl31754
MAEBL; Provisional
 720-1165 7.02e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  720 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 799
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  800 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 879
Cdd:PTZ00121 1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  880 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 959
Cdd:PTZ00121 1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  960 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1039
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772 1040 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1119
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 160358772 1120 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1165
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 363-983 1.41e-03

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


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   363 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 442
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   443 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 522
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   523 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 602
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   603 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 669
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   670 EGEKEKyktKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 744
Cdd:pfam02463  720 EELLAD---RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   745 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 823
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   824 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 903
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   904 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 983
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-291 6.88e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  173 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160358772  253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-277 1.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   189 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 268
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 160358772   269 LLLRHGGNP 277
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 178-290 5.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160358772  254 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 290
Cdd:PHA03095  120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
PTZ00121 PTZ00121
MAEBL; Provisional
 720-1165 7.02e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  720 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 799
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  800 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 879
Cdd:PTZ00121 1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  880 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 959
Cdd:PTZ00121 1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  960 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1039
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772 1040 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1119
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 160358772 1120 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1165
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 716-1049 1.53e-08

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 60.37  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   716 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 795
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   796 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 874
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   875 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 954
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   955 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1032
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 160358772  1033 HKDKIQINSLLKLKSEA 1049
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 185-256 1.13e-05

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: 50.40  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  185 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 250
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 160358772  251 DDTPLH 256
Cdd:cd22192   169 GNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 218-245 2.85e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 2.85e-05
                            10        20
                    ....*....|....*....|....*...
gi 160358772    218 GWTPLHEACNVGYYDVAKILIAAGADVN 245
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 719-983 1.40e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   719 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 793
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   794 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 867
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   868 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 947
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 160358772   948 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 983
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 363-983 1.41e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   363 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 442
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   443 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 522
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   523 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 602
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   603 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 669
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   670 EGEKEKyktKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 744
Cdd:pfam02463  720 EELLAD---RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   745 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 823
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   824 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 903
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   904 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 983
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-291 6.88e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  173 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160358772  253 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
174-291 1.83e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  174 QKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 160358772  254 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-311 8.45e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 8.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 160358772  258 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDE 311
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-291 7.52e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  175 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 254
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 160358772  255 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
189-277 1.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   189 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 268
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 160358772   269 LLLRHGGNP 277
Cdd:pfam12796   79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-286 1.33e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                          90       100
                  ....*....|....*....|....*....
gi 160358772  258 SASSGHRDIVKLLLRHGGNPFQANKHGER 286
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 178-290 5.32e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160358772  254 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 290
Cdd:PHA03095  120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-247 3.50e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 3.50e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   178 VNKRNERGETPLHMAAIRGDVKQVKELISlGANVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 247
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 177-291 6.95e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  177 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 160358772  257 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-276 1.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  120 STPVSILFGYPLSERKQM---ALLMQMTARDNSPDSTPNHPSQTTPAQKKTPSS-----SSRQKDkVNKRNERGETPLHM 191
Cdd:PHA03100   69 STPLHYLSNIKYNLTDVKeivKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSiveylLDNGAN-VNIKNSDGENLLHL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  192 AAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 253
Cdd:PHA03100  148 YLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                         170       180
                  ....*....|....*....|...
gi 160358772  254 PLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 147-276 1.24e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  147 DNSPDSTPNHPSQTTPAQKKTPSSSSRQKDkVNKRNERGETPLHMAAIRG-DVKQVKELISLGANVNVKDFAGWTPLHEA 225
Cdd:PHA02876  270 DDCKNTPLHHASQAPSLSRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQA 348

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 160358772  226 CNVGYY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA02876  349 STLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-284 2.56e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 72.24  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  116 GNKKSTPVSILFgyplserKQMALLMQMTARDNSPDSTpnhpSQTTPAQKKTPSSSSRQKDKVNkrnergETPLHMAAIR 195
Cdd:PTZ00322   23 GSRKRRAKPISF-------ERMAAIQEEIARIDTHLEA----LEATENKDATPDHNLTTEEVID------PVVAHMLTVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  196 -------GDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVK 268
Cdd:PTZ00322   86 lcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                         170
                  ....*....|....*.
gi 160358772  269 LLLRHGGNPFQANKHG 284
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
175-291 1.02e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  175 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 254
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 160358772  255 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 146-291 2.17e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  146 RDNSPDSTPNHPSQTTPAQKKTPSSSSRQKdKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 225
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  226 cnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02878  242 --VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 178-291 2.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 257
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 160358772  258 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PHA02874  261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 178-274 6.86e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNE-RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:PHA02878  160 INMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90
                  ....*....|....*....
gi 160358772  257 DSASS-GHRDIVKLLLRHG 274
Cdd:PHA02878  240 ISVGYcKDYDILKLLLEHG 258
PTZ00121 PTZ00121
MAEBL; Provisional
 720-1165 7.02e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  720 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 799
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  800 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 879
Cdd:PTZ00121 1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  880 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 959
Cdd:PTZ00121 1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  960 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1039
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772 1040 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1119
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 160358772 1120 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1165
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 186-273 7.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 7.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  186 ETPLHMAAIRGDVKQVKELISLGANVN---VKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 262
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90
                  ....*....|.
gi 160358772  263 HRDIVKLLLRH 273
Cdd:PHA02875  147 DIKGIELLIDH 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 178-287 9.81e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 9.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLH--MAAIRGDVKQVKELISLGANVNVKDFAGWTPLH-----EACNVgyyDVAKILIAAGADVNTQGLD 250
Cdd:PHA03095  110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVDDR 186

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 160358772  251 DDTPLHDSASSGHRD--IVKLLLRHGGNPFQANKHGERP 287
Cdd:PHA03095  187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 197-276 1.61e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  197 DVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 272
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105


                  ....
gi 160358772  273 HGGN 276
Cdd:PHA03095  106 AGAD 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
187-238 1.64e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160358772   187 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 238
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
218-271 2.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.14e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 160358772   218 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 271
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00121 PTZ00121
MAEBL; Provisional
 734-1068 1.37e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  734 KSTKEKHVSKERNFKEER--DKIKKESEKSFREEKIKDLKEERENIPTDKdseftslgmsaIEESIGLHLVEKEIDIEKQ 811
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRK-----------FEEARMAHFARRQAAIKAE 1275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  812 EKHIKESKEKPEKRSQIKEKDIEKMERKTFEKekkikhehkseKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNT 891
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEA-----------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  892 AAIKKTDDrEKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESin 971
Cdd:PTZ00121 1345 AEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-- 1421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  972 itNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQinsllKLKSEADK 1051
Cdd:PTZ00121 1422 --EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEE 1494

                         330
                  ....*....|....*..
gi 160358772 1052 PKPKSSPASKDTRPKEK 1068
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKK 1511
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 716-1049 1.53e-08

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 60.37  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   716 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 795
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   796 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 874
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   875 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 954
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   955 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1032
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 160358772  1033 HKDKIQINSLLKLKSEA 1049
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 197-291 2.60e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  197 DVKQVKELISLGANVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 275
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90
                  ....*....|....*.
gi 160358772  276 NPFQANKHGERPVDVA 291
Cdd:PHA02878  226 STDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 177-246 3.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.17e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  177 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 246
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00121 PTZ00121
MAEBL; Provisional
 369-1004 1.28e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  369 EEINKMIDDRHIlRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTSCSVIPE 448
Cdd:PTZ00121 1191 EELRKAEDARKA-EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  449 TS-NSDMQTKKEYVVSGEHKQKGKVKRKLKNQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFRKSFSP 527
Cdd:PTZ00121 1270 AAiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  528 KDDTSlhlfhistgKSPKHSCGLSEKQSTPLKQEHTKTclspGSSEMSLQPDLVR-YDNTESEFLPESSSVKSCKHKEKS 606
Cdd:PTZ00121 1350 AEAEA---------AADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKkADEAKKKAEEDKKKADELKKAAAA 1416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  607 KHQKDfhlEFGEKSNAKIKDEDHSPTFENSdctlKKMDKEGKTLKKHKLKHKEREKEKHKKEIEGEKEKYKTKDSAKELQ 686
Cdd:PTZ00121 1417 KKKAD---EAKKKAEEKKKADEAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  687 RSVEFDREFWKENFFKSDE---TEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKI--KKESEKS 761
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeeKKKAEEA 1569

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  762 FREekikdlkEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEkqekhikESKEKPEKRSQIKEKDIEKMERKTF 841
Cdd:PTZ00121 1570 KKA-------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-------EAKKAEEAKIKAEELKKAEEEKKKV 1635

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  842 EKEKKIKHEHKSEKDKLDLSECVDKIKEKDklyshhtEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD--------K 913
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAE-------EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakkaeelK 1708

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  914 EKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQ 993
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788

                         650
                  ....*....|.
gi 160358772  994 HEKPLSLKEKT 1004
Cdd:PTZ00121 1789 DEKRRMEVDKK 1799
Ank_5 pfam13857
Ankyrin repeats (many copies);
178-225 2.14e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 2.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 160358772   178 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 225
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 118-275 2.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  118 KKSTPVSILF--GYplsERKQMALLMQMTARDNSPDS---TPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMA 192
Cdd:PHA02876  306 KGETPLYLMAknGY---DTENIRTLIMLGADVNAADRlyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYA 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  193 AIRGDV----------------------------------KQVKELISLGANVNVKDFAGWTPLHEAC-NVGYYDVAKIL 237
Cdd:PHA02876  383 AVRNNVviintlldygadiealsqkigtalhfalcgtnpyMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEML 462

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 160358772  238 IAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 275
Cdd:PHA02876  463 LDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
177-255 2.98e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 2.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160358772  177 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 255
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 187-276 3.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  187 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 265
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216

                          90
                  ....*....|.
gi 160358772  266 IVKLLLRHGGN 276
Cdd:PHA02875  217 IVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 189-252 5.09e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 5.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160358772  189 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 252
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 184-285 1.14e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  184 RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 246
Cdd:PLN03192  557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 160358772  247 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 285
Cdd:PLN03192  637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 708-1007 1.51e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.51  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  708 DLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSK--ERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTdkdsef 785
Cdd:PTZ00108 1089 DYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKT------ 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  786 tslgmsaieesiglhlveKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVD 865
Cdd:PTZ00108 1163 ------------------KGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSD 1224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  866 KIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKtdDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSK 945
Cdd:PTZ00108 1225 QEDDEEQKTKPKKSSVKRLKSKKNNSSKSSE--DNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP 1302

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160358772  946 SEKGKNKEKDRE---LDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDE 1007
Cdd:PTZ00108 1303 SSPTKKKVKKRLegsLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 178-284 2.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  178 VNKRNERGETPLHMAAIRGDVKQ--VKELISLGANVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 246
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 160358772  247 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 284
Cdd:PHA02859  119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
237-291 2.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 160358772   237 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 143-272 3.02e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  143 MTARDNSPDSTPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDVK--QVKELISLGANVNVKDFAGWT 220
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 160358772  221 PLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLR 272
Cdd:PHA03095  260 PLHYA---AVFNnprACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 184-215 5.39e-06

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: 44.97  E-value: 5.39e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 160358772   184 RGETPLHMAAIR-GDVKQVKELISLGANVNVKD 215
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00121 PTZ00121
MAEBL; Provisional
 666-1064 5.62e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  666 KKEIEGEKEKYKTKDSAKELQRSVEFDR--EFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDD---KSTKEKH 740
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeakKKAEEAK 1483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  741 VSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKhIKESKE 820
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE-LKKAEE 1562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  821 KPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKE--KDKLYSHHTEKCHKEGEKSKNTAAIKKTD 898
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  899 DREKSREKMDRKHDKEKPEKERHLAESKEkhlmEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHI 978
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  979 QEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSP 1058
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798


                  ....*.
gi 160358772 1059 ASKDTR 1064
Cdd:PTZ00121 1799 KIKDIF 1804
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 183-291 7.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  183 ERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 262
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100
                  ....*....|....*....|....*....
gi 160358772  263 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 291
Cdd:PHA02875  180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 185-256 1.13e-05

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: 50.40  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  185 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 250
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 160358772  251 DDTPLH 256
Cdd:cd22192   169 GNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 234-291 1.18e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160358772  234 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 291
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
698-1007 1.35e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  698 ENFFKSDETED----LFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFRE-----EKIK 768
Cdd:PRK03918  138 DAILESDESREkvvrQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineisSELP 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  769 DLKEERENIPTDKDSeftslgMSAIEESIGlhlvEKEIDIEKQEKHIKESKEK---PEKRSQIKEKDIEKMERKTfekek 845
Cdd:PRK03918  218 ELREELEKLEKEVKE------LEELKEEIE----ELEKELESLEGSKRKLEEKireLEERIEELKKEIEELEEKV----- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  846 kikhehksekdkldlsECVDKIKEKDKLYS--------HHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD---KE 914
Cdd:PRK03918  283 ----------------KELKELKEKAEEYIklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkKK 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  915 KPEKERHLAESKEKHLM--EKKNKQSDNSEYSKSEKGKNKEK-DRELDKKEKSRDK--ESIN-----ITNSKHIQEEKKS 984
Cdd:PRK03918  347 LKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEieEEISkitarIGELKKEIKELKK 426

                         330       340
                  ....*....|....*....|...
gi 160358772  985 SIVDGNKAQHEKPLSLKEKTKDE 1007
Cdd:PRK03918  427 AIEELKKAKGKCPVCGRELTEEH 449
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 218-245 1.40e-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: 43.43  E-value: 1.40e-05
                           10        20
                   ....*....|....*....|....*....
gi 160358772   218 GWTPLHEAC-NVGYYDVAKILIAAGADVN 245
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 187-276 1.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  187 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSAS- 260
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISk 116

                          90
                  ....*....|....*..
gi 160358772  261 -SGHRDIVKLLLRHGGN 276
Cdd:PHA03100  117 kSNSYSIVEYLLDNGAN 133
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 674-983 2.19e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 2.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   674 EKYKTKDSAKELQRsvefdrefwkenffKSDETEDLFLnmEHESLTLEKKSKLEKNIKDDKSTKEKhvSKERNFKEERDK 753
Cdd:pfam02463  198 QELKLKEQAKKALE--------------YYQLKEKLEL--EEEYLLYLDYLKLNEERIDLLQELLR--DEQEEIESSKQE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   754 IKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLgmSAIEESIGLHLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDI 833
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   834 EK----MERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDR 909
Cdd:pfam02463  338 EElekeLKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160358772   910 KHDKEKPEKERHLAESKEKHLMEKK----NKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 983
Cdd:pfam02463  418 EDLLKEEKKEELEILEEEEESIELKqgklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 201-288 2.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  201 VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 280
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186


                  ....*...
gi 160358772  281 NKHGERPV 288
Cdd:PHA02874  187 DNNGESPL 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 218-245 2.85e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 2.85e-05
                            10        20
                    ....*....|....*....|....*...
gi 160358772    218 GWTPLHEACNVGYYDVAKILIAAGADVN 245
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 165-276 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  165 KKTPSSSSRQKDKVNKRNErgetplHMAAIRGDVKQ-----VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIA 239
Cdd:PHA02876  126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 160358772  240 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 276
Cdd:PHA02876  200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
209-256 4.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 4.07e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 160358772   209 ANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 256
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 250-277 4.30e-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: 4.30e-05
                            10        20
                    ....*....|....*....|....*...
gi 160358772    250 DDDTPLHDSASSGHRDIVKLLLRHGGNP 277
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-213 4.47e-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: 4.47e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 160358772    184 RGETPLHMAAIRGDVKQVKELISLGANVNV 213
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 250-282 2.00e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 2.00e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 160358772   250 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 282
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 192-270 2.66e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160358772  192 AAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 270
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-215 2.88e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 2.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 160358772   176 DKVNKRN-ERGETPLHMAAIRGDVKQVKELISLGANVNVKD 215
Cdd:pfam12796   51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 184-213 4.03e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 4.03e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 160358772   184 RGETPLHMAAIRGDVKQVKELISLGANVNV 213
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 198-284 4.20e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  198 VKQVKELISLGANVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 266
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127

                          90
                  ....*....|....*...
gi 160358772  267 VKLLLRHGGNPFQANKHG 284
Cdd:PHA02798  128 LLFMIENGADTTLLDKDG 145
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 218-246 4.32e-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: 39.16  E-value: 4.32e-04
                           10        20
                   ....*....|....*....|....*....
gi 160358772   218 GWTPLHEACNVGYYDVAKILIAAGADVNT 246
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 719-983 1.40e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   719 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 793
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   794 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 867
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   868 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 947
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 160358772   948 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 983
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 363-983 1.41e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   363 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 442
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   443 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 522
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   523 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 602
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   603 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 669
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   670 EGEKEKyktKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 744
Cdd:pfam02463  720 EELLAD---RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   745 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 823
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   824 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 903
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772   904 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 983
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 703-835 1.76e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  703 SDETEDLFLNMEHESLTLEKKSK-LEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFReEKIKDLKEERENIPTDk 781
Cdd:PRK00409  515 KEKLNELIASLEELERELEQKAEeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAIKEAKKEADEIIKE- 592

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 160358772  782 dseftslgMSAIEESIGLHLVEKEIdIEKQeKHIKESKEKPEKRSQIKEKDIEK 835
Cdd:PRK00409  593 --------LRQLQKGGYASVKAHEL-IEAR-KRLNKANEKKEKKKKKQKEKQEE 636
Ank_4 pfam13637
Ankyrin repeats (many copies);
178-205 2.41e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 2.41e-03
                           10        20
                   ....*....|....*....|....*...
gi 160358772   178 VNKRNERGETPLHMAAIRGDVKQVKELI 205
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 185-277 3.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  185 GETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 263
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114

                          90
                  ....*....|....
gi 160358772  264 RDIVKLLLRHGGNP 277
Cdd:PHA02875  115 LDIMKLLIARGADP 128
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 713-1063 8.99e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.19  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  713 MEHESLTLEKKSKLEKNIKDDKS----TKEKHVSKE---RNFKEERDKIKKESEKSFREEkikdlkEERENIPTDKDSEF 785
Cdd:PTZ00108 1004 LERELARLSNKVRFIKHVINGELvitnAKKKDLVKElkkLGYVRFKDIIKKKSEKITAEE------EEGAEEDDEADDED 1077

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  786 TSLGMSAIEESIglHLVEKEI---DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehksEKDKLDLS- 861
Cdd:PTZ00108 1078 DEEELGAAVSYD--YLLSMPIwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMWLE--------------DLDKFEEAl 1141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  862 ECVDKIKEKDKLYSHHTEKchKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKK--NKQSD 939
Cdd:PTZ00108 1142 EEQEEVEEKEIAKEQRLKS--KTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKpdNKKSN 1219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358772  940 NSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKE--- 1016
Cdd:PTZ00108 1220 SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESngg 1299

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160358772 1017 -----------------KDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSPASKDT 1063
Cdd:PTZ00108 1300 skpssptkkkvkkrlegSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDS 1363
 
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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