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Conserved domains on  [gi|1034603741|ref|XP_016881155|]
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ankyrin repeat domain-containing protein 12 isoform X4 [Homo sapiens]

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];
148-266 6.79e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.79e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  148 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 227
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603741  228 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
PTZ00121 super family cl31754
MAEBL; Provisional
 695-1140 8.32e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  695 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 774
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  775 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 854
Cdd:PTZ00121  1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  855 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 934
Cdd:PTZ00121  1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  935 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1014
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741 1015 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1094
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034603741 1095 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1140
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 ...
 338-958 2.25e-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: 43.04  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  338 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 417
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  418 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 497
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  498 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 577
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  578 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 644
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  645 EGEKEKYKTKDSAKElqrSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 719
Cdd:pfam02463  720 EELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  720 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 798
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  799 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 878
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  879 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 958
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
148-266 6.79e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.79e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  148 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 227
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603741  228 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
164-252 1.40e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  164 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 243
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 1034603741  244 LLLRHGGNP 252
Cdd:pfam12796   79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-265 5.25e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 228
Cdd:PHA03095    40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603741  229 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 265
Cdd:PHA03095   120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
PTZ00121 PTZ00121
MAEBL; Provisional
 695-1140 8.32e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  695 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 774
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  775 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 854
Cdd:PTZ00121  1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  855 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 934
Cdd:PTZ00121  1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  935 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1014
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741 1015 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1094
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034603741 1095 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1140
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 ...
 691-1024 2.13e-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: 59.60  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  691 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 770
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  771 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 849
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  850 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 929
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  930 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1007
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 1034603741 1008 HKDKIQINSLLKLKSEA 1024
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-231 1.11e-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: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  160 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 225
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*.
gi 1034603741  226 DDTPLH 231
Cdd:cd22192    169 GNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 193-220 2.81e-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: 2.81e-05
                            10        20
                    ....*....|....*....|....*...
gi 1034603741   193 GWTPLHEACNVGYYDVAKILIAAGADVN 220
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 694-958 1.63e-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: 43.51  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  694 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 768
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  769 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 842
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  843 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 922
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034603741  923 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 958
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 ...
 338-958 2.25e-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: 43.04  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  338 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 417
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  418 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 497
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  498 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 577
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  578 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 644
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  645 EGEKEKYKTKDSAKElqrSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 719
Cdd:pfam02463  720 EELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  720 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 798
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  799 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 878
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  879 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 958
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
148-266 6.79e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 6.79e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  148 RQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 227
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603741  228 TPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
149-266 1.81e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 1.81e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  149 QKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDT 228
Cdd:COG0666     76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034603741  229 PLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:COG0666    156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-286 8.34e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 8.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 232
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034603741  233 SASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDE 286
Cdd:COG0666    226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-266 7.42e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 7.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  150 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 229
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034603741  230 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:COG0666    124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
Ank_2 pfam12796
Ankyrin repeats (3 copies);
164-252 1.40e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 1.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  164 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIaAGADVNTQGlDDDTPLHDSASSGHRDIVK 243
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*....
gi 1034603741  244 LLLRHGGNP 252
Cdd:pfam12796   79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-261 1.31e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHD 232
Cdd:COG0666    179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258

                           90       100
                   ....*....|....*....|....*....
gi 1034603741  233 SASSGHRDIVKLLLRHGGNPFQANKHGER 261
Cdd:COG0666    259 AAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-265 5.25e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 5.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHM---AAIRGDVKQVKELISLGANVNVKDFAGWTPLH-EACNVGYYDVAKILIAAGADVNTQGLDDDT 228
Cdd:PHA03095    40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603741  229 PLHDSASSG--HRDIVKLLLRHGGNPFQANKHGERPVDV 265
Cdd:PHA03095   120 PLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-222 3.45e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 3.45e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQVKELISlGANVNVKDFaGWTPLHEACNVGYYDVAKILIAAGADVNTQ 222
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 152-266 7.49e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 7.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  152 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 231
Cdd:PHA02874   116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034603741  232 DSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:PHA02874   196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 126-251 7.99e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 7.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  126 NSTPNHPSQTTPAQKKTPSSSSRQKDkVNKRNERGETPLHMAAIRG-DVKQVKELISLGANVNVKDFAGWTPLHEACNVG 204
Cdd:PHA02876   274 NTPLHHASQAPSLSRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLD 352

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034603741  205 YY-DVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 251
Cdd:PHA02876   353 RNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 152-251 1.79e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  152 KVNKRNERGETPLHMAAIRGDVK------------------QVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 213
Cdd:PHA03100   133 NVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL 212

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1034603741  214 AAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 251
Cdd:PHA03100   213 DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 93-259 1.99e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 72.62  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741   93 GNKKSTPVSILFgyplserKQMALLMQMTARDNNSTpnHPSQTTPAQKKTPSSSSRQKDKVNkrnergETPLHMAAIR-- 170
Cdd:PTZ00322    23 GSRKRRAKPISF-------ERMAAIQEEIARIDTHL--EALEATENKDATPDHNLTTEEVID------PVVAHMLTVElc 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  171 -----GDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 245
Cdd:PTZ00322    88 qlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                          170
                   ....*....|....
gi 1034603741  246 LRHGGNPFQANKHG 259
Cdd:PTZ00322   168 SRHSQCHFELGANA 181
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-266 1.01e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  150 KDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTP 229
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034603741  230 LHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-266 1.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 1.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  118 MQMTARDNNSTPNHPSQTTPAQKKTPSSSSRQKdKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPL 197
Cdd:PHA02878   160 INMKDRHKGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034603741  198 HEAcnVGY---YDVAKILIAAGADVNTQG-LDDDTPLHDSASSghRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:PHA02878   239 HIS--VGYckdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 153-266 2.58e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEAcnVGYYDVAKILIAAGADVNTQGLDDDTPLHD 232
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHH 260

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034603741  233 SAS-SGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:PHA02874   261 AINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 161-248 7.32e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 7.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  161 ETPLHMAAIRGDVKQVKELISLGANVN---VKDfaGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 237
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADdvfYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90
                   ....*....|.
gi 1034603741  238 HRDIVKLLLRH 248
Cdd:PHA02875   147 DIKGIELLIDH 157
PTZ00121 PTZ00121
MAEBL; Provisional
 695-1140 8.32e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 8.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  695 LEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEEsigl 774
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---- 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  775 hLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKlyshhte 854
Cdd:PTZ00121  1383 -AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------- 1454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  855 kchkegEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELD 934
Cdd:PTZ00121  1455 ------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  935 KKEKSRDKESINITNSKHIQEEKKssivdgnKAQhekplslKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQI 1014
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELK-------KAE-------ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741 1015 NSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELK 1094
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1034603741 1095 IKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQ 1140
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-262 9.68e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 9.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLH--MAAIRGDVKQVKELISLGANVNVKDFAGWTPLH-----EACNVgyyDVAKILIAAGADVNTQGLD 225
Cdd:PHA03095   110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVDDR 186

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034603741  226 DDTPLHDSASSGHRD--IVKLLLRHGGNPFQANKHGERP 262
Cdd:PHA03095   187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTP 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 172-251 1.59e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  172 DVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKI---LIAAGADVNTQGLDDDTPLHDSASSGHR-DIVKLLLR 247
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105


                   ....
gi 1034603741  248 HGGN 251
Cdd:PHA03095   106 AGAD 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-213 1.62e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.62e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034603741  162 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILI 213
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
193-246 2.11e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034603741  193 GWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLL 246
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00121 PTZ00121
MAEBL; Provisional
 709-1043 1.69e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  709 KSTKEKHVSKERNFKEER--DKIKKESEKSFREEKIKDLKEERENIPTDKdseftslgmsaIEESIGLHLVEKEIDIEKQ 786
Cdd:PTZ00121  1207 KAEEERKAEEARKAEDAKkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRK-----------FEEARMAHFARRQAAIKAE 1275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  787 EKHIKESKEKPEKRSQIKEKDIEKMERKTFEKekkikhehkseKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNT 866
Cdd:PTZ00121  1276 EARKADELKKAEEKKKADEAKKAEEKKKADEA-----------KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  867 AAIKKTDDrEKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESin 946
Cdd:PTZ00121  1345 AEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-- 1421

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  947 itNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQinsllKLKSEADK 1026
Cdd:PTZ00121  1422 --EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-----EAKKKAEE 1494

                          330
                   ....*....|....*..
gi 1034603741 1027 PKPKSSPASKDTRPKEK 1043
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 ...
 691-1024 2.13e-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: 59.60  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  691 ESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFtsLGMSAIEE 770
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  771 SIGLHLVEKE-IDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcvDKIKEKDKLY 849
Cdd:pfam02463  242 LQELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK--VDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  850 SHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEK 929
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  930 DRELDKKEKSRDK--ESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDK 1007
Cdd:pfam02463  400 KSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330
                   ....*....|....*..
gi 1034603741 1008 HKDKIQINSLLKLKSEA 1024
Cdd:pfam02463  480 VKLQEQLELLLSRQKLE 496
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 172-266 2.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  172 DVKQVKELISLGANVNVKD-FAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGG 250
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90
                   ....*....|....*.
gi 1034603741  251 NPFQANKHGERPVDVA 266
Cdd:PHA02878   226 STDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 152-221 3.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.30e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  152 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNT 221
Cdd:PHA03100   184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00121 PTZ00121
MAEBL; Provisional
 344-979 1.57e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.07  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  344 EEINKMIDDRHIlRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTSCSVIPE 423
Cdd:PTZ00121  1191 EELRKAEDARKA-EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  424 TS-NSDMQTKKEYVVSGEHKQKGKVKRKLKNQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFRKSFSP 502
Cdd:PTZ00121  1270 AAiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  503 KDDTSlhlfhistgKSPKHSCGLSEKQSTPLKQEHTKTclspGSSEMSLQPDLVR-YDNTESEFLPESSSVKSCKHKEKS 581
Cdd:PTZ00121  1350 AEAEA---------AADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKkADEAKKKAEEDKKKADELKKAAAA 1416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  582 KHQKDfhlEFGEKSNAKIKDEDHSPTFENSdctlKKMDKEGKTLKKHKLKHKEREKEKHKKEIEGEKEKYKTKDSAKELQ 661
Cdd:PTZ00121  1417 KKKAD---EAKKKAEEKKKADEAKKKAEEA----KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  662 RSVEFDREFWKENFFKSDE---TEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKI--KKESEKS 736
Cdd:PTZ00121  1490 KKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeeKKKAEEA 1569

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  737 FREekikdlkEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEkqekhikESKEKPEKRSQIKEKDIEKMERKTF 816
Cdd:PTZ00121  1570 KKA-------EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-------EAKKAEEAKIKAEELKKAEEEKKKV 1635

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  817 EKEKKIKHEHKSEKDKLDLSECVDKIKEKDklyshhtEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD--------K 888
Cdd:PTZ00121  1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAE-------EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakkaeelK 1708

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  889 EKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQ 968
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788

                          650
                   ....*....|.
gi 1034603741  969 HEKPLSLKEKT 979
Cdd:PTZ00121  1789 DEKRRMEVDKK 1799
Ank_5 pfam13857
Ankyrin repeats (many copies);
153-200 2.11e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 2.11e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEA 200
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-230 2.94e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 2.94e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034603741  152 KVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPL 230
Cdd:COG0666    211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 162-251 3.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  162 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHR-D 240
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiD 216

                           90
                   ....*....|.
gi 1034603741  241 IVKLLLRHGGN 251
Cdd:PHA02875   217 IVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 164-227 5.02e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 5.02e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034603741  164 LHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDD 227
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 128-250 1.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  128 TPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDV---------------------------------- 173
Cdd:PHA02876   343 TPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVviintlldygadiealsqkigtalhfalcgtnpy 422

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603741  174 KQVKELISLGANVNVKDFAGWTPLHEAC-NVGYYDVAKILIAAGADVNTQGLDDDTPLhdSASSGHRDIVKLLLRHGG 250
Cdd:PHA02876   423 MSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 159-260 1.12e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  159 RGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKIL--IAAGADVNT--------------- 221
Cdd:PLN03192   557 KGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAagdllctaakrndlt 636

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034603741  222 -------QGLDDDTPLHDSASS-------GHRDIVKLLLRHGGNPFQANKHGE 260
Cdd:PLN03192   637 amkellkQGLNVDSEDHQGATAlqvamaeDHVDMVRLLIMNGADVDKANTDDD 689
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 162-251 1.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  162 TPLH-----MAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACN--VGYYDVAKILIAAGADVNTQGLDDDTPLHDSA 234
Cdd:PHA03100    70 TPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149

                           90
                   ....*....|....*....
gi 1034603741  235 SSGHRD--IVKLLLRHGGN 251
Cdd:PHA03100   150 ESNKIDlkILKLLIDKGVD 168
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 683-982 1.52e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 53.51  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  683 DLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSK--ERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTdkdsef 760
Cdd:PTZ00108  1089 DYLLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpKDMWLEDLDKFEEALEEQEEVEEKEIAKEQRLKSKT------ 1162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  761 tslgmsaieesiglhlveKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVD 840
Cdd:PTZ00108  1163 ------------------KGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSD 1224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  841 KIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKtdDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSK 920
Cdd:PTZ00108  1225 QEDDEEQKTKPKKSSVKRLKSKKNNSSKSSE--DNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKP 1302

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034603741  921 SEKGKNKEKDRE---LDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDE 982
Cdd:PTZ00108  1303 SSPTKKKVKKRLegsLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
Ank_5 pfam13857
Ankyrin repeats (many copies);
212-266 2.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603741  212 LIAAG-ADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 153-259 2.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQ--VKELISLGANVNVKdfagwTPLHEACNVGYY---------DVAKILIAAGADVNT 221
Cdd:PHA02859    44 VNDCNDLYETPIFSCLEKDKVNVeiLKFLIENGADVNFK-----TRDNNLSALHHYlsfnknvepEILKILIDSGSSITE 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034603741  222 QGLDDDTPLHDSAS--SGHRDIVKLLLRHGGNPFQANKHG 259
Cdd:PHA02859   119 EDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDN 158
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 159-190 5.32e-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: 5.32e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034603741  159 RGETPLHMAAIR-GDVKQVKELISLGANVNVKD 190
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00121 PTZ00121
MAEBL; Provisional
 641-1039 6.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 6.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  641 KKEIEGEKEKYKTKDSAKELQRSVEFDR--EFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDD---KSTKEKH 715
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeakKKAEEAK 1483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  716 VSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKhIKESKE 795
Cdd:PTZ00121  1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE-LKKAEE 1562

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  796 KPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKE--KDKLYSHHTEKCHKEGEKSKNTAAIKKTD 873
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  874 DREKSREKMDRKHDKEKPEKERHLAESKEkhlmEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHI 953
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  954 QEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSP 1033
Cdd:PTZ00121  1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798


                   ....*.
gi 1034603741 1034 ASKDTR 1039
Cdd:PTZ00121  1799 KIKDIF 1804
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 158-266 8.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 8.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  158 ERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSG 237
Cdd:PHA02875   100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                           90       100
                   ....*....|....*....|....*....
gi 1034603741  238 HRDIVKLLLRHGGNPfqaNKHGERPvDVA 266
Cdd:PHA02875   180 DIAICKMLLDSGANI---DYFGKNG-CVA 204
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-247 1.04e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  120 MTARDN--NSTPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDVK--QVKELISLGANVNVKDFAGWT 195
Cdd:PHA03095   180 VYAVDDrfRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQT 259

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034603741  196 PLHEAcnvGYYD---VAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLR 247
Cdd:PHA03095   260 PLHYA---AVFNnprACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-231 1.11e-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: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  160 GETPLHMAAIRGDVKQVKELISLGANVNV--------------KDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLD 225
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpknLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                   ....*.
gi 1034603741  226 DDTPLH 231
Cdd:cd22192    169 GNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 209-266 1.16e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603741  209 AKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVA 266
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 193-220 1.38e-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: 1.38e-05
                           10        20
                   ....*....|....*....|....*....
gi 1034603741  193 GWTPLHEAC-NVGYYDVAKILIAAGADVN 220
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 162-251 1.86e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  162 TPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYY-----DVAKILIAAGADVNTQGLDDDTPLHDSAS- 235
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISk 116

                           90
                   ....*....|....*..
gi 1034603741  236 -SGHRDIVKLLLRHGGN 251
Cdd:PHA03100   117 kSNSYSIVEYLLDNGAN 133
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
673-982 2.00e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  673 ENFFKSDETEDL----FLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFRE-----EKIK 743
Cdd:PRK03918   138 DAILESDESREKvvrqILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineisSELP 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  744 DLKEERENIPTDKDSeftslgMSAIEESIGlhlvEKEIDIEKQEKHIKESKEK---PEKRSQIKEKDIEKMERKTfekek 820
Cdd:PRK03918   218 ELREELEKLEKEVKE------LEELKEEIE----ELEKELESLEGSKRKLEEKireLEERIEELKKEIEELEEKV----- 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  821 kikhehksekdkldlsECVDKIKEKDKLYS--------HHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHD---KE 889
Cdd:PRK03918   283 ----------------KELKELKEKAEEYIklsefyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelkKK 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  890 KPEKERHLAESKEKHLM--EKKNKQSDNSEYSKSEKGKNKEK-DRELDKKEKSRDK--ESIN-----ITNSKHIQEEKKS 959
Cdd:PRK03918   347 LKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEieEEISkitarIGELKKEIKELKK 426

                          330       340
                   ....*....|....*....|...
gi 1034603741  960 SIVDGNKAQHEKPLSLKEKTKDE 982
Cdd:PRK03918   427 AIEELKKAKGKCPVCGRELTEEH 449
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 176-263 2.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  176 VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQA 255
Cdd:PHA02874   107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186


                   ....*...
gi 1034603741  256 NKHGERPV 263
Cdd:PHA02874   187 DNNGESPL 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 193-220 2.81e-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: 2.81e-05
                            10        20
                    ....*....|....*....|....*...
gi 1034603741   193 GWTPLHEACNVGYYDVAKILIAAGADVN 220
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 649-978 3.38e-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: 49.20  E-value: 3.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  649 EKYKTKDSAKELQRsvefdrefwkenffKSDETEDLFLnmEHESLTLEKKSKLEKNIKDDKSTKEKhvSKERNFKEERDK 728
Cdd:pfam02463  198 QELKLKEQAKKALE--------------YYQLKEKLEL--EEEYLLYLDYLKLNEERIDLLQELLR--DEQEEIESSKQE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  729 IKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLgmSAIEESIGLHLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDI 808
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  809 EK----MERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDR 884
Cdd:pfam02463  338 EElekeLKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  885 KHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDG 964
Cdd:pfam02463  418 EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497

                          330
                   ....*....|....
gi 1034603741  965 NKAQHEKPLSLKEK 978
Cdd:pfam02463  498 RSQKESKARSGLKV 511
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 140-251 3.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  140 KKTPSSSSRQKDKVNKRNErgetplHMAAIRGDVKQ-----VKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIA 214
Cdd:PHA02876   126 KEAISGNDIHYDKINESIE------YMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLS 199

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034603741  215 AGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGN 251
Cdd:PHA02876   200 YGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
184-231 4.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 4.02e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034603741  184 ANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLH 231
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 225-252 4.24e-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: 4.24e-05
                            10        20
                    ....*....|....*....|....*...
gi 1034603741   225 DDDTPLHDSASSGHRDIVKLLLRHGGNP 252
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-188 4.41e-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: 4.41e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1034603741   159 RGETPLHMAAIRGDVKQVKELISLGANVNV 188
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 225-257 1.97e-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: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034603741  225 DDDTPLHDSA-SSGHRDIVKLLLRHGGNPFQANK 257
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 167-245 2.63e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 2.63e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034603741  167 AAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLL 245
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-190 2.85e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 2.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034603741  151 DKVNKRN-ERGETPLHMAAIRGDVKQVKELISLGANVNVKD 190
Cdd:pfam12796   51 EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 159-188 3.98e-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: 3.98e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034603741  159 RGETPLHMAAIRGDVKQVKELISLGANVNV 188
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 193-221 4.27e-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: 4.27e-04
                           10        20
                   ....*....|....*....|....*....
gi 1034603741  193 GWTPLHEACNVGYYDVAKILIAAGADVNT 221
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 173-259 4.32e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  173 VKQVKELISLGANVNVKDFAGWTPLheaC----NVGYY----DVAKILIAAGADVNTQGLDDDTPLHDSASSGH---RDI 241
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsNIKDYkhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEI 127

                           90
                   ....*....|....*...
gi 1034603741  242 VKLLLRHGGNPFQANKHG 259
Cdd:PHA02798   128 LLFMIENGADTTLLDKDG 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 694-958 1.63e-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: 43.51  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  694 TLEKKSKLE---KNIKDDKSTKEKHVSKER--NFKEERDKIKKESEKSfrEEKIKDLKEERENipTDKDSEFTSLGMSAI 768
Cdd:TIGR02168  204 SLERQAEKAeryKELKAELRELELALLVLRleELREELEELQEELKEA--EEELEELTAELQE--LEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  769 EESIG-----LHLVEKEI-DIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKtfekekkikhehkSEKDKLDLSECVDKI 842
Cdd:TIGR02168  280 EEEIEelqkeLYALANEIsRLEQQKQILRERLANLERQLEELEAQLEELESK-------------LDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  843 KEKDKLYshhtekchkEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKpeKERHLAESKEKHLMEKKNKQSDNSEYSKSE 922
Cdd:TIGR02168  347 EELKEEL---------ESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034603741  923 KGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 958
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 678-810 1.89e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  678 SDETEDLFLNMEHESLTLEKKSK-LEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFReEKIKDLKEERENIPTDk 756
Cdd:PRK00409   515 KEKLNELIASLEELERELEQKAEeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAIKEAKKEADEIIKE- 592

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034603741  757 dseftslgMSAIEESIGLHLVEKEIdIEKQeKHIKESKEKPEKRSQIKEKDIEK 810
Cdd:PRK00409   593 --------LRQLQKGGYASVKAHEL-IEAR-KRLNKANEKKEKKKKKQKEKQEE 636
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 338-958 2.25e-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: 43.04  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  338 FKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTS 417
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  418 CSVIPETSNSDMQTKKEYVVSGEHKQKGKVKrklknQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFR 497
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISA-----HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  498 KSFSPKDDTSLHLFHIstgkspkhscGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRydNTESEFLPESSSVKSCKH 577
Cdd:pfam02463  572 ELPLGARKLRLLIPKL----------KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR--AKVVEGILKDTELTKLKE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  578 KEKSKHQKDFHLEFGEKSNA---KIKDEDHSPTFENSDCTLKKMDKEGKTLK----------KHKLKHKEREKEKHKKEI 644
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAeksEVKASLSELTKELLEIQELQEKAESELAKeeilrrqleiKKKEQREKEELKKLKLEA 719

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  645 EGEKEKYKTKDSAKElqrSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHV-----SKE 719
Cdd:pfam02463  720 EELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVeeekeEKL 796

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  720 RNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEK-PE 798
Cdd:pfam02463  797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKE 876

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  799 KRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSEcVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKS 878
Cdd:pfam02463  877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK-ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  879 REKMDRKhdKEKPEKERHLAESKEKHLMEKKNKQSDnSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKK 958
Cdd:pfam02463  956 EEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEER-YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
Ank_4 pfam13637
Ankyrin repeats (many copies);
153-180 2.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 2.38e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034603741  153 VNKRNERGETPLHMAAIRGDVKQVKELI 180
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 160-252 3.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603741  160 GETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDD-DTPLHDSASSGH 238
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKK 114

                           90
                   ....*....|....
gi 1034603741  239 RDIVKLLLRHGGNP 252
Cdd:PHA02875   115 LDIMKLLIARGADP 128
 
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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