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Conserved domains on  [gi|1335749719|ref|NP_001347001|]
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M-phase phosphoprotein 8 isoform 2 [Mus musculus]

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];
553-734 1.86e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 553 MKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLIT 632
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 633 KGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNS 712
Cdd:COG0666   142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                         170       180
                  ....*....|....*....|..
gi 1335749719 713 ALYFAKQCNNVLVYELLKSHLE 734
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGA 243
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 1.56e-30

chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349283  Cd Length: 51  Bit Score: 113.92  E-value: 1.56e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1335749719  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18633     1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
PTZ00121 super family cl31754
MAEBL; Provisional
 97-482 3.13e-11

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719   97 EDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMG 176
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  177 KLKDKFKTELESTSEIigfdVKTKKRIWEVKEelKDSKKPKKDEIKETKELKK-ANKRAEVRDLKIKIREDVKENRKTKK 255
Cdd:PTZ00121  1405 KKADELKKAAAAKKKA----DEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  256 ERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPR 335
Cdd:PTZ00121  1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  336 KFEEPK---EIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSrlsgEEKSLKSPDL---AEEVKL 409
Cdd:PTZ00121  1559 KAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELkkaEEEKKK 1634

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  410 VENLKSTDMEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI 482
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
553-734 1.86e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 553 MKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLIT 632
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 633 KGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNS 712
Cdd:COG0666   142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                         170       180
                  ....*....|....*....|..
gi 1335749719 713 ALYFAKQCNNVLVYELLKSHLE 734
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGA 243
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 1.56e-30

chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349283  Cd Length: 51  Bit Score: 113.92  E-value: 1.56e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1335749719  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18633     1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
616-705 4.73e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 4.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 616 MLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEaGAFVNVqQSNGETALMKACKRGNSDIVRL 695
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1335749719 696 VIECGADCNI 705
Cdd:pfam12796  80 LLEKGADINV 89
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
59-109 2.41e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.91  E-value: 2.41e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  59 FEVERILDMK-CEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:pfam00385   1 YEVERILDHRkDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
58-109 5.50e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 61.46  E-value: 5.50e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719   58 VFEVERILDMKCEGGKNL-YKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:smart00298   1 EYEVEKILDHRWKKKGELeYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
PTZ00121 PTZ00121
MAEBL; Provisional
 97-482 3.13e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719   97 EDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMG 176
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  177 KLKDKFKTELESTSEIigfdVKTKKRIWEVKEelKDSKKPKKDEIKETKELKK-ANKRAEVRDLKIKIREDVKENRKTKK 255
Cdd:PTZ00121  1405 KKADELKKAAAAKKKA----DEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  256 ERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPR 335
Cdd:PTZ00121  1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  336 KFEEPK---EIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSrlsgEEKSLKSPDL---AEEVKL 409
Cdd:PTZ00121  1559 KAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELkkaEEEKKK 1634

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  410 VENLKSTDMEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI 482
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 629-731 1.54e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 629 LLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSK 708
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

                          90       100
                  ....*....|....*....|....
gi 1335749719 709 HqnsALYFA-KQCNNVLVYELLKS 731
Cdd:PHA03100  257 T---LLYFKdKDLNTITKIKMLKK 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 676-705 5.98e-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: 40.65  E-value: 5.98e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1335749719  676 NGETALMKACKRGNSDIVRLVIECGADCNI 705
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 572-734 9.44e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 572 TNRIPNNLLRDAVKNGDYIAVKVALnsneeYNLDQEDSTGMTLVMLAA---AGGQDDLLRLLITKGAK------VNGRQK 642
Cdd:TIGR00870  48 PDRLGRSALFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISleyVDAVEAILLHLLAAFRKsgplelANDQYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 643 N----GTTALIHAAEKNFLTTVAILLEAGAFVNV----------QQSN----GETALMKACKRGNSDIVRLVIECGAD-- 702
Cdd:TIGR00870 123 SeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADil 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1335749719 703 ------------CNILSKHQNSALYFAKQCnnvlvYELLKSHLE 734
Cdd:TIGR00870 203 tadslgntllhlLVMENEFKAEYEELSCQM-----YNFALSLLD 241
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 219-509 2.65e-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: 41.50  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  219 DEIKETKELKKANKRAEVRDLKIKIREdVKENRKTKKERYIEsplESESPNDSLILEDDSEDFISDNRE-ENQNVRSVRD 297
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEE-LKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLkLNEERIDLLQ 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  298 KTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEpKEIKKLESTNAFLERRAIPKKQRNQDKG----ISNLE 373
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE-EELKLLAKEEEELKSELLKLERRKVDDEeklkESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  374 LNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEVKLVENLKSTDMEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFK 453
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  454 EIRNA------FDLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKTKDKCSLKEKRNTRDE 509
Cdd:pfam02463  403 EEKEAqlllelARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
COG5022 COG5022
Myosin heavy chain [General function prediction only];
91-494 3.80e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719   91 EPEVHLEDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEAdsdSDQQSDTKEDISPRKKKKKIKCKEETspEDLRK 170
Cdd:COG5022    865 KKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEI---IELKKSLSSDLIENLEFKTELIARLK--KLLNN 939

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  171 KRTKMGKLKDK-----------FKTELESTSEIIGFDVKTKKriwEVKEELKDSK---KPKKDEIKETKELKKA--NKRA 234
Cdd:COG5022    940 IDLEEGPSIEYvklpelnklheVESKLKETSEEYEDLLKKST---ILVREGNKANselKNFKKELAELSKQYGAlqESTK 1016

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  235 EVRDLKIKIREDVKENRKTKKERYIESPLESESPndsliLEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLD 314
Cdd:COG5022   1017 QLKELPVEVAELQSASKIISSESTELSILKPLQK-----LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTEN 1091

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  315 DLISIEEDAGTRVRRKKTKPR-----------KFEEPKEIKK-LESTNAFLERRAIPKKQRNQDKGISNLELN---KLPS 379
Cdd:COG5022   1092 LLKTINVKDLEVTNRNLVKPAnvlqfivaqmiKLNLLQEISKfLSQLVNTLEPVFQKLSVLQLELDGLFWEANleaLPSP 1171

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  380 PVFAQTLKSSRLSGEEKSLKSPDLAEEVKLVENLKSTDMEKEKKNEPKGKYQKryDLDKEEKARKEpkVLKSFKEIRNAF 459
Cdd:COG5022   1172 PPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLK--KLISEGWVPTE--YSTSLKGFNNLN 1247

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1335749719  460 DLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKT 494
Cdd:COG5022   1248 KKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVL 1282
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 600-726 4.72e-03

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: 40.38  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 600 EEYNLDQEDSTGMTLVMLAAAGGQ-DDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAG-AFVNVQQSN- 676
Cdd:cd22192     6 DELHLLQQKRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTSd 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719 677 ---GETALMKACKRGNSDIVRLVIECGADcniLSKHQNSALYFAKQCNNVLVY 726
Cdd:cd22192    86 lyqGETALHIAVVNQNLNLVRELIARGAD---VVSPRATGTFFRPGPKNLIYY 135
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
553-734 1.86e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 553 MKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLIT 632
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA--DVNARDKDGETPLHLAAYNGNLEIVKLLLE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 633 KGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNS 712
Cdd:COG0666   142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                         170       180
                  ....*....|....*....|..
gi 1335749719 713 ALYFAKQCNNVLVYELLKSHLE 734
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-732 3.91e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 3.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 546 MDLQLEWMKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDD 625
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA--DINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 626 LLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNI 705
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         170       180
                  ....*....|....*....|....*..
gi 1335749719 706 LSKHQNSALYFAKQCNNVLVYELLKSH 732
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEA 208
CD_MMP8 cd18633
chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), ...
 58-108 1.56e-30

chromodomain of M-phase phosphoprotein 8; The chromodomain of M-phase phosphoprotein 8 (MPP8), a component of the RanBPM-containing large protein complex, binds methylated H3K9. This may in turn recruit the H3K9 methyltransferases GLP and ESET, and DNA methyltransferase 3A to the promoter of the E-cadherin gene, mediating the E-cadherin gene silencing and promoting tumor cell motility and invasion. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349283  Cd Length: 51  Bit Score: 113.92  E-value: 1.56e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1335749719  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18633     1 VFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEVHLEDCKEVLLEFRK 51
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
571-730 1.07e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 571 TTNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIH 650
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGA--DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 651 AAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLK 730
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
573-730 1.87e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 573 NRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAA 652
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335749719 653 EKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV-LVYELLK 730
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLeIVKLLLE 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
616-705 4.73e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 4.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 616 MLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEaGAFVNVqQSNGETALMKACKRGNSDIVRL 695
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1335749719 696 VIECGADCNI 705
Cdd:pfam12796  80 LLEKGADINV 89
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
 59-108 1.68e-17

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 76.75  E-value: 1.68e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd00024     1 YEVEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
572-698 1.06e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 572 TNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 651
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGA--DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1335749719 652 AEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIE 698
Cdd:COG0666   227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
580-673 2.80e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 580 LRDAVKNGDYIAVKVALNsnEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKgAKVNgRQKNGTTALIHAAEKNFLTT 659
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1335749719 660 VAILLEAGAFVNVQ 673
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
648-732 1.19e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 648 LIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECgADCNILSkHQNSALYFAKQCNNVLVYE 727
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*
gi 1335749719 728 LLKSH 732
Cdd:pfam12796  79 LLLEK 83
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
59-109 2.41e-13

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.91  E-value: 2.41e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  59 FEVERILDMK-CEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:pfam00385   1 YEVERILDHRkDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CD_CDY cd18634
chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain ...
 58-108 5.21e-13

chromodomain of the Chromodomain Y-like protein family; This group includes the chromodomain found in the mammalian chromodomain Y-like (CDY) protein family, and similar proteins. The human CDY family includes 6 proteins: the genes encoding four of these: two copies of CDY1 (CDY1a, CDY1a) and two copies of CDY2(CDY2a and CDY2b), are located on chromosome Y, and the genes encoding the other two members (CDYL and CDYL2) are located on autosomes. The chromosomal genes are only present in primates, whereas the CDYL and CDYL2 genes exist in most mammalian species. The CDY family proteins contain two functional domains: a chromodomain involved in chromatin binding and a catalytic domain found in many coenzyme A (CoA)- dependent acylation enzymes. CDYL is ubiquitously expressed, whereas CDYL2 shows selective expression in tissues of testis, prostate, spleen, and leukocyte. The CDYL genes are ubiquitously expressed, the CDY genes are only expressed in the testis. Deletion of the CDY1b gene has been shown to be a risk factor for male infertility. Impairments in CDY2 expression could be implicated in the pathogenesis of maturation arrest (a failure of germ cell development).


Pssm-ID: 349284  Cd Length: 52  Bit Score: 64.00  E-value: 5.21e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  58 VFEVERILDM-KCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18634     1 LYEVERIVDKrKNKKGKTEYLVRWKGYDSEDDTWEPEQHLLNCEEFIHDFNR 52
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
 58-106 1.76e-12

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 62.72  E-value: 1.76e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1335749719  58 VFEVERILDM-----KCEGGKNLY-KVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18635     1 EFEVEKLVGIcygdpKKTGERGLYfKVRWKGYGPEEDTWEPIEGLSNCPEKIKEF 55
CHROMO smart00298
Chromatin organization modifier domain;
58-109 5.50e-12

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 61.46  E-value: 5.50e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719   58 VFEVERILDMKCEGGKNL-YKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:smart00298   1 EYEVEKILDHRWKKKGELeYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKK 53
CD_Clr4_like cd18632
N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar ...
 59-109 7.84e-12

N-terminal chromodomain of the fission yeast histone methyltransferase Clr4, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of cryptic loci regulator 4 (Clr4), a histone H3 lysine methyltransferase which targets H3K9. Clr4 regulates silencing and switching at the mating-type loci and affects chromatin structure at centromeres. Clr4 is a catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349282  Cd Length: 55  Bit Score: 60.98  E-value: 7.84e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  59 FEVERILDMKC--EGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKK 109
Cdd:cd18632     2 YEVEKIVDEKTdrNTAEPLYLVRWKNYSKNHDTWEPAENLSGCQAVLEKWKRK 54
PTZ00121 PTZ00121
MAEBL; Provisional
 97-482 3.13e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719   97 EDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMG 176
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  177 KLKDKFKTELESTSEIigfdVKTKKRIWEVKEelKDSKKPKKDEIKETKELKK-ANKRAEVRDLKIKIREDVKENRKTKK 255
Cdd:PTZ00121  1405 KKADELKKAAAAKKKA----DEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  256 ERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPR 335
Cdd:PTZ00121  1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  336 KFEEPK---EIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSrlsgEEKSLKSPDL---AEEVKL 409
Cdd:PTZ00121  1559 KAEEKKkaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELkkaEEEKKK 1634

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  410 VENLKSTDMEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEI 482
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
591-732 4.62e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 591 AVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFV 670
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335749719 671 NVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLKSH 732
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
 59-108 1.42e-10

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 57.10  E-value: 1.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18974     1 WEVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAPKAIQSYEK 50
CD_Tf2-1_POL_like cd18973
chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type ...
 59-108 2.32e-10

chromodomain of Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizoctonia solani AG-1 IB retrotransposable element Tf2 155 kDa protein type 1 (Tf2-1), and similar proteins. It belongs to the Ty3/gypsy family of long terminal repeat (LTR) retrotransposons. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349329  Cd Length: 50  Bit Score: 56.49  E-value: 2.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18973     1 YVVEAILDNKRRKGKWLYLVKWKGYGPEHNTWEPRENLEHAQKLLKKYYQ 50
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 58-106 2.61e-10

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349324  Cd Length: 57  Bit Score: 56.59  E-value: 2.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1335749719  58 VFEVERIL------DMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18968     1 EYEVEVILaarvvkDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDDLLERF 55
CD_NC-like cd18980
chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and ...
 59-106 9.92e-10

chromodomain of a Tasahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Trichosporon asahii var. asahii CBS 8904 retrotransposon nucleocapsid protein, and similar proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349336  Cd Length: 56  Bit Score: 54.88  E-value: 9.92e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1335749719  59 FEVERILDMKCEG---GKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18980     4 YEVEAILDHKVDRryrDPNFYLVRWRGYGPSHDSWEPTSALENAQDLLREF 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 629-731 1.54e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 629 LLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSK 708
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

                          90       100
                  ....*....|....*....|....
gi 1335749719 709 HqnsALYFA-KQCNNVLVYELLKS 731
Cdd:PHA03100  257 T---LLYFKdKDLNTITKIKMLKK 277
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 59-108 1.99e-09

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349281  Cd Length: 50  Bit Score: 53.98  E-value: 1.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEFRK 108
Cdd:cd18631     2 YVVEKVLDRRVVKGKVEYLLKWKGYPDEDNTWEPEENL-DCPDLIAEFEE 50
Ank_4 pfam13637
Ankyrin repeats (many copies);
644-697 1.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1335749719 644 GTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVI 697
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
 59-106 1.89e-08

chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog beta (also known as HP1beta, CBX1, and chromobox 1), and related proteins. HP1beta is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3).


Pssm-ID: 349297  Cd Length: 50  Bit Score: 51.10  E-value: 1.89e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEF 106
Cdd:cd18650     2 YVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENL-DCPDLIAEF 48
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 603-732 2.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 603 NLDQEDSTGMTLVMLAAAGGQDDL--LRLLITKGAKVNGrqkngttalihaaeknfLTTVAILLEAGAFVNVQQSNGETA 680
Cdd:PHA03100  133 NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVYGFTP 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719 681 LMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFA-KQCNNVLVYELLKSH 732
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAiLNNNKEIFKLLLNNG 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 564-737 2.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 564 GEDEPFITTNrIPNNLLrDAVKNGDYIAVKVALNSneeynldqedstGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKN 643
Cdd:PHA02874   58 GADINHINTK-IPHPLL-TAIKIGAHDIIKLLIDN------------GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 644 GTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV 723
Cdd:PHA02874  124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                         170
                  ....*....|....
gi 1335749719 724 LVYELLKSHLETLS 737
Cdd:PHA02874  204 ACIKLLIDHGNHIM 217
CD_HP1gamma_Cbx3 cd18652
chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier ...
 59-106 5.92e-08

chromodomain of heterochromatin protein 1 homolog gamma; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog gamma (also known as HP1gamma, Cbx3, and Chromobox 3), and related proteins. HP1gamma is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. In addition to being involved in transcriptional silencing in heterochromatin-like complexes, HP1gamma also binds lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the protein may explain the association of heterochromatin with the inner nuclear membrane. HP1gamma is also recruited to sites of ultraviolet-induced DNA damage and double-strand breaks. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma.


Pssm-ID: 349299  Cd Length: 50  Bit Score: 49.62  E-value: 5.92e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEF 106
Cdd:cd18652     2 FVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENL-DCPELIEAF 48
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 580-744 6.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 6.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 580 LRDAVKNGDYIAVKVALNSNEEYNlDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTT 659
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 660 VAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQN-SALYFAKQCNNVLVYELLkshletLSR 738
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLF------IKR 224


                  ....*.
gi 1335749719 739 VAEETI 744
Cdd:PHA02875  225 GADCNI 230
CD_POL_like cd18970
chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup ...
 59-100 6.34e-08

chromodomain of Hypsizygus marmoreus TY3B-I_0 protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Hypsizygus marmoreus TY3B-I_0 protein, a putative TY3/gypsy retrotransposon polyprotein, and similar proteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349326  Cd Length: 49  Bit Score: 49.74  E-value: 6.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCK 100
Cdd:cd18970     1 FFVERILDERRRGRGWQYLVRWLGYGPSDDSWLPRRELEECE 42
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
 59-106 7.88e-08

chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. HP1a is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CD of Drosophila melanogaster HP1a.


Pssm-ID: 349300  Cd Length: 50  Bit Score: 49.26  E-value: 7.88e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEF 106
Cdd:cd18653     2 YAVEKICDRRVRKGKVEYYLKWKGYPETENTWEPEENL-DCQDLIQQY 48
CD_EhHp1_like cd18638
chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This ...
 59-108 8.43e-08

chromodomain of Entamoeba histolytica heterochromatin protein 1, and similar proteins; This subgroup includes the N-terminal CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 (HP1)-like protein from Entamoeba histolytica, and similar proteins. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349288  Cd Length: 52  Bit Score: 49.56  E-value: 8.43e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLE-DCKEVLLEFRK 108
Cdd:cd18638     2 FEVEKIVKKKTVKGGTEYFVKWKGYSAKENTWETEDNLEkSYKEMIDEFEK 52
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
 59-108 9.96e-08

chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349298  Cd Length: 50  Bit Score: 49.22  E-value: 9.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEFRK 108
Cdd:cd18651     2 YVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNL-DCPELISEFMK 50
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 645-784 1.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 645 TTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVL 724
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 725 VYELLKSHLETLSRVAEETIRDYFESRLALLEPVfPIACHRlcegPDFSTdfnymPPQNM 784
Cdd:PTZ00322  163 VVQLLSRHSQCHFELGANAKPDSFTGKPPSLEDS-PISSHH----PDFSA-----VPQPM 212
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-107 1.35e-07

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349322  Cd Length: 49  Bit Score: 48.82  E-value: 1.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDcKEVLLEFR 107
Cdd:cd18966     1 YEVERILAERRDDGGKRYLVKWEGYPLEEATWEPEENIGD-EELLKEWE 48
Ank_5 pfam13857
Ankyrin repeats (many copies);
663-717 1.48e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1335749719 663 LLEAGAF-VNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFA 717
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
 58-108 2.32e-07

chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of chromodomain-containing protein 1 (CHp1), and similar proteins. Chp1 is needed for RNA interference-dependent heterochromatin formation in fission yeast. Chp1 is a member of the RNA-induced transcriptional silencing (RITS) complex which maintains the heterochromatin regions. The chromodomain of the Chp1 component binds the histone H3 lysine 9 methylated tail (H3K9me) and the core of the nucleosome. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349286  Cd Length: 52  Bit Score: 48.22  E-value: 2.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  58 VFEVERIL-DMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18636     1 VYEVEDILaDRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKK 52
CD_SUV39H1_like cd18639
chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin ...
 59-108 2.77e-07

chromodomain of histone methyltransferase SUV39H1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of human SUV39H1, a histone lysine methyltransferase (HMT) which catalyzes di- and tri-methylation of lysine 9 of histone H3 (H3K9me2/3), leading to heterochromatin formation and gene silencing. H3K9me2/3 represents a specific mark for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3, and/or CBX5) proteins to methylated histones. SUV39H1 mainly functions in heterochromatin regions. The human SUV39H1/2, histone H3K9 methyltransferases, are the mammalian homologs of Drosophila Su(var)3-9 and Schizosaccharomyces pombe Clr4. SUV39H1 contains a chromodomain at its N-terminus and a SET domain at its C-terminus. Although the SET domain performs the catalytic activity, the chromodomain of SUV39H1 is essential for the catalytic activity of SUV39H1. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349289  Cd Length: 49  Bit Score: 47.90  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEdCKEVLLEFRK 108
Cdd:cd18639     1 YEVEYLCDYKKIREQEYYLVKWKGYPDSENTWEPRQNLK-CSRLLKQFHK 49
PTZ00121 PTZ00121
MAEBL; Provisional
 195-509 4.97e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 4.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  195 FDVKTKKRIWEVKEELK----DSKKPKKDEIKETKELKKANKRAEvrdlkiKIREdVKENRKTKKERYIESPLESESPND 270
Cdd:PTZ00121  1081 FDAKEDNRADEATEEAFgkaeEAKKTETGKAEEARKAEEAKKKAE------DARK-AEEARKAEDARKAEEARKAEDAKR 1153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  271 SLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEPK---EIKKLE 347
Cdd:PTZ00121  1154 VEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkaeAVKKAE 1233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  348 STNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSS--------RLSGEEKSLKSPDLAEEVKLVENLKSTDME 419
Cdd:PTZ00121  1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  420 KEKKNEPKGKYQ----------------KRYDLDKEEKARKEPKVLKSFKEIRNAFDlfKKTTEEKNDVLENNSKREEI- 482
Cdd:PTZ00121  1314 AKKADEAKKKAEeakkkadaakkkaeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADAAKKKAEEKk 1391

                          330       340       350
                   ....*....|....*....|....*....|
gi 1335749719  483 ---SLDSKIMNDNKTKDKCSLKEKRNTRDE 509
Cdd:PTZ00121  1392 kadEAKKKAEEDKKKADELKKAAAAKKKAD 1421
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
 56-98 1.38e-06

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 45.92  E-value: 1.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1335749719  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLED 98
Cdd:cd18644     1 DLVYAAEKILKKRVRKGKVEYLVKWKGWSNKHNTWEPEENILD 43
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
 56-109 1.38e-06

chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349294  Cd Length: 53  Bit Score: 45.82  E-value: 1.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1335749719  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKeVLLEFRKK 109
Cdd:cd18647     1 EQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPR-LLLAFQKK 53
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-108 1.82e-06

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349320  Cd Length: 54  Bit Score: 45.79  E-value: 1.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1335749719  59 FEVERIL----DMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18964     1 FFVERIIgrrpSARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAKLIEDFEK 54
CD_POL_like cd18977
chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This ...
 59-107 1.85e-06

chromodomain of a Rhizoctonia solani AG-3 Rhs1AP polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Rhizoctonia solani AG-3 Rhs1AP, a putative Ty3/Gypsy polyprotein/retrotransposon which includes a protease, a reverse transcriptase, a ribonuclease H, and an integrase domain, in that order, with a chromodomain at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349333  Cd Length: 57  Bit Score: 45.55  E-value: 1.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  59 FEVERILDMKCEGGKN----LYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFR 107
Cdd:cd18977     4 YEVEKIVGEKWKKRKNrrvkLYKVRFKGYGPEEDEWLTKEELKNAPEILAEWK 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 592-717 1.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 592 VKVALNSNEEYNLDQEDsTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVN 671
Cdd:PHA02878  150 TKLLLSYGADINMKDRH-KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1335749719 672 VQQSNGETALMKACKR-GNSDIVRLVIECGADCNILSKHQN-SALYFA 717
Cdd:PHA02878  229 ARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSS 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 625-729 2.26e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 625 DLLRLLITKGAKVNGRQKNGTTAL---IHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNS-DIVRLVIECG 700
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAG 107

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1335749719 701 ADCNILSKHQNSAL--YFAKQCNNVLVYELL 729
Cdd:PHA03095  108 ADVNAKDKVGRTPLhvYLSGFNINPKVIRLL 138
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
 56-106 4.06e-06

chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349334  Cd Length: 52  Bit Score: 44.61  E-value: 4.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPevhLED--CKEVLLEF 106
Cdd:cd18978     1 DESYEVEKIINHRGEKNRRKYLVKWKGYDDTDNSWVT---QEDfnDKDMIDEY 50
PHA03095 PHA03095
ankyrin-like protein; Provisional
 625-702 5.13e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 625 DLLRLLITKGAKVNGRQKNGTTALiHAAEKNFLT---TVAILLEAGAFVNVQQSNGETALMKACKRGNSDI--VRLVIEC 699
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFNInpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDA 176


                  ...
gi 1335749719 700 GAD 702
Cdd:PHA03095  177 GAD 179
CD_Cbx7 cd18646
chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of ...
 55-103 5.87e-06

chromodomain of chromobox homolog 7; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 7 (CBX7), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX7 has been shown to function as a tumor suppressor in lung carcinoma and an oncogene in gastric cancer and lymphoma.


Pssm-ID: 349293  Cd Length: 56  Bit Score: 44.31  E-value: 5.87e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1335749719  55 GEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVL 103
Cdd:cd18646     1 GEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVM 49
CD_MT_like cd18962
chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; ...
 56-108 7.48e-06

chromodomain of a putative Coemansia reversa NRRL 1564 methyltransferase, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Coemansia reversa NRRL 1564 SET (Su(var)3-9, enhancer-of-zeste, trithorax) domain-containing protein, and similar proteins. The SU(VAR)3-9 protein is the main chromocenter-specific histone H3-K9 methyltransferase (HMTase) in Drosophila where it plays a role in heterochromatic gene silencing. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349318  Cd Length: 52  Bit Score: 43.71  E-value: 7.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLeDCKEVLLEFRK 108
Cdd:cd18962     1 EGHYVVEAIVNDVLIDGKHMYEVKWEGYPSDHNNWVAEWDL-NDKEILRKYNK 52
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
 59-98 8.84e-06

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 43.53  E-value: 8.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLED 98
Cdd:cd18627     1 FAAECILKKRIRKGKVEYLVKWKGWSQKYNTWEPEENILD 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 605-702 1.20e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 605 DQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTA-------------------------------LIHAAE 653
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAlwnaisakhhkifrilyhfasisdphaagdlLCTAAK 631

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1335749719 654 KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 702
Cdd:PLN03192  632 RNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PTZ00121 PTZ00121
MAEBL; Provisional
 105-561 1.42e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  105 EFRKKLAENKAKA--VRKDiqrlslnndifEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMGKLKD-K 181
Cdd:PTZ00121  1395 EAKKKAEEDKKKAdeLKKA-----------AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEaK 1463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  182 FKTELESTSEIIGFDVKTKKRIWEVKEELKDSKKpKKDEIKETKELKKANKRAEVRDLKIKIREDVK--ENRKTKKERYI 259
Cdd:PTZ00121  1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKA 1542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  260 ESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQegIFEKHLDDLISIEEDAGtrvRRKKTKPRKFEE 339
Cdd:PTZ00121  1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEK---KMKAEEAKKAEE 1617

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  340 PK----EIKKLESTNAFLERraIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSRlsgEEKSLKSPDL----AEEVKLVE 411
Cdd:PTZ00121  1618 AKikaeELKKAEEEKKKVEQ--LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---EEDKKKAEEAkkaeEDEKKAAE 1692

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  412 NLKSTDMEKEKKNEPKGKY----QKRYDLDKEEKARK---EPKVLKSFKEIRNAFDLfKKTTEEKNDV----LENNSKRE 480
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKEaeekKKAEELKKAEEENKikaEEAKKEAEEDKKKAEEA-KKDEEEKKKIahlkKEEEKKAE 1771

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  481 EISLDSK--IMNDNKTKD-KCSLKEKRNTRDETDTWAYIaAEGDQEVSDSVCQTDETSDGRQPVLSLGMDLQLEwmKLED 557
Cdd:PTZ00121  1772 EIRKEKEavIEEELDEEDeKRRMEVDKKIKDIFDNFANI-IEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE--EADA 1848


                   ....
gi 1335749719  558 FQKH 561
Cdd:PTZ00121  1849 FEKH 1852
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
572-681 1.59e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.64  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 572 TNRIPNNLLRDAVKNGDYIAVKVALNSNEeyNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 651
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGA--DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                          90       100       110
                  ....*....|....*....|....*....|
gi 1335749719 652 AEKNFLTTVAILLEAGAFVNVQQSNGETAL 681
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 571-697 1.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 571 TTNRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLdqEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIH 650
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI--EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1335749719 651 AAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRgNSDIVRLVI 697
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI 242
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 603-717 2.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 603 NLDQEDSTGMTLVMLAAAGGQD-DLLRLLITKGAKVNGRQKNGTTALIHAAEKN-FLTTVAILLEAGAFVNVQQSNGETA 680
Cdd:PHA02876  299 DVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTP 378

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1335749719 681 LMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFA 717
Cdd:PHA02876  379 IHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
CD_POL_like cd18972
chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and ...
 59-108 2.68e-05

chromodomain of a Moniliophthora perniciosa FA553 putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Moniliophthora perniciosa FA553 putative retrotelement polyprotein, which includes domains in the following order: a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related "chromo shadow" domain


Pssm-ID: 349328  Cd Length: 50  Bit Score: 42.12  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18972     1 YEVEAIVGHKPKKKPRQFLVSWLGYDSSHNEWKQKEELENARELLQDYLK 50
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
 76-108 2.75e-05

chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in chromodomain of Drosophila melanogaster chromator (also known as Chriz/Chro) chromodomain protein, and similar proteins. Chromator is a nuclear protein that plays a role in proper spindle dynamics during mitosis. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349290  Cd Length: 52  Bit Score: 42.28  E-value: 2.75e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1335749719  76 YKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18640    20 YLVKWENRSHHENTWEPMANLERCKYLLQMFEK 52
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 676-705 2.96e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 2.96e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1335749719 676 NGETALMKACKRGNSDIVRLVIECGADCNI 705
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
chromodomain cd18969
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members ...
 56-108 3.73e-05

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; for most members of this subgroup, the chromodomain is followed by a chromo shadow domain; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. For the majority of members of this subgroup, the chromodomain is followed by a chromo shadow domain (CSD).


Pssm-ID: 349325  Cd Length: 56  Bit Score: 42.13  E-value: 3.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1335749719  56 EDVFEVERILDMKCEG---GKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRK 108
Cdd:cd18969     1 EEEYEIEEILDVKKGGfedGKLAYFVKWKGYPSSENSWVTEEDAANAQEMIEEYWK 56
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
 59-93 3.94e-05

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 41.76  E-value: 3.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPE 93
Cdd:cd18975     1 YEVESILNSRLHRGKLQYLIQWKGYPLEEASWELE 35
PTZ00121 PTZ00121
MAEBL; Provisional
 135-481 4.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  135 DSDSDQQSDTKEDISPRKKKKKIKCKEETSP---EDLRKKRTKMGKLKDKFKTELESTSEiigfDVKTKKRIWEVKEELK 211
Cdd:PTZ00121  1078 DFDFDAKEDNRADEATEEAFGKAEEAKKTETgkaEEARKAEEAKKKAEDARKAEEARKAE----DARKAEEARKAEDAKR 1153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  212 DSKKPKKDEIKETKELKKAN--KRAEVRDLKIKIREdVKENRKTKKERYIESPLESESPNDsliLEDDSEDFISDNREEN 289
Cdd:PTZ00121  1154 VEIARKAEDARKAEEARKAEdaKKAEAARKAEEVRK-AEELRKAEDARKAEAARKAEEERK---AEEARKAEDAKKAEAV 1229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  290 QNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEPKEIKKLESTNAFLERRAIPKKQRNQDKGI 369
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  370 SNLELNKlpspvfAQTLKSSRLSGEEKSLKSPDLAEEVKLVENLKSTDMEKEKKNEPKGKYQKRYDLDKEEKARKEPKVL 449
Cdd:PTZ00121  1310 KAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1335749719  450 -KSFKEIRNAFDLFKKTTEEKNDVLENNSKREE 481
Cdd:PTZ00121  1384 kKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
 58-108 4.06e-05

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349316  Cd Length: 51  Bit Score: 41.78  E-value: 4.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  58 VFEVERILDMKC-EGGKNLYKVRWKGYTSEDDTWEPEVHLEdCKEVLLEFRK 108
Cdd:cd18960     1 VFVVERILDKRLgRNGGEEFLIKWQGFPESDSSWEPRENLQ-CDEMLEEFEK 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
611-664 4.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1335749719 611 GMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILL 664
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
CD_CEC-4_like cd18961
chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin ...
 59-108 5.09e-05

chromodomain of Caenorhabditis elegans chromodomain protein 4, and similar proteins; CHRomatin Organization Modifier (chromo) domain of Caenorhabditis elegans CEC-4, and similar proteins. CEC-4 is a perinuclear heterochromatin anchor, it mediates the anchoring of H3K9 methylation-bearing chromatin at the nuclear periphery in early to mid-stage embryos. It is necessary for anchoring, but does not affect transcriptional repression. CEC-4 contributes to the efficiency with which muscle differentiation is induced following ectopic expression of the master regulator, HLH-1 (MyoD in mammals). A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349317  Cd Length: 51  Bit Score: 41.32  E-value: 5.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719  59 FEVERILDMKCEGGKNLYKVRWKGYTSEDDT---WEPEvhLEDCKEVLLEFRK 108
Cdd:cd18961     1 YEVEKILSHRIVNGKPLYLVMWVGYPGPVENsemWEED--LKNCGELLKAYKD 51
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 676-705 5.98e-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: 40.65  E-value: 5.98e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1335749719  676 NGETALMKACKRGNSDIVRLVIECGADCNI 705
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
 55-100 6.34e-05

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 41.24  E-value: 6.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1335749719  55 GEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCK 100
Cdd:cd18649     1 GERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDAR 46
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 572-734 9.44e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 572 TNRIPNNLLRDAVKNGDYIAVKVALnsneeYNLDQEDSTGMTLVMLAA---AGGQDDLLRLLITKGAK------VNGRQK 642
Cdd:TIGR00870  48 PDRLGRSALFVAAIENENLELTELL-----LNLSCRGAVGDTLLHAISleyVDAVEAILLHLLAAFRKsgplelANDQYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 643 N----GTTALIHAAEKNFLTTVAILLEAGAFVNV----------QQSN----GETALMKACKRGNSDIVRLVIECGAD-- 702
Cdd:TIGR00870 123 SeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADil 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1335749719 703 ------------CNILSKHQNSALYFAKQCnnvlvYELLKSHLE 734
Cdd:TIGR00870 203 tadslgntllhlLVMENEFKAEYEELSCQM-----YNFALSLLD 241
PHA02798 PHA02798
ankyrin-like protein; Provisional
 625-734 9.80e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 9.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 625 DLLRLLITKGAKVNGRQKNGTTALIHAAE-----KNFLTTVAILLEAGAFVNVQQSNGETALMKACKRG---NSDIVRLV 696
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFM 131

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1335749719 697 IECGADCNILSKHQNSALYFAKQCNNVLVYELLKSHLE 734
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLE 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 606-699 1.70e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 606 QEDSTGMTLVMLA------AAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGET 679
Cdd:PTZ00322   71 EEVIDPVVAHMLTvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                          90       100
                  ....*....|....*....|
gi 1335749719 680 ALMKACKRGNSDIVRLVIEC 699
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRH 170
CD_Rhino cd18630
chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin ...
 58-106 2.01e-04

chromodomain of Drosophila melanogaster Rhino, and similar proteins; N-terminal CHRomatin Organization Modifier (chromo) domain of Drosophila melanogaster Rhino (also known as heterochromatin protein 1-like), and similar proteins. Rhino is a female-specific protein that affects chromosome structure and egg polarity that is required for germline PIWI-interacting RNA (piRNA) production. In Drosophila the RDC (rhino, deadlock, and cutoff) complex, composed of rhino, the protein deadlock (Del) and the Rai1-like transcription termination cofactor cutoff (Cuff) binds to chromatin of dual-strand piRNA clusters, special genomic regions, which encode piRNA precursors. The RDC complex is anchored to H3K9me3-marked chromatin in part via the H3K9me3-binding activity of Rhino, and is required for transcription of piRNA precursors. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349280  Cd Length: 51  Bit Score: 39.81  E-value: 2.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1335749719  58 VFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEF 106
Cdd:cd18630     1 EYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENLGNCMKLVADY 49
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 676-708 2.37e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1335749719 676 NGETALMKACKR-GNSDIVRLVIECGADCNILSK 708
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 575-734 3.02e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 575 IPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRllITKGAKVnGRQKnGTTALIHAAEK 654
Cdd:PLN03192  493 ILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLK--AKLDPDI-GDSK-GRTPLHIAASK 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 655 NFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNilSKHQNSALYFAKQCNNV-LVYELLKSHL 733
Cdd:PLN03192  569 GYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLtAMKELLKQGL 646


                  .
gi 1335749719 734 E 734
Cdd:PLN03192  647 N 647
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
 56-109 3.89e-04

chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer.


Pssm-ID: 349292  Cd Length: 55  Bit Score: 39.27  E-value: 3.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1335749719  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKeVLLEFRKK 109
Cdd:cd18645     1 EHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPR-LLIAFQNR 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 624-728 4.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 624 DDLLRLLITKGAKVNGRQKNGTTALiHAAEKNFLT--TVAILLEAGAFVNVQQS-NGETALMKACKrgNSDIVRLVIECG 700
Cdd:PHA02878  214 KPIVHILLENGASTDARDKCGNTPL-HISVGYCKDydILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYG 290

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1335749719 701 ADCNILSKHQNSAL------YFAKQCNNVLVYEL 728
Cdd:PHA02878  291 ADINSLNSYKLTPLssavkqYLCINIGRILISNI 324
CD_Swi6_like cd18637
chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a ...
 59-103 6.14e-04

chromodomain of fission yeast Swi6, and similar proteins; Fission yeast Swi6 protein is a structural and functional homolog of mammalian HP1 (heterochromatin protein 1) and is involved in the chromatin structure by binding to centromeres, telomeres, and the silent mating-type locus. Swi6 contains a N-terminal chromo (CHRromatin Organization MOdifier) domain and a C-terminal chromo shadow domain (CSD). Swi6 binds histone H3 tails methylated at Lys- and the cohesion subunit Psc3, leading to silencing the genes and sister chromatid cohesion. It is also involved in the repression of the silent mating-type loci MAT2 and MAT3. Swi6 may compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes. chromodomains mediate the interaction of the heterochromatin with other heterochromatin proteins, thereby affecting chromatin structure (e.g. Drosophila and human heterochromatin protein (HP1) and mammalian modifier 1 and modifier 2). CSDs have only been found in proteins that also possess a chromodomain.


Pssm-ID: 349287  Cd Length: 54  Bit Score: 38.64  E-value: 6.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1335749719  59 FEVERILD--MKCEGGKNLYKVRWKGYTSEDD-TWEPEVHLEDCKEVL 103
Cdd:cd18637     2 YVVEKILKhrMARKGGGYEYLLKWEGYDDPSDnTWSSEADCAGCKDLI 49
CD_POL_like cd18971
chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar ...
 59-100 7.78e-04

chromodomain of a Magnaporthe grisea putative retrotransposon polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in a Magnaporthe grisea putative retrotransposon polyprotein which includes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349327  Cd Length: 50  Bit Score: 38.14  E-value: 7.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1335749719  59 FEVERILDMK---CEGGKNLYKVRWKGYtsEDDTWEPEVHLEDCK 100
Cdd:cd18971     1 YEVEEILAARrrrIRGKGREVLVKWVGY--AEPTWEPLDNLADTA 43
PHA02798 PHA02798
ankyrin-like protein; Provisional
 625-720 1.17e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 625 DLLRLLITKGAKVNGRQKNGTT---ALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNS---DIVRLVIE 698
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                          90       100
                  ....*....|....*....|..
gi 1335749719 699 CGADCNIlskHQNSALYFAKQC 720
Cdd:PHA02798  170 KGVDINT---HNNKEKYDTLHC 188
chromodomain cd18967
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
 59-108 1.25e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349323  Cd Length: 55  Bit Score: 37.61  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1335749719  59 FEVERIL-----DMKCEGGKN---LYKVRWKGYtsEDDTWEPEVHLEDCKeVLLEFRK 108
Cdd:cd18967     1 WEIEAILahhmsDPRTHPGKPatmLYLTKWEGF--PDETWEPAESFDDRK-ILHDYRR 55
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 653-723 1.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1335749719 653 EKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV 723
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 219-509 2.65e-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: 41.50  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  219 DEIKETKELKKANKRAEVRDLKIKIREdVKENRKTKKERYIEsplESESPNDSLILEDDSEDFISDNRE-ENQNVRSVRD 297
Cdd:pfam02463  168 KRKKKEALKKLIEETENLAELIIDLEE-LKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLkLNEERIDLLQ 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  298 KTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEpKEIKKLESTNAFLERRAIPKKQRNQDKG----ISNLE 373
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE-EELKLLAKEEEELKSELLKLERRKVDDEeklkESEKE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  374 LNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEVKLVENLKSTDMEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFK 453
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1335749719  454 EIRNA------FDLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKTKDKCSLKEKRNTRDE 509
Cdd:pfam02463  403 EEKEAqlllelARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
Ank_5 pfam13857
Ankyrin repeats (many copies);
637-681 3.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1335749719 637 VNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETAL 681
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
CD_Cbx6 cd18648
chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of ...
 56-114 3.49e-03

chromodomain of chromobox homolog 6; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 6 (CBX6), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349295  Cd Length: 58  Bit Score: 36.57  E-value: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1335749719  56 EDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKeVLLEFRKKLAENK 114
Cdd:cd18648     1 ERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSR-LIAAFEQKERERE 58
Ank_4 pfam13637
Ankyrin repeats (many copies);
679-723 3.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1335749719 679 TALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNV 723
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 573-705 3.71e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 573 NRIPNNLLRDAVKNG---DYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDD---LLRLLITKGAKVNGR-QKNGT 645
Cdd:PHA02736   14 DIEGENILHYLCRNGgvtDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKeRVFGN 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1335749719 646 TAL-IHAAEKNFltTVAILLEAGAFVNVQQSN--GETALMKACKRGNSDIVRLVIECGADCNI 705
Cdd:PHA02736   94 TPLhIAVYTQNY--ELATWLCNQPGVNMEILNyaFKTPYYVACERHDAKMMNILRAKGAQCKV 154
COG5022 COG5022
Myosin heavy chain [General function prediction only];
91-494 3.80e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.22  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719   91 EPEVHLEDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEAdsdSDQQSDTKEDISPRKKKKKIKCKEETspEDLRK 170
Cdd:COG5022    865 KKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEI---IELKKSLSSDLIENLEFKTELIARLK--KLLNN 939

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  171 KRTKMGKLKDK-----------FKTELESTSEIIGFDVKTKKriwEVKEELKDSK---KPKKDEIKETKELKKA--NKRA 234
Cdd:COG5022    940 IDLEEGPSIEYvklpelnklheVESKLKETSEEYEDLLKKST---ILVREGNKANselKNFKKELAELSKQYGAlqESTK 1016

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  235 EVRDLKIKIREDVKENRKTKKERYIESPLESESPndsliLEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLD 314
Cdd:COG5022   1017 QLKELPVEVAELQSASKIISSESTELSILKPLQK-----LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTEN 1091

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  315 DLISIEEDAGTRVRRKKTKPR-----------KFEEPKEIKK-LESTNAFLERRAIPKKQRNQDKGISNLELN---KLPS 379
Cdd:COG5022   1092 LLKTINVKDLEVTNRNLVKPAnvlqfivaqmiKLNLLQEISKfLSQLVNTLEPVFQKLSVLQLELDGLFWEANleaLPSP 1171

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  380 PVFAQTLKSSRLSGEEKSLKSPDLAEEVKLVENLKSTDMEKEKKNEPKGKYQKryDLDKEEKARKEpkVLKSFKEIRNAF 459
Cdd:COG5022   1172 PPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLK--KLISEGWVPTE--YSTSLKGFNNLN 1247

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1335749719  460 DLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKT 494
Cdd:COG5022   1248 KKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVL 1282
Ank_5 pfam13857
Ankyrin repeats (many copies);
596-651 4.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1335749719 596 LNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHA 651
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 600-726 4.72e-03

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: 40.38  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 600 EEYNLDQEDSTGMTLVMLAAAGGQ-DDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAG-AFVNVQQSN- 676
Cdd:cd22192     6 DELHLLQQKRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTSd 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1335749719 677 ---GETALMKACKRGNSDIVRLVIECGADcniLSKHQNSALYFAKQCNNVLVY 726
Cdd:cd22192    86 lyqGETALHIAVVNQNLNLVRELIARGAD---VVSPRATGTFFRPGPKNLIYY 135
PHA03095 PHA03095
ankyrin-like protein; Provisional
 625-767 7.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 625 DLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAI--LLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGAD 702
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1335749719 703 CNILSKHQNSALYFA-KQCNNVLVYELLKSHLETlsRVAEETIrDYFESRLALLepvfPIACHRLC 767
Cdd:PHA03095  283 INAVSSDGNTPLSLMvRNNNGRAVRAALAKNPSA--ETVAATL-NTASVAGGDI----PSDATRLC 341
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
 57-110 7.74e-03

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 35.73  E-value: 7.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719  57 DVFEVERILDMK-CEGGKNL-----YKVRWKGYTSEDDTWEPEvhlEDCKEVLLEFRKKL 110
Cdd:cd18663     2 DYVEVDRILDVSvSTDPNTGepvthYLVKWCSLPYEDSTWELE---EDVDPAKIEEFEKL 58
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 623-704 8.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 623 QDDLL--RLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECG 700
Cdd:PHA02876  155 QDELLiaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234


                  ....
gi 1335749719 701 ADCN 704
Cdd:PHA02876  235 SNIN 238
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 202-302 9.33e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 39.45  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335749719 202 RIWEVKEELKDSKKPKKDEIKETKELKK--ANKRAEVRDlkiKIREDVKENRKTKKERYIESPLESESPNDSLILEDDSE 279
Cdd:PRK00247  321 RAPELHAENAEIKKTRTAEKNEAKARKKeiAQKRRAAER---EINREARQERAAAMARARARRAAVKAKKKGLIDASPNE 397

                          90       100
                  ....*....|....*....|...
gi 1335749719 280 DFISDNREENQNVRSVRDKTAQE 302
Cdd:PRK00247  398 DTPSENEESKGSPPQVEATTTAE 420
CD_POL_like cd18976
chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup ...
 61-106 9.93e-03

chromodomain of uncharacterized putative retroelement polyprotein proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in uncharacterized putative retrotransposon proteins, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349332  Cd Length: 51  Bit Score: 35.24  E-value: 9.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1335749719  61 VERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLED-CKEVLLEF 106
Cdd:cd18976     3 VESLLDRRKVRGQVQYLVKWRGFPRSEATWEPREELMRrCAELVAAY 49
 
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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