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Conserved domains on  [gi|1953419023|ref|XP_038304813|]
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dystrophin isoform X12 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
2891-3052 2.82e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


:

Pssm-ID: 320004  Cd Length: 162  Bit Score: 356.65  E-value: 2.82e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2891 SLSAACDALDQHNLKQNDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 2970
Cdd:cd16246      1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2971 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3050
Cdd:cd16246     81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                   ..
gi 1953419023 3051 MR 3052
Cdd:cd16246    161 MR 162
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3077-3125 5.83e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


:

Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 5.83e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023 3077 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3125
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
116-330 2.64e-26

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 109.46  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  116 YQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIgtgKLSEDEETEVQEQ 195
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  196 MNLLNSRWECLRVASMEKQSNLHKVLMDLQ-NQQLKELNDWLTKTEERtrkMEKEPLGPDIEDLKRQVQQHKVLQEDLEQ 274
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023  275 EQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 330
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1878-2091 2.55e-23

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.98  E-value: 2.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1878 KWRRFHYDMKILNQWLTEAEQFLKKTQIPENWEHAK-YKWYLKELQDGIGQRQSVVRVLNATGEEIIQQSSKtDASILQE 1956
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1957 KLGSLNLRWQEVCKQLAERKKRLEEQKNiLSEFQRDVNEFVLWLEEADNVANIPLEPGNEQQLKEKLEQVKLLAEELPLR 2036
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 2037 QGILKQLNETGGTVLVSAPlsPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEA 2091
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2456-2699 8.69e-22

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 96.36  E-value: 8.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2456 LLQQFPLDLEKFLAWLTEAETTANVLQDAthkerllEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLRslEGS 2535
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2536 DDAALLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2615
Cdd:cd00176     72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2616 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTQWEKLNVHSADWQRKI 2695
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                   ....
gi 1953419023 2696 DEAL 2699
Cdd:cd00176    210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2238-2454 1.29e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 90.20  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2238 LADFNRAWTELTDWLSLLDRVIKSQrVMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2317
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2318 DRIERIQSQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEAPYTVDAIQKKITETKQLAKDLR 2397
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953419023 2398 QWQINVDVANDLALKLLRDYSADDTRKVHMITENINASWASIHKRLSEREAALEETH 2454
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
822-1036 3.74e-14

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 74.02  E-value: 3.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  822 KLRKIQNHIKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEfAGRLE 901
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  902 TELRELNTQWDYMCRQVYARKEALKGGLDKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQTAVEEMKRAKEEAQ 981
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023  982 QKEAKVKLLTESVNSVIAQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEE 1036
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
499-705 2.01e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 2.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  499 DITELHSWITRSEAVLQSPEFAiyRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 578
Cdd:cd00176      8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  579 QLNSRWIEFCQLLSERLNWLEYQNNIITFYNQLQQLEQMTTTAENWLKTQPTTTSePTAIKSQLKICKDEINRLSALQPQ 658
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023  659 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFNQVFADVQAREKELQ 705
Cdd:cd00176    162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
899-1709 4.11e-13

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 4.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  899 RLETELRELNTQWDYMCRQV-----YAR-KEALKggldktvSLQKDLSEMHewMTQAEEEYLERDFEYKtpdELQTAVEE 972
Cdd:TIGR02168  190 RLEDILNELERQLKSLERQAekaerYKElKAELR-------ELELALLVLR--LEELREELEELQEELK---EAEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  973 MKRAKEEAQQKEAKVKLLTESVNSVIaQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKAN 1052
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1053 KWLSEVEVKLkttenisggaEEIAEVLDSLENLMQHSEDnpnqirilaqtltdggvmdelINEELETFNSRWRELHEEAV 1132
Cdd:TIGR02168  337 EELAELEEKL----------EELKEELESLEAELEELEA---------------------ELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1133 RRQKLLEQSIQSaqeIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQK--IQSDLTSHEISLEEMKKHNQGKETA 1210
Cdd:TIGR02168  386 SKVAQLELQIAS---LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1211 QRVLS-QIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEvkmhlpalETKSVEQEvvQSQLNHCVNLYKSLSEVK 1289
Cdd:TIGR02168  463 LEELReELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE--------GVKALLKN--QSGLSGILGVLSELISVD 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1290 SEVEMVIktgrqivqkkqtenpkelderVTALKLHyneLGAKVTERKQQLEKC---LKLSRKMRKEMNALTEW----LAA 1362
Cdd:TIGR02168  533 EGYEAAI---------------------EAALGGR---LQAVVVENLNAAKKAiafLKQNELGRVTFLPLDSIkgteIQG 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1363 TDMELTKRsaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEAL--KTVLGKKEMLVEDKLSLLNSNWIaVTSRA 1440
Cdd:TIGR02168  589 NDREILKN--IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALelAKKLRPGYRIVTLDGDLVRPGGV-ITGGS 665
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1441 EEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLDESEKKKpQQKEDILKRLKAEMNDIRPKVDSTRDQAANL------ 1514
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1515 ---MANRGDHCRKVVEPKISELNHRFAAISHRIKTGKAsiplkELEQFNSDIQKLLEPLEAEIQQGVNLKEEdfnkdmse 1591
Cdd:TIGR02168  745 leeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDELRAE-------- 811
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1592 dnegtVKELLQRGDNLQQRITDERKReeIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY---KRQADDLLKCLDD 1668
Cdd:TIGR02168  812 -----LTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERAS 884
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1669 IEKKLASLPEPRD---------ERKIKEIDRELQKKKEELNAVRRQAEGL 1709
Cdd:TIGR02168  885 LEEALALLRSELEelseelrelESKRSELRRELEELREKLAQLELRLEGL 934
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
715-925 3.29e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 68.63  E-value: 3.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  715 RYQETMSTILTWIQQSETKLSIPQVTVTEYDIMEQRLgELQALQSSLQEQQNGLNYLSTTVKEMSKKAPlsDISRKYQSE 794
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  795 FEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIKtLKKWITEVDVFLKEEWPaLGDSEILKRQLKQCRLLVNDIQTI 874
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953419023  875 QPSLNSVNEGAQKMKNEAEPEFAGRLETELRELNTQWDYMCRQVYARKEAL 925
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2700-2806 5.57e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


:

Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 61.95  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2700 ERLQELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYN 2779
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1953419023 2780 LNTLEDLNTRWKLLQVAIEDRIRQLHE 2806
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
2825-2854 7.08e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 7.08e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953419023 2825 GPWERAISPNKVPYYINHETQTTCWDHPKM 2854
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
332-599 3.33e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 50.91  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  332 KWQRFTEEQCLFSAWLSEKEDAVNKIHTTgfKDQSEVLSNLQKLAVLKTDLEKKKQTMDKLCSLNQDLLSAlkNTVVAHK 411
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  412 MEAWLDNFAQRWDNLVQKLEkssaqisqavtttqpsltqttvmetvtmvttrehilvkhaqeelpppppqKKRQIIVDSE 491
Cdd:cd00176     77 IQERLEELNQRWEELRELAE--------------------------------------------------ERRQRLEEAL 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  492 IRKRLDVDITELHSWITRSEAVLQSPEfaIYRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 571
Cdd:cd00176    107 DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                          250       260
                   ....*....|....*....|....*...
gi 1953419023  572 SIKQASEQLNSRWIEFCQLLSERLNWLE 599
Cdd:cd00176    183 EIEEKLEELNERWEELLELAEERQKKLE 210
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1651-1875 4.61e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 50.52  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1651 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1723
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1724 Q--LSKRWREIESKFAQFRRLnfaqihtvheesvvamtedmpLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCaQDF 1801
Cdd:cd00176     81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1802 EDLFKQEESLKNIKDSLQQISGRIDIIHNKKTAALHSATPAERAKLQEALSRLDFQWERVNNMYKDRQGRFDRS 1875
Cdd:cd00176    139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1-17 5.05e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


The actual alignment was detected with superfamily member cd21233:

Pssm-ID: 444660  Cd Length: 111  Bit Score: 39.14  E-value: 5.05e-03
                           10
                   ....*....|....*..
gi 1953419023    1 MYITSLFQVLPQQVSIE 17
Cdd:cd21233     95 MYVTSLFQVLPQQVSIE 111
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
2891-3052 2.82e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 356.65  E-value: 2.82e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2891 SLSAACDALDQHNLKQNDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 2970
Cdd:cd16246      1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2971 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3050
Cdd:cd16246     81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                   ..
gi 1953419023 3051 MR 3052
Cdd:cd16246    161 MR 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
2855-2973 6.35e-57

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430392  Cd Length: 123  Bit Score: 193.51  E-value: 6.35e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2855 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQVINCLTTIYDRLEQEHN 2932
Cdd:pfam09068    1 TELMQELQDFNNIRFSAYRTAMKLRALQKRLCLDLVDLWNLIEAFDEHGLNslENDLLLDVSELETLLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1953419023 2933 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 2973
Cdd:pfam09068   81 TthQVNVPLSVDLLLNWLLNVYDPQRTGKIRVLSFKVALVLLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3077-3125 5.83e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 5.83e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023 3077 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3125
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
116-330 2.64e-26

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 109.46  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  116 YQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIgtgKLSEDEETEVQEQ 195
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  196 MNLLNSRWECLRVASMEKQSNLHKVLMDLQ-NQQLKELNDWLTKTEERtrkMEKEPLGPDIEDLKRQVQQHKVLQEDLEQ 274
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023  275 EQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 330
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1878-2091 2.55e-23

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.98  E-value: 2.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1878 KWRRFHYDMKILNQWLTEAEQFLKKTQIPENWEHAK-YKWYLKELQDGIGQRQSVVRVLNATGEEIIQQSSKtDASILQE 1956
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1957 KLGSLNLRWQEVCKQLAERKKRLEEQKNiLSEFQRDVNEFVLWLEEADNVANIPLEPGNEQQLKEKLEQVKLLAEELPLR 2036
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 2037 QGILKQLNETGGTVLVSAPlsPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEA 2091
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2456-2699 8.69e-22

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 96.36  E-value: 8.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2456 LLQQFPLDLEKFLAWLTEAETTANVLQDAthkerllEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLRslEGS 2535
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2536 DDAALLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2615
Cdd:cd00176     72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2616 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTQWEKLNVHSADWQRKI 2695
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                   ....
gi 1953419023 2696 DEAL 2699
Cdd:cd00176    210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2238-2454 1.29e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 90.20  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2238 LADFNRAWTELTDWLSLLDRVIKSQrVMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2317
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2318 DRIERIQSQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEAPYTVDAIQKKITETKQLAKDLR 2397
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953419023 2398 QWQINVDVANDLALKLLRDYSADDTRKVHMITENINASWASIHKRLSEREAALEETH 2454
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3073-3118 8.77e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 8.77e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953419023 3073 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3118
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3074-3117 2.12e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.12e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1953419023  3074 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3117
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
822-1036 3.74e-14

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 74.02  E-value: 3.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  822 KLRKIQNHIKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEfAGRLE 901
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  902 TELRELNTQWDYMCRQVYARKEALKGGLDKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQTAVEEMKRAKEEAQ 981
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023  982 QKEAKVKLLTESVNSVIAQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEE 1036
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
499-705 2.01e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 2.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  499 DITELHSWITRSEAVLQSPEFAiyRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 578
Cdd:cd00176      8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  579 QLNSRWIEFCQLLSERLNWLEYQNNIITFYNQLQQLEQMTTTAENWLKTQPTTTSePTAIKSQLKICKDEINRLSALQPQ 658
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023  659 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFNQVFADVQAREKELQ 705
Cdd:cd00176    162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
899-1709 4.11e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 4.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  899 RLETELRELNTQWDYMCRQV-----YAR-KEALKggldktvSLQKDLSEMHewMTQAEEEYLERDFEYKtpdELQTAVEE 972
Cdd:TIGR02168  190 RLEDILNELERQLKSLERQAekaerYKElKAELR-------ELELALLVLR--LEELREELEELQEELK---EAEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  973 MKRAKEEAQQKEAKVKLLTESVNSVIaQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKAN 1052
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1053 KWLSEVEVKLkttenisggaEEIAEVLDSLENLMQHSEDnpnqirilaqtltdggvmdelINEELETFNSRWRELHEEAV 1132
Cdd:TIGR02168  337 EELAELEEKL----------EELKEELESLEAELEELEA---------------------ELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1133 RRQKLLEQSIQSaqeIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQK--IQSDLTSHEISLEEMKKHNQGKETA 1210
Cdd:TIGR02168  386 SKVAQLELQIAS---LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1211 QRVLS-QIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEvkmhlpalETKSVEQEvvQSQLNHCVNLYKSLSEVK 1289
Cdd:TIGR02168  463 LEELReELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE--------GVKALLKN--QSGLSGILGVLSELISVD 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1290 SEVEMVIktgrqivqkkqtenpkelderVTALKLHyneLGAKVTERKQQLEKC---LKLSRKMRKEMNALTEW----LAA 1362
Cdd:TIGR02168  533 EGYEAAI---------------------EAALGGR---LQAVVVENLNAAKKAiafLKQNELGRVTFLPLDSIkgteIQG 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1363 TDMELTKRsaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEAL--KTVLGKKEMLVEDKLSLLNSNWIaVTSRA 1440
Cdd:TIGR02168  589 NDREILKN--IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALelAKKLRPGYRIVTLDGDLVRPGGV-ITGGS 665
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1441 EEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLDESEKKKpQQKEDILKRLKAEMNDIRPKVDSTRDQAANL------ 1514
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1515 ---MANRGDHCRKVVEPKISELNHRFAAISHRIKTGKAsiplkELEQFNSDIQKLLEPLEAEIQQGVNLKEEdfnkdmse 1591
Cdd:TIGR02168  745 leeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDELRAE-------- 811
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1592 dnegtVKELLQRGDNLQQRITDERKReeIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY---KRQADDLLKCLDD 1668
Cdd:TIGR02168  812 -----LTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERAS 884
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1669 IEKKLASLPEPRD---------ERKIKEIDRELQKKKEELNAVRRQAEGL 1709
Cdd:TIGR02168  885 LEEALALLRSELEelseelrelESKRSELRRELEELREKLAQLELRLEGL 934
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
715-925 3.29e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 68.63  E-value: 3.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  715 RYQETMSTILTWIQQSETKLSIPQVTVTEYDIMEQRLgELQALQSSLQEQQNGLNYLSTTVKEMSKKAPlsDISRKYQSE 794
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  795 FEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIKtLKKWITEVDVFLKEEWPaLGDSEILKRQLKQCRLLVNDIQTI 874
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953419023  875 QPSLNSVNEGAQKMKNEAEPEFAGRLETELRELNTQWDYMCRQVYARKEAL 925
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1896-2584 4.39e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.78  E-value: 4.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1896 AEQFLKKTQIPENWEHAKYKWYLKELQDGIGQRQSVVRVLnatgeEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLAER 1975
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQEELKEA-----EEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1976 KKRLEEQKNILSEFQRDVNEFVlwlEEADNVANIPLEPG-----NEQQLKEKLEQVKLLAEELPLRQGILKQLNEtggtv 2050
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILR---ERLANLERQLEELEaqleeLESKLDELAEELAELEEKLEELKEELESLEA----- 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2051 lvSAPLSPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQLEIYNQPNQTGPFD 2130
Cdd:TIGR02168  359 --ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2131 --------IKEIEVAVQAKQPDVEGILSKGQHLYKEKP-ATQPAKRKLEDLSSDWKVVTQLLQELRAKQPGPAPGLTTVR 2201
Cdd:TIGR02168  437 elqaeleeLEEELEELQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2202 APPSQTVTLVTQPAVTK--ETAISKLEMPSSLLLEVPALADFNRA-----WTELTDWLSLLDRVIKSQRVMVGDLEDINE 2274
Cdd:TIGR02168  517 GLSGILGVLSELISVDEgyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2275 mIIKQKATLQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD----------------------- 2318
Cdd:TIGR02168  597 -IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssile 674
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2319 ---RIERIQSQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEAPYTVDAIQKKITETKQLAKD 2395
Cdd:TIGR02168  675 rrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2396 LRQWQINVDVANDLALKLLRDYSADDTRKVHMITENINA---SWASIHKRLSEREAALEETHRLLQQFPLDLEKFLAWLT 2472
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2473 EAETTANVLQDAthKERLLEDSKGVRELMKQWQDLQGEIEAhtDIYHNLDENGQKVLRSLEGSDDAALLQRRLDNMNFKW 2552
Cdd:TIGR02168  835 ATERRLEDLEEQ--IEELSEDIESLAAEIEELEELIEELES--ELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          730       740       750
                   ....*....|....*....|....*....|..
gi 1953419023 2553 SELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2584
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SPEC smart00150
Spectrin repeats;
1880-1980 1.54e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 1.54e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  1880 RRFHYDMKILNQWLTEAEQFLKKTQIPENWEHAKYKW-YLKELQDGIGQRQSVVRVLNATGEEIIQQSSKtDASILQEKL 1958
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1953419023  1959 GSLNLRWQEVCKQLAERKKRLE 1980
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1877-1981 4.12e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 62.34  E-value: 4.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1877 EKWRRFHYDMKILNQWLTEAEQFLKKTQIPENWEH--AKYKWYlKELQDGIGQRQSVVRVLNATGEEIIQqSSKTDASIL 1954
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1953419023 1955 QEKLGSLNLRWQEVCKQLAERKKRLEE 1981
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2700-2806 5.57e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 61.95  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2700 ERLQELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYN 2779
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1953419023 2780 LNTLEDLNTRWKLLQVAIEDRIRQLHE 2806
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
112-218 1.05e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 61.18  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  112 NLDSYQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIGTGKlseDEETE 191
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEE 77
                           90       100
                   ....*....|....*....|....*..
gi 1953419023  192 VQEQMNLLNSRWECLRVASMEKQSNLH 218
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
822-925 1.17e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 60.80  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  822 KLRKIQNHIKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEaEPEFAGRLE 901
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
                           90       100
                   ....*....|....*....|....
gi 1953419023  902 TELRELNTQWDYMCRQVYARKEAL 925
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
116-217 2.22e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   116 YQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIgtgKLSEDEETEVQEQ 195
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1953419023   196 MNLLNSRWECLRVASMEKQSNL 217
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1247 7.85e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.69  E-value: 7.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1041 WHELLSYLEKANKWLSEVEVKLKTTENISG--GAEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGGVMD-ELINEEL 1117
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1118 ETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQK-IQSDLTSHEIS 1196
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953419023 1197 LEEMKKhnQGKETAQRV-LSQIDVAQKKLQDVSMKFRLFQKPA-NFEQRLQES 1247
Cdd:cd00176    162 LKSLNE--LAEELLEEGhPDADEEIEEKLEELNERWEELLELAeERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
2241-2342 1.00e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.11  E-value: 1.00e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2241 FNRAWTELTDWLSLLDRVIKSQrVMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2320
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1953419023  2321 ERIQSQWDEVQEHLQNRRQQLN 2342
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2701-2811 1.28e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 60.92  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2701 RLQELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYNL 2780
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1953419023 2781 NTLEDLNTRWKLLQVAIEDRIRQLHEAHRDF 2811
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1111-1874 2.26e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.58  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1111 ELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAayiadkvdaaqmpQEAQKIQSDL 1190
Cdd:COG1196    263 EEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELE-------------ELEERLEELK 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1191 TSHEISLEEMKKHNQGKETAQRVLSQIDVAQKKLQDvsMKFRLFQKPANFEQRLQESKMILDEvkmhlpALETKSVEQEV 1270
Cdd:COG1196    330 EKIEALKEELEERETLLEELEQLLAELEEAKEELEE--KLSALLEELEELFEALREELAELEA------ELAEIRNELEE 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1271 VQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTEnPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMR 1350
Cdd:COG1196    402 LKREIESLEERLERLSERLEDLKEELKELEAELEELQTE-LEELNEELEELEEQLEELRDRLKELERELAELQEELQRLE 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1351 KEMNALTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVhlksvtEVGEALKTVLGKkemlvedklsllN 1430
Cdd:COG1196    481 KELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKE------KYETALEAALGN------------R 542
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1431 SNWIAVTSraEEWLNLLLEYQKhMENFDQNVDYITNWIIQADALLDESEKKKPQQKEDILKRLKAEMNDIRP-----KVD 1505
Cdd:COG1196    543 LQAVVVEN--EEVAKKAIEFLK-ENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFvlgdtLVV 619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1506 STRDQAANLMANRGDHCR------KVVEPKiselnhrfaaishRIKTGKASIPLKELEQfnsdiQKLLEPLEAEIQQGVN 1579
Cdd:COG1196    620 DDLEQARRLARKLRIKYRivtldgDLVEPS-------------GSITGGSRNKRSSLAQ-----KRELKELEEELAELEA 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1580 LKEEdfnkdmsedNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQ 1658
Cdd:COG1196    682 QLEK---------LEEELKSLKNELRSLEDLLEElRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEE 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1659 ADDLLKCLDDIEKKLASLPE--PRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMA---------VEPTQIQLSK 1727
Cdd:COG1196    753 LEELQERLEELEEELESLEEalAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALErelesleqrRERLEQEIEE 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1728 RWREIESKFAQFRRLNfAQIHTVHEEsvvamTEDMPLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCAQDFEDLFKQ 1807
Cdd:COG1196    833 LEEEIEELEEKLDELE-EELEELEKE-----LEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEE 906
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 1808 EESLKNIKDSLQQISGRIDIIHNKKTAALHSATPA--------ERAKLQEALSRLDFQWERVNNMYKDRQGRFDR 1874
Cdd:COG1196    907 IEKLRERLEELEAKLERLEVELPELEEELEEEYEDtletelerEIERLEEEIEALGPVNLRAIEEYEEVEERYEE 981
PTZ00121 PTZ00121
MAEBL; Provisional
1125-1814 3.21e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1125 RELHEEAVRRQKlleqsIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKH 1203
Cdd:PTZ00121  1236 KKDAEEAKKAEE-----ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkKADEAKKK 1310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1204 NQGKETAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMI-LDEVKMHLPALETKSVEQEVVQSQLNHCVNLY 1282
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1283 KSLSEVKSEVEMVIKTGRQiVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNALTEWLAA 1362
Cdd:PTZ00121  1391 KKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1363 TDMELTKRSAVEGMpsnlDSEVAWGKAtqKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEE 1442
Cdd:PTZ00121  1470 KKADEAKKKAEEAK----KADEAKKKA--EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1443 WLNLLLEYQKHMEnfdqnvdyitnwIIQADALLDESEKKKPQQKEDILKRLKAEMNDIRPK-VDSTRDQAANLMANRGDH 1521
Cdd:PTZ00121  1544 EKKKADELKKAEE------------LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArIEEVMKLYEEEKKMKAEE 1611
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1522 CRKVVEPKIselnhrfaaishriktgKASiPLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMSEDNEGTVKEL 1600
Cdd:PTZ00121  1612 AKKAEEAKI-----------------KAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEED 1673
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1601 LQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPR 1680
Cdd:PTZ00121  1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1681 DER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRR--------LNFAQIHTVH 1751
Cdd:PTZ00121  1754 EEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggkegnlvINDSKEMEDS 1830
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953419023 1752 EESVVAMTEDMPLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCAQDFEDLFKQEESLKNI 1814
Cdd:PTZ00121  1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKI 1893
SPEC smart00150
Spectrin repeats;
2458-2567 3.92e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.57  E-value: 3.92e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2458 QQFPLDLEKFLAWLTEAETTANvlqdathKERLLEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLRslEGSDD 2537
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-------SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 1953419023  2538 AALLQRRLDNMNFKWSELRKKSLNIRSHLE 2567
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
2825-2854 7.08e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 7.08e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953419023 2825 GPWERAISPNKVPYYINHETQTTCWDHPKM 2854
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1895-2719 1.19e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 61.27  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1895 EAEQFLKKTQIPENWEHAKYKWYLKELQDGIGQRQSVVRVLNATGEEII-----QQSSKTDASILQEKLGSLNLRWQEVC 1969
Cdd:COG1196    208 QAEKAERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEelqeeLEEAEKEIEELKSELEELREELEELQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1970 K---QLAERKKRLEEQKNILSEFQRDVNEFVLWLEEADNV---------ANIPLEPGNEQQLKEKLEQVKLLAEELPLRQ 2037
Cdd:COG1196    288 EellELKEEIEELEGEISLLRERLEELENELEELEERLEElkekiealkEELEERETLLEELEQLLAELEEAKEELEEKL 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2038 GILKQLNETGGTVLVsaplspEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQL 2117
Cdd:COG1196    368 SALLEELEELFEALR------EELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTEL 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2118 EIYNQPNQTGPFDIKEIEVAVQAKQPDVEGILSKGQHLYKEKPATQPAKRKLEDLSSDWKVVTQLLQELRAKQPGPAPGL 2197
Cdd:COG1196    442 EELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPV 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2198 TTVRAPPSQTVT------------LVTQPAVTKETAISKLE--------------MPSSLLLEVPALADFNRAWTELTDW 2251
Cdd:COG1196    522 AELIKVKEKYETaleaalgnrlqaVVVENEEVAKKAIEFLKenkagratflpldrIKPLRSLKSDAAPGFLGLASDLIDF 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2252 LSLLDRVIKS---QRVMVGDLEDINEMiikqkATLQDLEQRRPQLE-ELITAAQNLKNKTSNQEARTIITDRIERIQSQW 2327
Cdd:COG1196    602 DPKYEPAVRFvlgDTLVVDDLEQARRL-----ARKLRIKYRIVTLDgDLVEPSGSITGGSRNKRSSLAQKRELKELEEEL 676
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2328 DEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEApytvdaIQKKITETKQLAKDLRqwqinvdvAN 2407
Cdd:COG1196    677 AELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRE------LAALEEELEQLQSRLE--------EL 742
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2408 DLALKLLRDYSADDTRKVHMITENINaswaSIHKRLSEREAALEETHRLLQQfpldLEKFLAWLTEAETTAnvlqdathK 2487
Cdd:COG1196    743 EEELEELEEELEELQERLEELEEELE----SLEEALAKLKEEIEELEEKRQA----LQEELEELEEELEEA--------E 806
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2488 ERLLEDSKGVRELMKQWQDLQGEIEAhtdIYHNLDEngqkvlrslegsddaalLQRRLDNMNFKWSELRKKSLNIRSHLE 2567
Cdd:COG1196    807 RRLDALERELESLEQRRERLEQEIEE---LEEEIEE-----------------LEEKLDELEEELEELEKELEELKEELE 866
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2568 ASSDQWKRLHLSLQELlvwlQLKDDELSRQApiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGL 2647
Cdd:COG1196    867 ELEAEKEELEDELKEL----EEEKEELEEEL---------RELESELAELKEEIEKLRERLEELEAKLERLEVE--LPEL 931
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953419023 2648 EKLYQEPRELPPEERAQNVTRLLRKQAEE---VN----TQWEKLNVHSADWQRKIDEALERLQELQEATDELDLKLRQA 2719
Cdd:COG1196    932 EEELEEEYEDTLETELEREIERLEEEIEAlgpVNlraiEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRER 1010
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
2822-2854 2.54e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 51.83  E-value: 2.54e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1953419023  2822 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 2854
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2336-2452 2.79e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 2.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2336 NRRQQLNEMLKDSTQWLEAKEEaeqvlgqarakLESWKEAPYTVDAIQKKITETKQLAKDLRQWQINVDVANDLALKLLr 2415
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEA-----------LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1953419023 2416 DYSADDTRKVHMITENINASWASIHKRLSEREAALEE 2452
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1650-1752 3.07e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.86  E-value: 3.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1650 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1727
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 1953419023 1728 RWREIESKFAQFRRLNFAQIHTVHE 1752
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
2826-2852 6.99e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 50.58  E-value: 6.99e-08
                           10        20
                   ....*....|....*....|....*..
gi 1953419023 2826 PWERAISPNKVPYYINHETQTTCWDHP 2852
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SPEC smart00150
Spectrin repeats;
2703-2804 1.04e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 1.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2703 QELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYNLNT 2782
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1953419023  2783 LEDLNTRWKLLQVAIEDRIRQL 2804
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
332-599 3.33e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.91  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  332 KWQRFTEEQCLFSAWLSEKEDAVNKIHTTgfKDQSEVLSNLQKLAVLKTDLEKKKQTMDKLCSLNQDLLSAlkNTVVAHK 411
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  412 MEAWLDNFAQRWDNLVQKLEkssaqisqavtttqpsltqttvmetvtmvttrehilvkhaqeelpppppqKKRQIIVDSE 491
Cdd:cd00176     77 IQERLEELNQRWEELRELAE--------------------------------------------------ERRQRLEEAL 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  492 IRKRLDVDITELHSWITRSEAVLQSPEfaIYRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 571
Cdd:cd00176    107 DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                          250       260
                   ....*....|....*....|....*...
gi 1953419023  572 SIKQASEQLNSRWIEFCQLLSERLNWLE 599
Cdd:cd00176    183 EIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1651-1875 4.61e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.52  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1651 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1723
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1724 Q--LSKRWREIESKFAQFRRLnfaqihtvheesvvamtedmpLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCaQDF 1801
Cdd:cd00176     81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1802 EDLFKQEESLKNIKDSLQQISGRIDIIHNKKTAALHSATPAERAKLQEALSRLDFQWERVNNMYKDRQGRFDRS 1875
Cdd:cd00176    139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
499-599 1.03e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 1.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   499 DITELHSWITRSEAVLQSPEFAiyRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 578
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1953419023   579 QLNSRWIEFCQLLSERLNWLE 599
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2455-2557 1.34e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2455 RLLQQFPLDLEKFLAWLTEAETTANvlqdathKERLLEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLrsLEG 2534
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 1953419023 2535 SDDAALLQRRLDNMNFKWSELRK 2557
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
SPEC smart00150
Spectrin repeats;
830-926 1.99e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 1.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   830 IKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEfAGRLETELRELNT 909
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNE 84
                            90
                    ....*....|....*..
gi 1953419023   910 QWDYMCRQVYARKEALK 926
Cdd:smart00150   85 RWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1653-1735 2.01e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.01e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  1653 YQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDG--AAMAVEPTQI 1723
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLesveallKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90
                    ....*....|..
gi 1953419023  1724 QLSKRWREIESK 1735
Cdd:smart00150   81 ELNERWEELKEL 92
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1526-2033 1.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1526 VEPKISELNHRFAAISHRIKtgKASIPLKELEQFNSDIQKLLEPLEA--EIQQGVNLKEEDFNKDMSEDNEgTVKELLQR 1603
Cdd:PRK03918   191 IEELIKEKEKELEEVLREIN--EISSELPELREELEKLEKEVKELEElkEEIEELEKELESLEGSKRKLEE-KIRELEER 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1604 GDNLQQRITD-ERKREEIKiKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPrdE 1682
Cdd:PRK03918   268 IEELKKEIEElEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL--K 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1683 RKIKEIDRELQKKK------EELNAVRRQAEGLSEDGAAMAVEPTQIQL---SKRWREIESKFAQFRRlNFAQIHTVHEE 1753
Cdd:PRK03918   345 KKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELeelEKAKEEIEEEISKITA-RIGELKKEIKE 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1754 SVVAM-----------------TEDMPLEISyvpSTYLTEITHVSQALSEVEELLnapdlcaqdfEDLFKQEESLKNIkd 1816
Cdd:PRK03918   424 LKKAIeelkkakgkcpvcgrelTEEHRKELL---EEYTAELKRIEKELKEIEEKE----------RKLRKELRELEKV-- 488
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1817 slqqISGRIDIIHNKKTAAlhsatpaERAKLQEALSRLDFqwERVNNMYKDrqgrFDRSVEKWRRFHYDMKILNQWLTEA 1896
Cdd:PRK03918   489 ----LKKESELIKLKELAE-------QLKELEEKLKKYNL--EELEKKAEE----YEKLKEKLIKLKGEIKSLKKELEKL 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1897 EQFLKKTQIPENwEHAKYKWYLKELQDGIGQR--------QSVVRVLNATGEEIIQ-QSSKTDASILQEKLGSLNLRWQE 1967
Cdd:PRK03918   552 EELKKKLAELEK-KLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYLElKDAEKELEREEKELKKLEEELDK 630
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1968 VCKQLAERKKRLEEQKNILSEFQRDVNEfvlwlEEADNVANIPLEPGNE--------QQLKEKLEQVKLLAEEL 2033
Cdd:PRK03918   631 AFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEYLELSRElaglraelEELEKRREEIKKTLEKL 699
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2252-2366 4.07e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2252 LSLLDRVIKSQRVMVG-DLEDINEMIikqkatlQDLEQRRPQLEELITAAQNLKnktsnQEARTIITDRIERIQSQWDEV 2330
Cdd:PRK00409   497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALL-----KEAEKLKEELEEKKEKLQEEE 564
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1953419023 2331 QEHLQNRRQQLNEMLKdstqwlEAKEEAEQVLGQAR 2366
Cdd:PRK00409   565 DKLLEEAEKEAQQAIK------EAKKEADEIIKELR 594
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
469-840 2.13e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.93  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  469 KHAQEELPPPPPQKKRQIIVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIYRKEGNFSDLKEKVNAIEREKAEKFRK 548
Cdd:COG1196    659 KRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSR 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  549 LQDASRSAQALVEQMVNegvNADSIKQASEQLNSrwiefcqlLSERLNWLE-YQNNIITFYNQLQQLEQMTTTAENWLKT 627
Cdd:COG1196    739 LEELEEELEELEEELEE---LQERLEELEEELES--------LEEALAKLKeEIEELEEKRQALQEELEELEEELEEAER 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  628 QPTTTSEptAIKSQLKICKDEINRLSALQPQIERLKIQSIALKEKGQgpmFLDADFVAFTNHFNQVFADVQAREKELQTI 707
Cdd:COG1196    808 RLDALER--ELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE---ELEKELEELKEELEELEAEKEELEDELKEL 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  708 FDSLppMRYQETMSTILTWIQQSETKLSIPQVTVTEYDIMEQRL-GELQALQSSLQEQqnGLNYLSTTVKEMSKKAP--- 783
Cdd:COG1196    883 EEEK--EELEEELRELESELAELKEEIEKLRERLEELEAKLERLeVELPELEEELEEE--YEDTLETELEREIERLEeei 958
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953419023  784 --LSDISRKYQSEFEEIEGRWKKLSSQLvehcqklEEQMAKLRKIQNHIKTLKKWITEV 840
Cdd:COG1196    959 eaLGPVNLRAIEEYEEVEERYEELKSQR-------EDLEEAKEKLLEVIEELDKEKRER 1010
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
602-705 2.94e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.61  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  602 NNIITFYNQLQQLEQMTTTAENWLKTQPTTTSePTAIKSQLKICKDEINRLSALQPQIERLKIQSIAL-KEKGQGPMFLD 680
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*
gi 1953419023  681 ADFVAFTNHFNQVFADVQAREKELQ 705
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
334-432 4.33e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 4.33e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   334 QRFTEEQCLFSAWLSEKEDAVNkiHTTGFKDQSEVLSNLQKLAVLKTDLEKKKQTMDKLCSLNQDLLSalKNTVVAHKME 413
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA--SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIE 76
                            90
                    ....*....|....*....
gi 1953419023   414 AWLDNFAQRWDNLVQKLEK 432
Cdd:smart00150   77 ERLEELNERWEELKELAEE 95
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
1-17 5.05e-03

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 39.14  E-value: 5.05e-03
                           10
                   ....*....|....*..
gi 1953419023    1 MYITSLFQVLPQQVSIE 17
Cdd:cd21233     95 MYVTSLFQVLPQQVSIE 111
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
2891-3052 2.82e-113

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 356.65  E-value: 2.82e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2891 SLSAACDALDQHNLKQNDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 2970
Cdd:cd16246      1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2971 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3050
Cdd:cd16246     81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                   ..
gi 1953419023 3051 MR 3052
Cdd:cd16246    161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
2891-3052 1.58e-103

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 328.81  E-value: 1.58e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2891 SLSAACDALDQHNLK-QNDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 2969
Cdd:cd16242      1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2970 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 3049
Cdd:cd16242     81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                   ...
gi 1953419023 3050 WMR 3052
Cdd:cd16242    161 WLK 163
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
2892-3052 3.22e-84

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 273.31  E-value: 3.22e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2892 LSAACDALDQHNLKQNDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 2971
Cdd:cd16247      2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2972 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 3051
Cdd:cd16247     82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

                   .
gi 1953419023 3052 R 3052
Cdd:cd16247    162 R 162
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
2891-3051 2.92e-80

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 262.04  E-value: 2.92e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2891 SLSAACDALDQHNLKQNDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 2970
Cdd:cd16248      1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2971 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3050
Cdd:cd16248     81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160

                   .
gi 1953419023 3051 M 3051
Cdd:cd16248    161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
2892-3051 9.73e-68

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 226.38  E-value: 9.73e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2892 LSAACDALDQHNLKQ-NDQPMDILQVINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 2970
Cdd:cd15901      2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2971 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3050
Cdd:cd15901     82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161

                   .
gi 1953419023 3051 M 3051
Cdd:cd15901    162 L 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
2855-2973 6.35e-57

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430392  Cd Length: 123  Bit Score: 193.51  E-value: 6.35e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2855 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQVINCLTTIYDRLEQEHN 2932
Cdd:pfam09068    1 TELMQELQDFNNIRFSAYRTAMKLRALQKRLCLDLVDLWNLIEAFDEHGLNslENDLLLDVSELETLLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1953419023 2933 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 2973
Cdd:pfam09068   81 TthQVNVPLSVDLLLNWLLNVYDPQRTGKIRVLSFKVALVLLC 123
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
2977-3068 6.33e-50

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilisation of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 430393  Cd Length: 90  Bit Score: 172.48  E-value: 6.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2977 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 3056
Cdd:pfam09069    1 LVDKYRYLFSQISDSNGLLDQRKLGLLLHELLQLPRQVGEVAAFGG--IEPSVRSCFEQVGGKPKIELNHFLDWLMSEPQ 78
                           90
                   ....*....|..
gi 1953419023 3057 SMVWLPVLHRVA 3068
Cdd:pfam09069   79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3077-3125 5.83e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 5.83e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023 3077 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3125
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
116-330 2.64e-26

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 109.46  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  116 YQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIgtgKLSEDEETEVQEQ 195
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  196 MNLLNSRWECLRVASMEKQSNLHKVLMDLQ-NQQLKELNDWLTKTEERtrkMEKEPLGPDIEDLKRQVQQHKVLQEDLEQ 274
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023  275 EQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 330
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1878-2091 2.55e-23

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 100.98  E-value: 2.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1878 KWRRFHYDMKILNQWLTEAEQFLKKTQIPENWEHAK-YKWYLKELQDGIGQRQSVVRVLNATGEEIIQQSSKtDASILQE 1956
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1957 KLGSLNLRWQEVCKQLAERKKRLEEQKNiLSEFQRDVNEFVLWLEEADNVANIPLEPGNEQQLKEKLEQVKLLAEELPLR 2036
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 2037 QGILKQLNETGGTVLVSAPlsPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEA 2091
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2456-2699 8.69e-22

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 96.36  E-value: 8.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2456 LLQQFPLDLEKFLAWLTEAETTANVLQDAthkerllEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLRslEGS 2535
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2536 DDAALLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2615
Cdd:cd00176     72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2616 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTQWEKLNVHSADWQRKI 2695
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                   ....
gi 1953419023 2696 DEAL 2699
Cdd:cd00176    210 EEAL 213
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
2891-3051 1.72e-21

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 93.90  E-value: 1.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2891 SLSAACDALDQHNLKQND-----QPMDILQVINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 2965
Cdd:cd16245      1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2966 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 3045
Cdd:cd16245     78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157

                   ....*.
gi 1953419023 3046 LFLDWM 3051
Cdd:cd16245    158 QFIGWW 163
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2238-2454 1.29e-19

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 90.20  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2238 LADFNRAWTELTDWLSLLDRVIKSQrVMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2317
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2318 DRIERIQSQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEAPYTVDAIQKKITETKQLAKDLR 2397
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953419023 2398 QWQINVDVANDLALKLLRDYSADDTRKVHMITENINASWASIHKRLSEREAALEETH 2454
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
2910-3051 6.56e-19

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrobrevins contain one or two syntrophin binding sites (SBSs).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 86.52  E-value: 6.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2910 PMDILQVINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLF 2985
Cdd:cd16244     22 ELSVSRLETLLSSIYyqlnKRLPTTHQ--IDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTLCAGKLVDKLRYIF 99
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023 2986 KQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCFQfANNKPEIEAalFLDWM 3051
Cdd:cd16244    100 SQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFP-GQSKVTVND--FLDVM 160
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
226-432 7.68e-17

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 82.11  E-value: 7.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  226 NQQLKELNDWLTKTEErtrKMEKEPLGPDIEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESsGDHATAALEEQL 305
Cdd:cd00176      6 LRDADELEAWLSEKEE---LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  306 KVLGDRWANICRWTEDRWVLLQDiLLKWQRFTEEQCLFSAWLSEKEDAVNKIHTTgfKDQSEVLSNLQKLAVLKTDLEKK 385
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEE-ALDLQQFFRDADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1953419023  386 KQTMDKLCSLNQDLLSALKNTVVAHKmEAWLDNFAQRWDNLVQKLEK 432
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEI-EEKLEELNERWEELLELAEE 204
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3073-3118 8.77e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 8.77e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953419023 3073 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3118
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3074-3117 2.12e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.12e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1953419023  3074 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3117
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
822-1036 3.74e-14

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 74.02  E-value: 3.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  822 KLRKIQNHIKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEfAGRLE 901
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  902 TELRELNTQWDYMCRQVYARKEALKGGLDKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQTAVEEMKRAKEEAQ 981
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023  982 QKEAKVKLLTESVNSVIAQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEE 1036
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
499-705 2.01e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.09  E-value: 2.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  499 DITELHSWITRSEAVLQSPEFAiyRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 578
Cdd:cd00176      8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  579 QLNSRWIEFCQLLSERLNWLEYQNNIITFYNQLQQLEQMTTTAENWLKTQPTTTSePTAIKSQLKICKDEINRLSALQPQ 658
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023  659 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFNQVFADVQAREKELQ 705
Cdd:cd00176    162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2350-2569 2.52e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 71.71  E-value: 2.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2350 QWLEAKEEAEQVLGQARAKLESWkEAPYTVDAIQKKITETKQLAKDLRQWQINVDVANDLALKLLRDYSaDDTRKVHMIT 2429
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2430 ENINASWASIHKRLSEREAALEETHRLLQQFpLDLEKFLAWLTEAETTANvlqdathKERLLEDSKGVRELMKQWQDLQG 2509
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-------SEDLGKDLESVEELLKKHKELEE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2510 EIEAHTDIYHNLDENGQKvLRSLEGSDDAALLQRRLDNMNFKWSELRKKSLNIRSHLEAS 2569
Cdd:cd00176    154 ELEAHEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2572-2808 3.42e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 71.32  E-value: 3.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2572 QWKRLHLSLQELLVWLQLKDDELSRQAPiGGDFPAVQKQNDVHRAFKRELKTKEPVImstletvriflteqplEGLEKLY 2651
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERV----------------EALNELG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2652 QEPRELPPEERAQnvtrlLRKQAEEVNTQWEKLNVHSADWQRKIDEALERLQELQEAtDELDLKLRQAEVIKGSWQPVGD 2731
Cdd:cd00176     64 EQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953419023 2732 LliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYNLN-TLEDLNTRWKLLQVAIEDRIRQLHEAH 2808
Cdd:cd00176    138 L--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEeKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
899-1709 4.11e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 75.86  E-value: 4.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  899 RLETELRELNTQWDYMCRQV-----YAR-KEALKggldktvSLQKDLSEMHewMTQAEEEYLERDFEYKtpdELQTAVEE 972
Cdd:TIGR02168  190 RLEDILNELERQLKSLERQAekaerYKElKAELR-------ELELALLVLR--LEELREELEELQEELK---EAEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  973 MKRAKEEAQQKEAKVKLLTESVNSVIaQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKAN 1052
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEI-EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1053 KWLSEVEVKLkttenisggaEEIAEVLDSLENLMQHSEDnpnqirilaqtltdggvmdelINEELETFNSRWRELHEEAV 1132
Cdd:TIGR02168  337 EELAELEEKL----------EELKEELESLEAELEELEA---------------------ELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1133 RRQKLLEQSIQSaqeIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQK--IQSDLTSHEISLEEMKKHNQGKETA 1210
Cdd:TIGR02168  386 SKVAQLELQIAS---LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1211 QRVLS-QIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEvkmhlpalETKSVEQEvvQSQLNHCVNLYKSLSEVK 1289
Cdd:TIGR02168  463 LEELReELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE--------GVKALLKN--QSGLSGILGVLSELISVD 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1290 SEVEMVIktgrqivqkkqtenpkelderVTALKLHyneLGAKVTERKQQLEKC---LKLSRKMRKEMNALTEW----LAA 1362
Cdd:TIGR02168  533 EGYEAAI---------------------EAALGGR---LQAVVVENLNAAKKAiafLKQNELGRVTFLPLDSIkgteIQG 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1363 TDMELTKRsaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEAL--KTVLGKKEMLVEDKLSLLNSNWIaVTSRA 1440
Cdd:TIGR02168  589 NDREILKN--IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALelAKKLRPGYRIVTLDGDLVRPGGV-ITGGS 665
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1441 EEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLDESEKKKpQQKEDILKRLKAEMNDIRPKVDSTRDQAANL------ 1514
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1515 ---MANRGDHCRKVVEPKISELNHRFAAISHRIKTGKAsiplkELEQFNSDIQKLLEPLEAEIQQGVNLKEEdfnkdmse 1591
Cdd:TIGR02168  745 leeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDELRAE-------- 811
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1592 dnegtVKELLQRGDNLQQRITDERKReeIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY---KRQADDLLKCLDD 1668
Cdd:TIGR02168  812 -----LTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERAS 884
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1669 IEKKLASLPEPRD---------ERKIKEIDRELQKKKEELNAVRRQAEGL 1709
Cdd:TIGR02168  885 LEEALALLRSELEelseelrelESKRSELRRELEELREKLAQLELRLEGL 934
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1784-1981 1.42e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.78  E-value: 1.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1784 LSEVEELLNAPDLcAQDFEDLFKQEESLKNIKDSLQQISGRIDIIhNKKTAALHSATPAERAKLQEALSRLDFQWERVNN 1863
Cdd:cd00176     16 LSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEAL-NELGEQLIEEGHPDAEEIQERLEELNQRWEELRE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1864 MYKDRQGRFDRSVEKWRRFHyDMKILNQWLTEAEQFLKKTQIPENWEHAKYKW-YLKELQDGIGQRQSVVRVLNATGEEI 1942
Cdd:cd00176     94 LAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLkKHKELEEELEAHEPRLKSLNELAEEL 172
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1953419023 1943 IQQSSKTDASILQEKLGSLNLRWQEVCKQLAERKKRLEE 1981
Cdd:cd00176    173 LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
715-925 3.29e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 68.63  E-value: 3.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  715 RYQETMSTILTWIQQSETKLSIPQVTVTEYDIMEQRLgELQALQSSLQEQQNGLNYLSTTVKEMSKKAPlsDISRKYQSE 794
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  795 FEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIKtLKKWITEVDVFLKEEWPaLGDSEILKRQLKQCRLLVNDIQTI 874
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953419023  875 QPSLNSVNEGAQKMKNEAEPEFAGRLETELRELNTQWDYMCRQVYARKEAL 925
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1896-2584 4.39e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.78  E-value: 4.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1896 AEQFLKKTQIPENWEHAKYKWYLKELQDGIGQRQSVVRVLnatgeEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLAER 1975
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQEELKEA-----EEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1976 KKRLEEQKNILSEFQRDVNEFVlwlEEADNVANIPLEPG-----NEQQLKEKLEQVKLLAEELPLRQGILKQLNEtggtv 2050
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILR---ERLANLERQLEELEaqleeLESKLDELAEELAELEEKLEELKEELESLEA----- 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2051 lvSAPLSPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQLEIYNQPNQTGPFD 2130
Cdd:TIGR02168  359 --ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2131 --------IKEIEVAVQAKQPDVEGILSKGQHLYKEKP-ATQPAKRKLEDLSSDWKVVTQLLQELRAKQPGPAPGLTTVR 2201
Cdd:TIGR02168  437 elqaeleeLEEELEELQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2202 APPSQTVTLVTQPAVTK--ETAISKLEMPSSLLLEVPALADFNRA-----WTELTDWLSLLDRVIKSQRVMVGDLEDINE 2274
Cdd:TIGR02168  517 GLSGILGVLSELISVDEgyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2275 mIIKQKATLQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD----------------------- 2318
Cdd:TIGR02168  597 -IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssile 674
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2319 ---RIERIQSQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEAPYTVDAIQKKITETKQLAKD 2395
Cdd:TIGR02168  675 rrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2396 LRQWQINVDVANDLALKLLRDYSADDTRKVHMITENINA---SWASIHKRLSEREAALEETHRLLQQFPLDLEKFLAWLT 2472
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2473 EAETTANVLQDAthKERLLEDSKGVRELMKQWQDLQGEIEAhtDIYHNLDENGQKVLRSLEGSDDAALLQRRLDNMNFKW 2552
Cdd:TIGR02168  835 ATERRLEDLEEQ--IEELSEDIESLAAEIEELEELIEELES--ELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          730       740       750
                   ....*....|....*....|....*....|..
gi 1953419023 2553 SELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2584
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
2915-3052 9.49e-12

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 320001  Cd Length: 163  Bit Score: 65.87  E-value: 9.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2915 QVINCLTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFK----QVAS 2990
Cdd:cd16243     26 EVSQALERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGG 104
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953419023 2991 STGFCDQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 3052
Cdd:cd16243    105 SSGSITRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
SPEC smart00150
Spectrin repeats;
1880-1980 1.54e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.12  E-value: 1.54e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  1880 RRFHYDMKILNQWLTEAEQFLKKTQIPENWEHAKYKW-YLKELQDGIGQRQSVVRVLNATGEEIIQQSSKtDASILQEKL 1958
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1953419023  1959 GSLNLRWQEVCKQLAERKKRLE 1980
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1877-1981 4.12e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 62.34  E-value: 4.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1877 EKWRRFHYDMKILNQWLTEAEQFLKKTQIPENWEH--AKYKWYlKELQDGIGQRQSVVRVLNATGEEIIQqSSKTDASIL 1954
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1953419023 1955 QEKLGSLNLRWQEVCKQLAERKKRLEE 1981
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2700-2806 5.57e-11

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 61.95  E-value: 5.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2700 ERLQELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYN 2779
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDL--ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1953419023 2780 LNTLEDLNTRWKLLQVAIEDRIRQLHE 2806
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
112-218 1.05e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 61.18  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  112 NLDSYQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIGTGKlseDEETE 191
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEE 77
                           90       100
                   ....*....|....*....|....*..
gi 1953419023  192 VQEQMNLLNSRWECLRVASMEKQSNLH 218
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
822-925 1.17e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 60.80  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  822 KLRKIQNHIKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEaEPEFAGRLE 901
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
                           90       100
                   ....*....|....*....|....
gi 1953419023  902 TELRELNTQWDYMCRQVYARKEAL 925
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
221-328 1.25e-10

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 60.80  E-value: 1.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  221 LMDLQNQQLKELNDWLTKTEErtrKMEKEPLGPDIEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVdESSGDHATAA 300
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 1953419023  301 LEEQLKVLGDRWANICRWTEDRWVLLQD 328
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
116-217 2.22e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   116 YQTALEEVLSWLLSAEDALQAQgEISNDVEEVKEQFHTHEGYMMDLTSHQGRVGNVLQLGSQLIgtgKLSEDEETEVQEQ 195
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1953419023   196 MNLLNSRWECLRVASMEKQSNL 217
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
701-1711 4.45e-10

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 66.23  E-value: 4.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  701 EKELQTIFDSLPPMRyQETMSTILTWIQQSETKLSIPQVTVTEY---DIMEQRLGELQALQSSLQEQQNGLNYLSTTVKE 777
Cdd:TIGR01612  702 KSKIDKEYDKIQNME-TATVELHLSNIENKKNELLDIIVEIKKHihgEINKDLNKILEDFKNKEKELSNKINDYAKEKDE 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  778 MSK-KAPLSDISRKY--QSEFEEI-EGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIKTLK-KWITEVDVFLKEEwpaLG 852
Cdd:TIGR01612  781 LNKyKSKISEIKNHYndQINIDNIkDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKdDFLNKVDKFINFE---NN 857
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  853 DSEILKRQLKQCRLLVNDIQTiQPSLNSVNEGAQKMKNEAE--PEFAGRLETELRELNT--QWDYMCRQVYARKEALKGG 928
Cdd:TIGR01612  858 CKEKIDSEHEQFAELTNKIKA-EISDDKLNDYEKKFNDSKSliNEINKSIEEEYQNINTlkKVDEYIKICENTKESIEKF 936
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  929 LDKTVSLQKDLSEMHEwmTQAEEEYLERDFEYKTPDELQTAVEEMKRAKEEA--QQKEAKVKLLTESVNSviaqappaaq 1006
Cdd:TIGR01612  937 HNKQNILKEILNKNID--TIKESNLIEKSYKDKFDNTLIDKINELDKAFKDAslNDYEAKNNELIKYFND---------- 1004
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1007 eaLKKELDTLTTNYQWlctrlngkcKTLEEVWACWHELLSYLEKANKWLSEVEVKLKTT-ENISGGAE-EIAEVLDSL-E 1083
Cdd:TIGR01612 1005 --LKANLGKNKENMLY---------HQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSiYNIIDEIEkEIGKNIELLnK 1073
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1084 NLMQHSE------------------------------DNPNQIRILAQTLTDGgvMDELINEELETFNSRWR---ELHEE 1130
Cdd:TIGR01612 1074 EILEEAEinitnfneikeklkhynfddfgkeenikyaDEINKIKDDIKNLDQK--IDHHIKALEEIKKKSENyidEIKAQ 1151
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1131 AVRRQKLLEQSI--QSAQEIEKSlhlIQESLSSIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ--G 1206
Cdd:TIGR01612 1152 INDLEDVADKAIsnDDPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLsyG 1220
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1207 KETAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKSLS 1286
Cdd:TIGR01612 1221 KNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNISHD 1284
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1287 EVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNALTEWLAatdm 1365
Cdd:TIGR01612 1285 DDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA---- 1349
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1366 eltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVedKLSLLNSNWIAVTSRAEEWLN 1445
Cdd:TIGR01612 1350 -------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIESTLD 1413
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1446 llleyQKHMENFDQNVDYITNWIIQADALLDESEKKKPQQKEDILKRLK-AEMNDirpkvdstrDQAANLMANRGDHCRK 1524
Cdd:TIGR01612 1414 -----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKnIEMAD---------NKSQHILKIKKDNATN 1479
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1525 VVEPKISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMSEDNEGTV 1597
Cdd:TIGR01612 1480 DHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHK 1558
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1598 KELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEKK 1672
Cdd:TIGR01612 1559 KFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEKK 1632
                         1050      1060      1070
                   ....*....|....*....|....*....|....*....
gi 1953419023 1673 LASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1711
Cdd:TIGR01612 1633 ISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
2926-3051 6.56e-10

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 60.42  E-value: 6.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2926 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 3005
Cdd:cd16250     42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1953419023 3006 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 3051
Cdd:cd16250    120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1247 7.85e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.69  E-value: 7.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1041 WHELLSYLEKANKWLSEVEVKLKTTENISG--GAEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGGVMD-ELINEEL 1117
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDleSVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1118 ETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQK-IQSDLTSHEIS 1196
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953419023 1197 LEEMKKhnQGKETAQRV-LSQIDVAQKKLQDVSMKFRLFQKPA-NFEQRLQES 1247
Cdd:cd00176    162 LKSLNE--LAEELLEEGhPDADEEIEEKLEELNERWEELLELAeERQKKLEEA 212
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
2920-3033 7.89e-10

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 60.30  E-value: 7.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2920 LTTIYDRLEQE--HNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQ 2997
Cdd:cd16249     32 LSTIFYQLNKRmpTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVMVY 111
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1953419023 2998 RRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCF 3033
Cdd:cd16249    112 GRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 145
SPEC smart00150
Spectrin repeats;
2241-2342 1.00e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.11  E-value: 1.00e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2241 FNRAWTELTDWLSLLDRVIKSQrVMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2320
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1953419023  2321 ERIQSQWDEVQEHLQNRRQQLN 2342
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2701-2811 1.28e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 60.92  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2701 RLQELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYNL 2780
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1953419023 2781 NTLEDLNTRWKLLQVAIEDRIRQLHEAHRDF 2811
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1553-1741 1.59e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 60.54  E-value: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1553 LKELEQFNSDIQKLLEPLEAEIQQgvnLKEEDFNKDMsEDNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQTKHN 1632
Cdd:cd00176     16 LSEKEELLSSTDYGDDLESVEALL---KKHEALEAEL-AAHEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1633 ALKDLrSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQ 1705
Cdd:cd00176     90 ELREL-AEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLesveellKKHKELEEELEAHEPRLKSLNEL 168
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1953419023 1706 AEGLSEDG---AAMAVEPTQIQLSKRWREIESKFAQFRR 1741
Cdd:cd00176    169 AEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQK 207
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1123-1739 1.98e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.92  E-value: 1.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1123 RWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKK 1202
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1203 HNQGK-----ETAQRVLSQIDVAQKKLQDVSMKFRLFQKP-ANFEQRLQESKMILDEVKMHLPALETK--SVEQEVVQSQ 1274
Cdd:TIGR02168  313 NLERQleeleAQLEELESKLDELAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1275 L------NHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRK 1348
Cdd:TIGR02168  393 LqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1349 MRKEMNALTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGE----ALKTVL--------- 1415
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaAIEAALggrlqavvv 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1416 ------------------GKKEMLVEDKLS--LLNSNWIAVTSRAEEWLNLLLEYQKHMENFDQNVDYITNWIIQADALl 1475
Cdd:TIGR02168  553 enlnaakkaiaflkqnelGRVTFLPLDSIKgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL- 631
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1476 desekkkpQQKEDILKRLKAEMNDIRPKVDS-TRDQAANLMANRGDHCRKVVEPKISELNHRFAAISHRIKtgKASIPLK 1554
Cdd:TIGR02168  632 --------DNALELAKKLRPGYRIVTLDGDLvRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIA--ELEKALA 701
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1555 ELEQFNSDIQKLLEPLEA---EIQQGVNLKEEDFnkdmsEDNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTK 1630
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKeleELSRQISALRKDL-----ARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAEEE 776
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1631 HNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEELNAVRRQAEGLS 1710
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQIEELS 851
                          650       660
                   ....*....|....*....|....*....
gi 1953419023 1711 EDGAAMAVEPTQIQLSKrwREIESKFAQF 1739
Cdd:TIGR02168  852 EDIESLAAEIEELEELI--EELESELEAL 878
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1111-1874 2.26e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.58  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1111 ELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAayiadkvdaaqmpQEAQKIQSDL 1190
Cdd:COG1196    263 EEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELE-------------ELEERLEELK 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1191 TSHEISLEEMKKHNQGKETAQRVLSQIDVAQKKLQDvsMKFRLFQKPANFEQRLQESKMILDEvkmhlpALETKSVEQEV 1270
Cdd:COG1196    330 EKIEALKEELEERETLLEELEQLLAELEEAKEELEE--KLSALLEELEELFEALREELAELEA------ELAEIRNELEE 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1271 VQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTEnPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMR 1350
Cdd:COG1196    402 LKREIESLEERLERLSERLEDLKEELKELEAELEELQTE-LEELNEELEELEEQLEELRDRLKELERELAELQEELQRLE 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1351 KEMNALTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVhlksvtEVGEALKTVLGKkemlvedklsllN 1430
Cdd:COG1196    481 KELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKE------KYETALEAALGN------------R 542
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1431 SNWIAVTSraEEWLNLLLEYQKhMENFDQNVDYITNWIIQADALLDESEKKKPQQKEDILKRLKAEMNDIRP-----KVD 1505
Cdd:COG1196    543 LQAVVVEN--EEVAKKAIEFLK-ENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFvlgdtLVV 619
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1506 STRDQAANLMANRGDHCR------KVVEPKiselnhrfaaishRIKTGKASIPLKELEQfnsdiQKLLEPLEAEIQQGVN 1579
Cdd:COG1196    620 DDLEQARRLARKLRIKYRivtldgDLVEPS-------------GSITGGSRNKRSSLAQ-----KRELKELEEELAELEA 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1580 LKEEdfnkdmsedNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQ 1658
Cdd:COG1196    682 QLEK---------LEEELKSLKNELRSLEDLLEElRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEE 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1659 ADDLLKCLDDIEKKLASLPE--PRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMA---------VEPTQIQLSK 1727
Cdd:COG1196    753 LEELQERLEELEEELESLEEalAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALErelesleqrRERLEQEIEE 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1728 RWREIESKFAQFRRLNfAQIHTVHEEsvvamTEDMPLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCAQDFEDLFKQ 1807
Cdd:COG1196    833 LEEEIEELEEKLDELE-EELEELEKE-----LEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEE 906
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 1808 EESLKNIKDSLQQISGRIDIIHNKKTAALHSATPA--------ERAKLQEALSRLDFQWERVNNMYKDRQGRFDR 1874
Cdd:COG1196    907 IEKLRERLEELEAKLERLEVELPELEEELEEEYEDtletelerEIERLEEEIEALGPVNLRAIEEYEEVEERYEE 981
PTZ00121 PTZ00121
MAEBL; Provisional
1125-1814 3.21e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 3.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1125 RELHEEAVRRQKlleqsIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKH 1203
Cdd:PTZ00121  1236 KKDAEEAKKAEE-----ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkKADEAKKK 1310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1204 NQGKETAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMI-LDEVKMHLPALETKSVEQEVVQSQLNHCVNLY 1282
Cdd:PTZ00121  1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1283 KSLSEVKSEVEMVIKTGRQiVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNALTEWLAA 1362
Cdd:PTZ00121  1391 KKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1363 TDMELTKRSAVEGMpsnlDSEVAWGKAtqKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEE 1442
Cdd:PTZ00121  1470 KKADEAKKKAEEAK----KADEAKKKA--EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1443 WLNLLLEYQKHMEnfdqnvdyitnwIIQADALLDESEKKKPQQKEDILKRLKAEMNDIRPK-VDSTRDQAANLMANRGDH 1521
Cdd:PTZ00121  1544 EKKKADELKKAEE------------LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArIEEVMKLYEEEKKMKAEE 1611
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1522 CRKVVEPKIselnhrfaaishriktgKASiPLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMSEDNEGTVKEL 1600
Cdd:PTZ00121  1612 AKKAEEAKI-----------------KAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEED 1673
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1601 LQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPR 1680
Cdd:PTZ00121  1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1681 DER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRR--------LNFAQIHTVH 1751
Cdd:PTZ00121  1754 EEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggkegnlvINDSKEMEDS 1830
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953419023 1752 EESVVAMTEDMPLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCAQDFEDLFKQEESLKNI 1814
Cdd:PTZ00121  1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKI 1893
SPEC smart00150
Spectrin repeats;
2458-2567 3.92e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.57  E-value: 3.92e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2458 QQFPLDLEKFLAWLTEAETTANvlqdathKERLLEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLRslEGSDD 2537
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-------SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 1953419023  2538 AALLQRRLDNMNFKWSELRKKSLNIRSHLE 2567
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
226-327 4.90e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 4.90e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   226 NQQLKELNDWLTKTEertRKMEKEPLGPDIEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDEsSGDHATAALEEQL 305
Cdd:smart00150    4 LRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1953419023   306 KVLGDRWANICRWTEDRWVLLQ 327
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
2825-2854 7.08e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.30  E-value: 7.08e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953419023 2825 GPWERAISPNKVPYYINHETQTTCWDHPKM 2854
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
935-1142 9.12e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 58.23  E-value: 9.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  935 LQKDLSEMHEWMTQAEEEYLERDFEyKTPDELQTAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPAAQEaLKKELD 1014
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1015 TLTTNYQWLCTRLNGKCKTLEEVWAcWHELLSYLEKANKWLSEVEVKLKTTENIS--GGAEEIAEVLDSLENLMQHSEDN 1092
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHEPR 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953419023 1093 PNQIRILAQTLTDGGV--MDELINEELETFNSRWRELHEEAVRRQKLLEQSI 1142
Cdd:cd00176    162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1895-2719 1.19e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 61.27  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1895 EAEQFLKKTQIPENWEHAKYKWYLKELQDGIGQRQSVVRVLNATGEEII-----QQSSKTDASILQEKLGSLNLRWQEVC 1969
Cdd:COG1196    208 QAEKAERYQELKAELRELELALLLAKLKELRKELEELEEELSRLEEELEelqeeLEEAEKEIEELKSELEELREELEELQ 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1970 K---QLAERKKRLEEQKNILSEFQRDVNEFVLWLEEADNV---------ANIPLEPGNEQQLKEKLEQVKLLAEELPLRQ 2037
Cdd:COG1196    288 EellELKEEIEELEGEISLLRERLEELENELEELEERLEElkekiealkEELEERETLLEELEQLLAELEEAKEELEEKL 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2038 GILKQLNETGGTVLVsaplspEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQL 2117
Cdd:COG1196    368 SALLEELEELFEALR------EELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTEL 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2118 EIYNQPNQTGPFDIKEIEVAVQAKQPDVEGILSKGQHLYKEKPATQPAKRKLEDLSSDWKVVTQLLQELRAKQPGPAPGL 2197
Cdd:COG1196    442 EELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPV 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2198 TTVRAPPSQTVT------------LVTQPAVTKETAISKLE--------------MPSSLLLEVPALADFNRAWTELTDW 2251
Cdd:COG1196    522 AELIKVKEKYETaleaalgnrlqaVVVENEEVAKKAIEFLKenkagratflpldrIKPLRSLKSDAAPGFLGLASDLIDF 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2252 LSLLDRVIKS---QRVMVGDLEDINEMiikqkATLQDLEQRRPQLE-ELITAAQNLKNKTSNQEARTIITDRIERIQSQW 2327
Cdd:COG1196    602 DPKYEPAVRFvlgDTLVVDDLEQARRL-----ARKLRIKYRIVTLDgDLVEPSGSITGGSRNKRSSLAQKRELKELEEEL 676
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2328 DEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEApytvdaIQKKITETKQLAKDLRqwqinvdvAN 2407
Cdd:COG1196    677 AELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRE------LAALEEELEQLQSRLE--------EL 742
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2408 DLALKLLRDYSADDTRKVHMITENINaswaSIHKRLSEREAALEETHRLLQQfpldLEKFLAWLTEAETTAnvlqdathK 2487
Cdd:COG1196    743 EEELEELEEELEELQERLEELEEELE----SLEEALAKLKEEIEELEEKRQA----LQEELEELEEELEEA--------E 806
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2488 ERLLEDSKGVRELMKQWQDLQGEIEAhtdIYHNLDEngqkvlrslegsddaalLQRRLDNMNFKWSELRKKSLNIRSHLE 2567
Cdd:COG1196    807 RRLDALERELESLEQRRERLEQEIEE---LEEEIEE-----------------LEEKLDELEEELEELEKELEELKEELE 866
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2568 ASSDQWKRLHLSLQELlvwlQLKDDELSRQApiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGL 2647
Cdd:COG1196    867 ELEAEKEELEDELKEL----EEEKEELEEEL---------RELESELAELKEEIEKLRERLEELEAKLERLEVE--LPEL 931
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953419023 2648 EKLYQEPRELPPEERAQNVTRLLRKQAEE---VN----TQWEKLNVHSADWQRKIDEALERLQELQEATDELDLKLRQA 2719
Cdd:COG1196    932 EEELEEEYEDTLETELEREIERLEEEIEAlgpVNlraiEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRER 1010
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
899-1711 1.53e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  899 RLETELRELNTQWDYMCRQV-----YARKEALKGGLDKTVsLQKDLSEMHEWMTQAEEEY--LERDFEYKTPD------- 964
Cdd:COG1196    190 RLEDLLEELEKQLEKLERQAekaerYQELKAELRELELAL-LLAKLKELRKELEELEEELsrLEEELEELQEEleeaeke 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  965 --ELQTAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPAAQEALKKELDTLTT---------NYQWLCTRLNGKCKT 1033
Cdd:COG1196    269 ieELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERleelkekieALKEELEERETLLEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1034 LEEVWACWHELLSYLEKANKWLSEVEVKLKTT--ENISGGAEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGGVMDE 1111
Cdd:COG1196    349 LEQLLAELEEAKEELEEKLSALLEELEELFEAlrEELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELK 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1112 LINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLT 1191
Cdd:COG1196    429 ELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLE 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1192 SHEISLEEMK-------KHNQGKETA---------QRVLSQIDVAQKKLQDVSMKFRLFQ---KPANFEQ--RLQESKMI 1250
Cdd:COG1196    509 ALESGLPGVYgpvaeliKVKEKYETAleaalgnrlQAVVVENEEVAKKAIEFLKENKAGRatfLPLDRIKplRSLKSDAA 588
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1251 LDEVKMHLPALETKSVEQEVVQSQLNH--CVNLYKS----LSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLH 1324
Cdd:COG1196    589 PGFLGLASDLIDFDPKYEPAVRFVLGDtlVVDDLEQarrlARKLRIKYRIVTLDGDLVEPSGSITGGSRNKRSSLAQKRE 668
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1325 YNELGAKVTERKQQLEKCLKLSRKMRKEMNALTEWLAATDMELtkrsavegmpsnldsevawgkatqKEIEKQKVHLKSV 1404
Cdd:COG1196    669 LKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQL------------------------EELERQLEELKRE 724
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1405 TEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLDESEKKKPQ 1484
Cdd:COG1196    725 LAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEE 804
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1485 QKEDI------LKRLKAEMNDIRPKVDSTRDQAANLMANRGDHCRKVVEPKISELNHRFAAISHRIKTGKASIPLKELEQ 1558
Cdd:COG1196    805 AERRLdalereLESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEE 884
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1559 FNSDIQKLLEPLEAEIQQgvNLKEEDFNKDMSEDNEGTVKELLQRGDNLQQRITDERK---REEIKIKQQLLQTKHNALK 1635
Cdd:COG1196    885 EKEELEEELRELESELAE--LKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEdtlETELEREIERLEEEIEALG 962
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023 1636 DLrsqrRKKALEishQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRElqKKKEELNAVRRQAEGLSE 1711
Cdd:COG1196    963 PV----NLRAIE---EYEEVEERYEELKSQREDLEEAKEKL-----LEVIEELDKE--KRERFKETFDKINENFSE 1024
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
2822-2854 2.54e-08

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 51.83  E-value: 2.54e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1953419023  2822 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 2854
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2336-2452 2.79e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 54.25  E-value: 2.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2336 NRRQQLNEMLKDSTQWLEAKEEaeqvlgqarakLESWKEAPYTVDAIQKKITETKQLAKDLRQWQINVDVANDLALKLLr 2415
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEA-----------LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1953419023 2416 DYSADDTRKVHMITENINASWASIHKRLSEREAALEE 2452
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1650-1752 3.07e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.86  E-value: 3.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1650 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1727
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 1953419023 1728 RWREIESKFAQFRRLNFAQIHTVHE 1752
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1113-1988 3.47e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 3.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1113 INEELETfnsRWRELHEEAVRRQKLLEQSiqsAQEIEKSLHLIQESLSSIDKQLAAYiadKVDAAQMPQEAQKIQSDLTS 1192
Cdd:TIGR02168  194 ILNELER---QLKSLERQAEKAERYKELK---AELRELELALLVLRLEELREELEEL---QEELKEAEEELEELTAELQE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1193 HEISLEEMKKHNQGKEtaqrvlSQIDVAQKKLQDVSMKFrlfqkpanfeQRLQESKMILDEVKMHLPA-LETKSVEQEVV 1271
Cdd:TIGR02168  265 LEEKLEELRLEVSELE------EEIEELQKELYALANEI----------SRLEQQKQILRERLANLERqLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1272 QSQLNhCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRK 1351
Cdd:TIGR02168  329 ESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1352 EMNALTEWLAATDMELTK--RSAVEGMPSNLDSEVAwgkATQKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLL 1429
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEEllKKLEEAELKELQAELE---ELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1430 NsnwiavtsRAEEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLD---ESEKKKPQQKEDILKRLKAEMNDIRPKVDS 1506
Cdd:TIGR02168  485 A--------QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGYEAAIEAALGGRLQAVVVENLN 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1507 TRDQAANLMANRGDHCR-----KVVEPKISELNHRFAAISHRIKTGkasiPLKELEQFNSDIQKLLEPLEA------EIQ 1575
Cdd:TIGR02168  557 AAKKAIAFLKQNELGRVtflplDSIKGTEIQGNDREILKNIEGFLG----VAKDLVKFDPKLRKALSYLLGgvlvvdDLD 632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1576 QGVNL-KEEDFNKDM-----------------SEDNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKD 1636
Cdd:TIGR02168  633 NALELaKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEElEEKIAELEKALAELRKELEELEE 712
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1637 LRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE--RKIKEIDRELQKKKEELNAVRRQAEGLSEDga 1714
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleAEIEELEERLEEAEEELAEAEAEIEELEAQ-- 790
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1715 amaVEPTQIQLSKRWREIESKFAQFRRLNfaqihtvheesvvamtedmpleisyvpstylteiTHVSQALSEVEELLNAP 1794
Cdd:TIGR02168  791 ---IEQLKEELKALREALDELRAELTLLN----------------------------------EEAANLRERLESLERRI 833
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1795 DLCAQDFEDLfkqEESLKNIKDSLQQISGRID---IIHNKKTAALHSATpAERAKLQEALSRLdfqwervnnmyKDRQGR 1871
Cdd:TIGR02168  834 AATERRLEDL---EEQIEELSEDIESLAAEIEeleELIEELESELEALL-NERASLEEALALL-----------RSELEE 898
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1872 FDRSVEKWRRfhyDMKILNQWLTEAEQflKKTQIPENWEHAKYKwyLKELQDGIGQRQSVvrvlnaTGEEIIQQSSKTDA 1951
Cdd:TIGR02168  899 LSEELRELES---KRSELRRELEELRE--KLAQLELRLEGLEVR--IDNLQERLSEEYSL------TLEEAEALENKIED 965
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023 1952 SILQ------------EKLGSLNLRWQEVCKQLAERKKRLEEQKNILSE 1988
Cdd:TIGR02168  966 DEEEarrrlkrlenkiKELGPVNLAAIEEYEELKERYDFLTAQKEDLTE 1014
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1986-2091 5.15e-08

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 53.48  E-value: 5.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1986 LSEFQRDVNEFVLWLEEADNVANIPLEPGNEQQLKEKLEQVKLLAEELPLRQGILKQLNETgGTVLVSAplSPEEQDKLE 2065
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNEL-AEKLIDE--GHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 1953419023 2066 NKLKQTNLQWIKVSRNLPEKQEEIEA 2091
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
2826-2852 6.99e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 425661 [Multi-domain]  Cd Length: 30  Bit Score: 50.58  E-value: 6.99e-08
                           10        20
                   ....*....|....*....|....*..
gi 1953419023 2826 PWERAISPNKVPYYINHETQTTCWDHP 2852
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SPEC smart00150
Spectrin repeats;
2703-2804 1.04e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.33  E-value: 1.04e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2703 QELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEITPLKENVSYVNDLARQLTTLGIQLSPYNLNT 2782
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1953419023  2783 LEDLNTRWKLLQVAIEDRIRQL 2804
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1344-1449 1.66e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 51.94  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1344 KLSRKMRKEMNALTEWLAATDMELTKRSaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVE 1423
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 1953419023 1424 DKLSLLNSNWIAVTSRAEEWLNLLLE 1449
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1452-1549 1.81e-07

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 51.94  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1452 KHMENFDQNVDYITNWIIQADALLDESEKKK----PQQKEDILKRLKAEMNDIRPKVDSTRDQAANLMANrGDHCRKVVE 1527
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKdlesVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
                           90       100
                   ....*....|....*....|..
gi 1953419023 1528 PKISELNHRFAAISHRIKTGKA 1549
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQ 101
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
3079-3125 3.49e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 48.97  E-value: 3.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1953419023 3079 CNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRvaKGHKMHYPMVEY 3125
Cdd:cd02249      3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1240-1449 3.96e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.60  E-value: 3.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1240 FEQRLQESKMILDEVKMHLPALETKSVEQEVvQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPkELDERVT 1319
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1320 ALKLHYNELGAKVTERKQQLEKCLKLSRKMRkEMNALTEWLAATDMELTKRSAVEGMPSnLDSEVAWGKATQKEIEKQKV 1399
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953419023 1400 HLKSVTEVGEAL-KTVLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLNLLLE 1449
Cdd:cd00176    161 RLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
332-599 3.33e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.91  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  332 KWQRFTEEQCLFSAWLSEKEDAVNKIHTTgfKDQSEVLSNLQKLAVLKTDLEKKKQTMDKLCSLNQDLLSAlkNTVVAHK 411
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  412 MEAWLDNFAQRWDNLVQKLEkssaqisqavtttqpsltqttvmetvtmvttrehilvkhaqeelpppppqKKRQIIVDSE 491
Cdd:cd00176     77 IQERLEELNQRWEELRELAE--------------------------------------------------ERRQRLEEAL 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  492 IRKRLDVDITELHSWITRSEAVLQSPEfaIYRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 571
Cdd:cd00176    107 DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                          250       260
                   ....*....|....*....|....*...
gi 1953419023  572 SIKQASEQLNSRWIEFCQLLSERLNWLE 599
Cdd:cd00176    183 EIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
935-1036 3.62e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 48.08  E-value: 3.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  935 LQKDLSEMHEWMTQAEEEYLERDFEyKTPDELQTAVEEMKRAKEEAQQKEAKVKLLTESVNSVIaQAPPAAQEALKKELD 1014
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 1953419023 1015 TLTTNYQWLCTRLNGKCKTLEE 1036
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1477-1747 4.28e-06

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


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 51.61  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1477 ESEKKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLMANRGDHCRKVVE--PKISELNHRFAAISHRIKTGKAsiplk 1554
Cdd:COG1340      2 LAMLDKLDELELKRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVRElrEKAQELREERDEINEEVQELKE----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1555 ELEQFNSDIQKL--------------------LEPLEAEIQQgvnLKEEDFNKDMSEDNEgtvKELLQRGDNLQQRITDE 1614
Cdd:COG1340     77 KRDEINAKLQELrkeyrelkekrnefnlggrsIKSLEREIER---LEKKQQTSVLTPEEE---RELVQKIKELRKELEDA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1615 RKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE--RKIKEIDREL 1692
Cdd:COG1340    151 KKALEENEKLKELKAEIDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEADELRKEADELHEEFVElsKKIDELHEEF 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 1693 QKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQI 1747
Cdd:COG1340    231 RNLQNELRELEKKIKALRAKEKAAKRREKREELKERAEEIYEKFKRGEKLTTEEL 285
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1651-1875 4.61e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.52  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1651 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1723
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1724 Q--LSKRWREIESKFAQFRRLnfaqihtvheesvvamtedmpLEISYVPSTYLTEITHVSQALSEVEELLNAPDLCaQDF 1801
Cdd:cd00176     81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1802 EDLFKQEESLKNIKDSLQQISGRIDIIHNKKTAALHSATPAERAKLQEALSRLDFQWERVNNMYKDRQGRFDRS 1875
Cdd:cd00176    139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
3079-3122 5.11e-06

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 45.80  E-value: 5.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1953419023 3079 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 3122
Cdd:cd02338      3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
919-1341 5.52e-06

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.42  E-value: 5.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  919 YARKEALKGGLDKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQTAVEE-------------------------- 972
Cdd:pfam05483  176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeykkeindkekqvsllliqitekenk 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  973 -------MKRAKEEAQQKEAKVKLLTESVNSVIaqappAAQEALKKELDTLTTNYQwlctRLNGKCKTLEEVWACWHELL 1045
Cdd:pfam05483  256 mkdltflLEESRDKANQLEEKTKLQDENLKELI-----EKKDHLTKELEDIKMSLQ----RSMSTQKALEEDLQIATKTI 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1046 SYLEKANKWLSEVEVKLKTTENISggAEEIAEVLDSLENLM----QHSEDNPNQIRILAQTLTDGGV----MDELIN--- 1114
Cdd:pfam05483  327 CQLTEEKEAQMEELNKAKAAHSFV--VTEFEATTCSLEELLrteqQRLEKNEDQLKIITMELQKKSSeleeMTKFKNnke 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1115 ---EELETFNSRWRELHEEAVRRQKLLEQSIQSAQEI-------EKSLHLIQESLSSIdKQLAAYIADKVDAAQMPQEAQ 1184
Cdd:pfam05483  405 velEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAI-KTSEEHYLKEVEDLKTELEKE 483
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1185 KIQS-DLTSH--EISLE-------------EMKKH----NQGKETAQRVLSQIDVAQKKlqDVSMKFRLFQKPANFEQRL 1244
Cdd:pfam05483  484 KLKNiELTAHcdKLLLEnkeltqeasdmtlELKKHqediINCKKQEERMLKQIENLEEK--EMNLRDELESVREEFIQKG 561
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1245 QESKMILDEVKMHLPALETKSVEQEVVQSQL-NHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENpkeldERVTALKL 1323
Cdd:pfam05483  562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILeNKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN-----KQLNAYEI 636
                          490
                   ....*....|....*...
gi 1953419023 1324 HYNELGAKVTERKQQLEK 1341
Cdd:pfam05483  637 KVNKLELELASAKQKFEE 654
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
771-1358 6.03e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 6.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  771 LSTTVKEMSKkapLSDISRKYQSEFEEIEGRWKKLSsqlvEHCQKLEEQMAKLRKIQNHIKTLKKWITEVDVFLKEewpa 850
Cdd:PRK03918   202 LEEVLREINE---ISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---- 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  851 lgdseiLKRQLKQCRLLVNDIQTIQPS------LNSVNEGAQKMKNEAEPEfAGRLETELRELNTQWDYMCRQVyARKEA 924
Cdd:PRK03918   271 ------LKKEIEELEEKVKELKELKEKaeeyikLSEFYEEYLDELREIEKR-LSRLEEEINGIEERIKELEEKE-ERLEE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  925 LKGgldKTVSLQKDLSEMHEWMTQAEE--------EYLERDFEYKTPDELQTAVEEMKRAKEEAQQKEAKVKLLTESVNS 996
Cdd:PRK03918   343 LKK---KLKELEKRLEELEERHELYEEakakkeelERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  997 VIAQappaaqeaLKKELDTLTtnyqwlctRLNGKCKT----LEEvwacwHELLSYLEKANKWLSEVEVKLKTTENISgga 1072
Cdd:PRK03918   420 EIKE--------LKKAIEELK--------KAKGKCPVcgreLTE-----EHRKELLEEYTAELKRIEKELKEIEEKE--- 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1073 EEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVR---RQKLLEQSIQSAQEIE 1149
Cdd:PRK03918   476 RKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEELK 555
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1150 KSLHLIQESLSSIDKQLAAYIadkvdaaqmpqeaqkiqsdltsheisleemkkhnqgKETAQRVLSQIDVAQKKLQDVSM 1229
Cdd:PRK03918   556 KKLAELEKKLDELEEELAELL------------------------------------KELEELGFESVEELEERLKELEP 599
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1230 KFRLFQKPANFEQRLQESKMildevkmhlpalETKSVEQEVVQSqlnhcvnlYKSLSEVKSEVEMVIKTGRQIVQKKQTE 1309
Cdd:PRK03918   600 FYNEYLELKDAEKELEREEK------------ELKKLEEELDKA--------FEELAETEKRLEELRKELEELEKKYSEE 659
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1953419023 1310 NPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNALTE 1358
Cdd:PRK03918   660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
964-1854 7.05e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 7.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  964 DELQTAVEE----MKRAKEEAQQKEAKVKLLTEsvnsviaqAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEEVWA 1039
Cdd:TIGR02169  187 ERLDLIIDEkrqqLERLRREREKAERYQALLKE--------KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1040 CWHELLSYLEKANKWLSEV--EVKLKTTENISGGAEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGgvmDELINEEL 1117
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEELnkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL---EAEIDKLL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1118 ETFNSRWRELHEEAVRRQKL----------LEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIAD----KVDAAQMPQEA 1183
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLteeyaelkeeLEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinelKRELDRLQEEL 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1184 QKIQSDLTSHEISLEEMK-KHNQGKETAQRVLSQIDVAQKKLQdvsmkfRLFQKPANFEQRLQESKMILDEVKMHLPALE 1262
Cdd:TIGR02169  416 QRLSEELADLNAAIAGIEaKINELEEEKEDKALEIKKQEWKLE------QLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1263 TKSVEQEVVQSQLNHCVNLYKSLSEV-KSEVEMVIKTGRQIVQKKQtenpkeldERVTALKLHY-NELGAKVTERKQQLE 1340
Cdd:TIGR02169  490 RELAEAEAQARASEERVRGGRAVEEVlKASIQGVHGTVAQLGSVGE--------RYATAIEVAAgNRLNNVVVEDDAVAK 561
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1341 KCLKLSRKMRKEmnaltewlAATDMELTKRSAVEGMPSNLDSEVAWGKAT-----QKEIEKQKVHLKSVTEVGEALKT-- 1413
Cdd:TIGR02169  562 EAIELLKRRKAG--------RATFLPLNKMRDERRDLSILSEDGVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDIEAar 633
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1414 -VLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLnllleyqkhmenfdqnvdyitnwiiqadALLDESEKKKPQQKEDILKR 1492
Cdd:TIGR02169  634 rLMGKYRMVTLEGELFEKSGAMTGGSRAPRGG----------------------------ILFSRSEPAELQRLRERLEG 685
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1493 LKAEMNDIRPKVDSTRDQAANLMANRGDHCRKVVE--PKISELNHRFAAISHRIKTGKASIplKELEQFNSDIQKLLEPL 1570
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEieKEIEQLEQEEEKLKERLEELEEDL--SSLEQEIENVKSELKEL 763
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1571 EAEIQQgvnlKEEDFNKDMSEDNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEIS 1649
Cdd:TIGR02169  764 EARIEE----LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1650 HQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLskrw 1729
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA---- 910
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1730 rEIESKFAQFRRLNfAQIHTVHEEsvVAMTEDMPLEISYVPSTYLTeITHVSQALSEVEELLNAPD----LCAQDFEDLF 1805
Cdd:TIGR02169  911 -QIEKKRKRLSELK-AKLEALEEE--LSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEpvnmLAIQEYEEVL 985
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953419023 1806 KQEESLKNIKDSLQ----QISGRIDIIHNKKTAALHSATPAERAKLQEALSRL 1854
Cdd:TIGR02169  986 KRLDELKEKRAKLEeerkAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL 1038
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1133-1711 9.04e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.58  E-value: 9.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1133 RRQKLLEQSIQSAQEIEKSLH-----LIQEsLSSIDKQLAAYIADKVDAAQMPQEAQKIqsdLTSHEISLEEmkkhnqgk 1207
Cdd:PRK02224   185 QRGSLDQLKAQIEEKEEKDLHerlngLESE-LAELDEEIERYEEQREQARETRDEADEV---LEEHEERREE-------- 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1208 etaqrvlsqIDVAQKKLQDVSMKFR-LFQKPANFEQRLQESKMILDEVKMHLPAL----ETKSVEQEVVQSQLNhcvnly 1282
Cdd:PRK02224   253 ---------LETLEAEIEDLRETIAeTEREREELAEEVRDLRERLEELEEERDDLlaeaGLDDADAEAVEARRE------ 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1283 kSLSEVKSEVEMVIKTGRQIVQKKQ------TENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNAL 1356
Cdd:PRK02224   318 -ELEDRDEELRDRLEECRVAAQAHNeeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1357 TEWLAATDMEL----TKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVG---------------EALKTVLGK 1417
Cdd:PRK02224   397 RERFGDAPVDLgnaeDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvegsphvETIEEDRER 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1418 KEMLvEDKLSLLNSNWIAVTSRAEEwLNLLLEYQKHMENFDQNVDYITNWIIQADALLDEsekkkpqqKEDILKRLKAEM 1497
Cdd:PRK02224   477 VEEL-EAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEE--------KRERAEELRERA 546
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1498 NDIRPKVDSTRDQAANLMaNRGDHCRKVVepkiSELNHRFAAISHRIKTgkasipLKELEqfnsDIQKLLEPLEAEIQQg 1577
Cdd:PRK02224   547 AELEAEAEEKREAAAEAE-EEAEEAREEV----AELNSKLAELKERIES------LERIR----TLLAAIADAEDEIER- 610
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1578 VNLKEEDFNkDMSEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKaleishqwyqykr 1657
Cdd:PRK02224   611 LREKREALA-ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREER------------- 676
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1658 qaDDLLKCLDDIEKKLASLPEPRDERKikeidrELQKKKEELNAVRRQAEGLSE 1711
Cdd:PRK02224   677 --DDLQAEIGAVENELEELEELRERRE------ALENRVEALEALYDEAEELES 722
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2232-2345 9.08e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 49.37  E-value: 9.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2232 LLEVPALADFNRAWTELTDWLSLLDRVIKSQrVMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNKtSNQE 2311
Cdd:cd00176    102 LEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPD 179
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1953419023 2312 ARTIITDRIERIQSQWDEVQEHLQNRRQQLNEML 2345
Cdd:cd00176    180 ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
695-1339 9.73e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 9.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  695 ADVQAREKELQTIFDSLppMRYQETMSTILTWIQQSETKLSIPQVTVTEydiMEQRLGELQALQSSLQEQQNGLnylstt 774
Cdd:TIGR02168  232 LRLEELREELEELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSE---LEEEIEELQKELYALANEISRL------ 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  775 vkEMSKkaplsdisRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIKTLKKWITEVDVFLKEEWPALGDS 854
Cdd:TIGR02168  301 --EQQK--------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  855 EILKRQL---------------KQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEFAGRLETELRELNtqwdymcRQVY 919
Cdd:TIGR02168  371 ESRLEELeeqletlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ-------AELE 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  920 ARKEALKGGLDKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQTAVEEMKRAKEEAQQKEAKVK----------- 988
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLknqsglsgilg 523
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  989 --------------------------LLTESVNSVIAQAPPAAQEALKK----ELDTLTTNYqwLCTRLNGKCKTLEEVW 1038
Cdd:TIGR02168  524 vlselisvdegyeaaieaalggrlqaVVVENLNAAKKAIAFLKQNELGRvtflPLDSIKGTE--IQGNDREILKNIEGFL 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1039 ACWHELLSYLEKANKWLS----------------EVEVKLKTTENI--------------SGGAEE----IAEVLDSLEN 1084
Cdd:TIGR02168  602 GVAKDLVKFDPKLRKALSyllggvlvvddldnalELAKKLRPGYRIvtldgdlvrpggviTGGSAKtnssILERRREIEE 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1085 LMQHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDK 1164
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1165 QLAAYIADKVDAAQMPQEA-QKIQSDLTSHEISLEEMKKHNQGKETAQRVLS--QIDVAQKKLQDVSMKFRLFQKPANFE 1241
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALDELRAELTllNEEAANLRERLESLERRIAATERRLE 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1242 QRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSE----VKSEVEMVIKTGRQIVQKKQ--TENPKELD 1315
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSelRRELEELR 921
                          730       740
                   ....*....|....*....|....
gi 1953419023 1316 ERVTALKLHYNELGAKVTERKQQL 1339
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDNLQERL 945
SPEC smart00150
Spectrin repeats;
499-599 1.03e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 1.03e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   499 DITELHSWITRSEAVLQSPEFAiyRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 578
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1953419023   579 QLNSRWIEFCQLLSERLNWLE 599
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1554-2375 1.12e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1554 KELEQFNSDIQKLlEPLEAEIQQGVNLKEEDFNKDMSEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNA 1633
Cdd:TIGR02168  239 EELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1634 LKDLRSQ------RRKKALEISHQWyqyKRQADDLLKCLDDIEKKLASLPEPRD--ERKIKEIDRELQKKKEELNAVRRQ 1705
Cdd:TIGR02168  318 LEELEAQleelesKLDELAEELAEL---EEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1706 AEGLSEDGAAMAVEPTQIQLSKRwREIESKFAQFRRLNFAQIHTVHEESVvamTEDMPLEisyvpstylTEITHVSQALS 1785
Cdd:TIGR02168  395 IASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELE---ELEEELE---------ELQEELERLEE 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1786 EVEELLNAPDLCAQDFEDLFKQEESLKNIKDSLQQISGRIDIIHNKKTAALHsatpaERAKLQEALSRLdfqWERVNnmy 1865
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK-----NQSGLSGILGVL---SELIS--- 530
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1866 kdrqgrFDrsvEKW----------RRFHYDMKILNQWLtEAEQFLKKtqipenweHAKYKWYLKELQDGIGQRQSVVRVL 1935
Cdd:TIGR02168  531 ------VD---EGYeaaieaalggRLQAVVVENLNAAK-KAIAFLKQ--------NELGRVTFLPLDSIKGTEIQGNDRE 592
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1936 NATGEEIIQQSSK---TDASILQEKLGSL--NLRWQEVCKQLAERKKRLEEQKNILSEFQRDVNEFVLWLEEADNVANIP 2010
Cdd:TIGR02168  593 ILKNIEGFLGVAKdlvKFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSI 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2011 LEPGNE-QQLKEKLEQVKLLAEELplrqgiLKQLNETggtvlvsaplsPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEI 2089
Cdd:TIGR02168  673 LERRREiEELEEKIEELEEKIAEL------EKALAEL-----------RKELEELEEELEQLRKELEELSRQISALRKDL 735
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2090 EAHVKDLGQLEEQLNHLLLWLSPIRNQLEIYNQPNQTGPFDIKEIEVAVQAKQPDVEGILSkgqhlykekpATQPAKRKL 2169
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----------ELKALREAL 805
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2170 EDLSsdwKVVTQLLQELRAKQPGPAPGLTTVRAPPSQTVTLVTQPAVTKETaISKLEmpsslllevPALADFNRAWTELT 2249
Cdd:TIGR02168  806 DELR---AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLA---------AEIEELEELIEELE 872
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2250 DWLSLLDRVIKSQRVmvgDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQnlknktsnqeartiitDRIERIQSQWDE 2329
Cdd:TIGR02168  873 SELEALLNERASLEE---ALALLRSELEELSEELRELESKRSELRRELEELR----------------EKLAQLELRLEG 933
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*..
gi 1953419023 2330 VQEHLQNRRQQLNEMLKDSTQWLEAKEEA-EQVLGQARAKLESWKEA 2375
Cdd:TIGR02168  934 LEVRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRLENK 980
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2455-2557 1.34e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.54  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2455 RLLQQFPLDLEKFLAWLTEAETTANvlqdathKERLLEDSKGVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLrsLEG 2534
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 1953419023 2535 SDDAALLQRRLDNMNFKWSELRK 2557
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
165-1165 1.77e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.87  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  165 QGRVGNVLQLGSQ--------LIGTGKL-SEDEETE-----VQEQMNLLNSRWECL--RVASMEKQSNLHKVLMDLQNQq 228
Cdd:COG1196    143 QGKVEEIINAKPEerrklieeAAGVSKYkERKEEAErklerTEENLERLEDLLEELekQLEKLERQAEKAERYQELKAE- 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  229 LKELNDWLTKTEERTRKMEKEPLgpdIEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKvl 308
Cdd:COG1196    222 LRELELALLLAKLKELRKELEEL---EEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEE-- 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  309 gdrwanicrwtedrwvlLQDILLKWQRFTEEqclfsawLSEKEDAVNKIHTTGFKDQSEVLSNLQKLAVLKTDLEKKKQT 388
Cdd:COG1196    297 -----------------IEELEGEISLLRER-------LEELENELEELEERLEELKEKIEALKEELEERETLLEELEQL 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  389 ---MDKLCSLNQDLLSALKNTVVAHKmeawlDNFAQRWDNLVQKLEKSSAQISQavtttqpsltqttvmetvtmvttreh 465
Cdd:COG1196    353 laeLEEAKEELEEKLSALLEELEELF-----EALREELAELEAELAEIRNELEE-------------------------- 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  466 ilvkhAQEELPPPPPQKKRQiivdSEIRKRLDVDITELHSWITRSEAVLQSPEFAIYRKEGNFSDLKEKVNAIEREKAEK 545
Cdd:COG1196    402 -----LKREIESLEERLERL----SERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAEL 472
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  546 FRKLQDASR---SAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNW-LEYQNNI-ITFYNQLQQLEqmttt 620
Cdd:COG1196    473 QEELQRLEKelsSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVkEKYETALeAALGNRLQAVV----- 547
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  621 aenwlktqptTTSEPTAIKSQLKICKDEINRLSALQPQIERLKIQSIALKEKGQGPMFLDA-DF-VAFTNHFNQVFADVq 698
Cdd:COG1196    548 ----------VENEEVAKKAIEFLKENKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLiDFdPKYEPAVRFVLGDT- 616
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  699 arekelqTIFDSLPPMRYQETMSTILTWIQQSETKLSIPQVTVT----EYDIMEQRLGELQALQSSLQEQQNGLNYLSTT 774
Cdd:COG1196    617 -------LVVDDLEQARRLARKLRIKYRIVTLDGDLVEPSGSITggsrNKRSSLAQKRELKELEEELAELEAQLEKLEEE 689
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  775 VKEmskkapLSDISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIKTLKKWITEVDvflkeewpalGDS 854
Cdd:COG1196    690 LKS------LKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELE----------EEL 753
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  855 EILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEFAgRLETELRELNtqwdymcrqvyARKEALKGGLDKTVS 934
Cdd:COG1196    754 EELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELE-ELEEELEEAE-----------RRLDALERELESLEQ 821
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  935 LQKDLSEMHEWMTQAEEEYLERDfeyktpDELQTAVEEMKRAKEEAQQKEAKVKLLTESVNSVIaqappaaqEALKKELD 1014
Cdd:COG1196    822 RRERLEQEIEELEEEIEELEEKL------DELEEELEELEKELEELKEELEELEAEKEELEDEL--------KELEEEKE 887
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1015 TLTTNYQWLCTRLngkcktleevwacwHELLSYLEKANKWLSEVEVKLKTTENISggaEEIAEVLDSLENLMQHSEDNpN 1094
Cdd:COG1196    888 ELEEELRELESEL--------------AELKEEIEKLRERLEELEAKLERLEVEL---PELEEELEEEYEDTLETELE-R 949
                          970       980       990      1000      1010      1020      1030
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953419023 1095 QIRILAQTLTDGGVMDELINEELETFNSRWRELHEEavrrqklleqsiqsAQEIEKSLHLIQESLSSIDKQ 1165
Cdd:COG1196    950 EIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQ--------------REDLEEAKEKLLEVIEELDKE 1006
SPEC smart00150
Spectrin repeats;
830-926 1.99e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 1.99e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   830 IKTLKKWITEVDVFLKEEWPAlGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEfAGRLETELRELNT 909
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNE 84
                            90
                    ....*....|....*..
gi 1953419023   910 QWDYMCRQVYARKEALK 926
Cdd:smart00150   85 RWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1653-1735 2.01e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.01e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  1653 YQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDG--AAMAVEPTQI 1723
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLesveallKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90
                    ....*....|..
gi 1953419023  1724 QLSKRWREIESK 1735
Cdd:smart00150   81 ELNERWEELKEL 92
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1480-2395 2.59e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.48  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1480 KKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLManrgdhcrkvvepkiselnhRFAAISHRIKTGKASIPLKELEQF 1559
Cdd:COG1196    178 ERKLERTEENLERLEDLLEELEKQLEKLERQAEKAE--------------------RYQELKAELRELELALLLAKLKEL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1560 NSDIQKLLEPLEaeiqqgvNLKEEdfnkdmSEDNEGTVKELLQRGDNLQQRItdERKREEIKIKQQLLQTKHNALKDLRS 1639
Cdd:COG1196    238 RKELEELEEELS-------RLEEE------LEELQEELEEAEKEIEELKSEL--EELREELEELQEELLELKEEIEELEG 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1640 QRRkkaleishqwyQYKRQADDLLKCLDDIEKKLASLPEPRDERK-----IKEIDRELQKKKEELNAVRRQAEglsedga 1714
Cdd:COG1196    303 EIS-----------LLRERLEELENELEELEERLEELKEKIEALKeeleeRETLLEELEQLLAELEEAKEELE------- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1715 amaveptqIQLSKRWREIESKFAQFRrlnfAQIHTVHEEsvvamtedmpleisyvpstyLTEITHVSQAL-SEVEELLNA 1793
Cdd:COG1196    365 --------EKLSALLEELEELFEALR----EELAELEAE--------------------LAEIRNELEELkREIESLEER 412
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1794 PDLCAQDFEDLFKQEESLKNIKDSLQQISGRIDIIHNKKTAALHSATpAERAKLQEALSRLDFQWERVNNMYKDRQGRFD 1873
Cdd:COG1196    413 LERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELR-DRLKELERELAELQEELQRLEKELSSLEARLD 491
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1874 RSVEKWRRFHYD---MKILNQWLTEA----EQFLKktqIPENWEHAkykwylkelqdgigqrqsVVRVLNATGEEIIQQS 1946
Cdd:COG1196    492 RLEAEQRASQGVravLEALESGLPGVygpvAELIK---VKEKYETA------------------LEAALGNRLQAVVVEN 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1947 sKTDASILQEKLGSLNLRWQ-----EVCKQLAERKKRLEEQKNILS----EFQ---RDVNEFVL-------WLEEADNVA 2007
Cdd:COG1196    551 -EEVAKKAIEFLKENKAGRAtflplDRIKPLRSLKSDAAPGFLGLAsdliDFDpkyEPAVRFVLgdtlvvdDLEQARRLA 629
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2008 NIPLEP------------------GNEQQLKEKLEQVKLLAEELPLRQGILKQLNETGGTVLVSaplsPEEQDKLENKLK 2069
Cdd:COG1196    630 RKLRIKyrivtldgdlvepsgsitGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSL----KNELRSLEDLLE 705
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2070 QTNLQWIKVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQLEIYNQpnqtgpfDIKEIEVAVQAKQPDVEGIL 2149
Cdd:COG1196    706 ELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQE-------RLEELEEELESLEEALAKLK 778
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2150 SKGQHLYKEKPATQPAKRKLEDLSSDWKVVTQLLQELRAKQpgpapglttvrappsqtvtlvTQPAVTKETAISKLEMPS 2229
Cdd:COG1196    779 EEIEELEEKRQALQEELEELEEELEEAERRLDALERELESL---------------------EQRRERLEQEIEELEEEI 837
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2230 SLLLEvpALADFNRAWTELTDWLSLLDRVIKSQRVMVGDLED----INEMIIKQKATLQDLEQRRPQLEELITAAQNLKN 2305
Cdd:COG1196    838 EELEE--KLDELEEELEELEKELEELKEELEELEAEKEELEDelkeLEEEKEELEEELRELESELAELKEEIEKLRERLE 915
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2306 --KTSNQEARTIITDRIERIQSQWDEVQEH-LQNRRQQLNEMLKD-STQWLEAKEEAEQVLGQAR---AKLESWKEApyt 2378
Cdd:COG1196    916 elEAKLERLEVELPELEEELEEEYEDTLETeLEREIERLEEEIEAlGPVNLRAIEEYEEVEERYEelkSQREDLEEA--- 992
                          970
                   ....*....|....*..
gi 1953419023 2379 VDAIQKKITETKQLAKD 2395
Cdd:COG1196    993 KEKLLEVIEELDKEKRE 1009
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1240-1648 2.70e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.10  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1240 FEQRLQESKMILDEVKMHLPALETKSVEqevVQSQLNHC------VNLYKSLSEVKSEVEMVIkTGRQIVQKKQTENpkE 1313
Cdd:COG1196    170 YKERKEEAERKLERTEENLERLEDLLEE---LEKQLEKLerqaekAERYQELKAELRELELAL-LLAKLKELRKELE--E 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1314 LDERVTALKLHYNELGAKVTERKQQLEKclklSRKMRKEMNALTEWLAATDMELTKrsavegmpsnldsevawgkaTQKE 1393
Cdd:COG1196    244 LEEELSRLEEELEELQEELEEAEKEIEE----LKSELEELREELEELQEELLELKE--------------------EIEE 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1394 IEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMENFDqnvdyitnwiiQADA 1473
Cdd:COG1196    300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELE-----------EKLS 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1474 LLDESEKKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLMANRGDHCRkvvepKISELNHRFAAISHRIKTGKasipl 1553
Cdd:COG1196    369 ALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSE-----RLEDLKEELKELEAELEELQ----- 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1554 KELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMSEDN-EGTVKELLQRGDNLQ-QRITDERKREEIKIKQQLLQTKH 1631
Cdd:COG1196    439 TELEELNEELEELEEQLEELRDRLKELERELAELQEELQRlEKELSSLEARLDRLEaEQRASQGVRAVLEALESGLPGVY 518
                          410
                   ....*....|....*....
gi 1953419023 1632 NALKDLRSQRRK--KALEI 1648
Cdd:COG1196    519 GPVAELIKVKEKyeTALEA 537
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
427-1205 2.70e-05

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 50.35  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  427 VQKLEKSSAQISQAVTTTQPSLTQTTVMETVTMVTTREHILVKHAQEELPPPPPQKKRQIIVDSEIRKRLDVDITELHSw 506
Cdd:TIGR00618  221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI- 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  507 itrsEAVLQSPEfaiyRKEGNFSDLKEKvnaiEREKAEKFRKLQDASRSAQALVEQMVNEGV---NADSIKQASEQLNSR 583
Cdd:TIGR00618  300 ----KAVTQIEQ----QAQRIHTELQSK----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSI 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  584 WIEFCQLLSERLNWLEYQNNIITFYNQLQQLEQMTTTAENWLKTQPTTTSEPTAIKSQLKICKDEInrlsalQPQIERLK 663
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ------ELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  664 IQSIALKEKGQgpmfldadfvaftnhfnqvfaDVQAREKELQTIFDSLPPMryqetmstiltwIQQSETKLSIPQVTVTE 743
Cdd:TIGR00618  442 LCAAAITCTAQ---------------------CEKLEKIHLQESAQSLKER------------EQQLQTKEQIHLQETRK 488
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  744 YDIMEQRLGELQALQSSLQEQQnglnylsttvKEMSKKAPLSDISRKYQSEFEEIEGRWKKlssqlveHCQKLEEQMAKL 823
Cdd:TIGR00618  489 KAVVLARLLELQEEPCPLCGSC----------IHPNPARQDIDNPGPLTRRMQRGEQTYAQ-------LETSEEDVYHQL 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  824 RKIQNHIKTLKKWITEVD---VFLKEEWPALgdSEILKRqlkqcrlLVNDIQTIQPSLNSVNEgAQKMKNEAEPEFAGRL 900
Cdd:TIGR00618  552 TSERKQRASLKEQMQEIQqsfSILTQCDNRS--KEDIPN-------LQNITVRLQDLTEKLSE-AEDMLACEQHALLRKL 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  901 ETELRELN-TQWDYMCRQVYARKEALKGGLDKTVsLQKDLSEMHEWMTQAEEEYLERdfEYKTPDELQTAVEEMKRAKEE 979
Cdd:TIGR00618  622 QPEQDLQDvRLHLQQCSQELALKLTALHALQLTL-TQERVREHALSIRVLPKELLAS--RQLALQKMQSEKEQLTYWKEM 698
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  980 AQQKEAKVKLLTESVNSV------IAQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANK 1053
Cdd:TIGR00618  699 LAQCQTLLRELETHIEEYdrefneIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA 778
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1054 WLSEVEVKLkttENISGGAEEIAEVLDSLENLMQHSEDNPNQIRILAQtltdggvmdELINEELETFNSRWRELHEE--A 1131
Cdd:TIGR00618  779 ELSHLAAEI---QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC---------ETLVQEEEQFLSRLEEKSATlgE 846
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953419023 1132 VRRQ--KLLEQSIQSAQEIEKSLHLIQES--LSSIDKQLAAYIADKvdaaqMPQEAQKIQSDLTSHEISLEEMKKHNQ 1205
Cdd:TIGR00618  847 ITHQllKYEECSKQLAQLTQEQAKIIQLSdkLNGINQIKIQFDGDA-----LIKFLHEITLYANVRLANQSEGRFHGR 919
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1474-2122 2.84e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.10  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1474 LLDESEKKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLMANRGDHcrkvvEPKISELNHRFAAISHRI--KTGKASI 1551
Cdd:COG1196    218 LKAELRELELALLLAKLKELRKELEELEEELSRLEEELEELQEELEEA-----EKEIEELKSELEELREELeeLQEELLE 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1552 PLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMSEDN-EGTVKELLQRGDNLQQRITD-----ERKREEIKIKQQ 1625
Cdd:COG1196    293 LKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEAlKEELEERETLLEELEQLLAEleeakEELEEKLSALLE 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1626 LLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEELNAVRRQ 1705
Cdd:COG1196    373 ELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDL-----KEELKELEAELEELQTELEELNEE 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1706 AEGLSEdgaamAVEPTQIQLSKRWREIESKFAQFRRLNFaqiHTVHEESVVAMTEDMPLEISYVPSTYLTEITHVSQALS 1785
Cdd:COG1196    448 LEELEE-----QLEELRDRLKELERELAELQEELQRLEK---ELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYG 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1786 EVEELLNAPD---------LCAQDFEDLFKQEESLKNIKDSL-QQISGRIDIIhnkktaalhsatPAERAKLQEALSRLD 1855
Cdd:COG1196    520 PVAELIKVKEkyetaleaaLGNRLQAVVVENEEVAKKAIEFLkENKAGRATFL------------PLDRIKPLRSLKSDA 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1856 FQWervNNMYKDRQGRFDRSVEKWRRFHYDMKILNQWLTEAEQFLKKTQIPENW-------------------EHAKYKW 1916
Cdd:COG1196    588 APG---FLGLASDLIDFDPKYEPAVRFVLGDTLVVDDLEQARRLARKLRIKYRIvtldgdlvepsgsitggsrNKRSSLA 664
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1917 YLKELQDGIGQRQSVVRVLNATGEEIIQQSSKTDAsiLQEKLGSLNLRWQEVCKQLAERKKRLEEQKNILSEFQRDVNEF 1996
Cdd:COG1196    665 QKRELKELEEELAELEAQLEKLEEELKSLKNELRS--LEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1997 VLWLEEADNvaniplepgneqQLKEKLEQVKLLAEELPLRQGILKQLNETGGTVLVSAPLSPEEQDKLENKLKQTNLQWI 2076
Cdd:COG1196    743 EEELEELEE------------ELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLD 810
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1953419023 2077 KVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQLEIYNQ 2122
Cdd:COG1196    811 ALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEK 856
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1388-1545 2.89e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 47.83  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1388 KATQKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMENFDQNVDyITNW 1467
Cdd:cd00176     43 EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQW 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1468 IIQADALLDESEK-KKPQQKEDILKRLKAEMNDI---RPKVDSTRDQAANLMANRGDHCRKVVEPKISELNHRFAAISHR 1543
Cdd:cd00176    122 LEEKEAALASEDLgKDLESVEELLKKHKELEEELeahEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLEL 201

                   ..
gi 1953419023 1544 IK 1545
Cdd:cd00176    202 AE 203
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1239-1830 5.26e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 49.37  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1239 NFEQRLQESKMILDEvkmhlpalETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKtgrqivQKKQTENPKELDERV 1318
Cdd:COG0419    189 ELEGQLSELLEDIED--------LLEALEEELKELKKLEEIQEEQEEEELEQEIEALEE------RLAELEEEKERLEEL 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1319 TALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEmnaLTEWLAATDMELTKRSAVEGMPSNLDSEVawgkatQKEIEKQK 1398
Cdd:COG0419    255 KARLLEIESLELEALKIREEELRELERLLEELEE---KIERLEELEREIEELEEELEGLRALLEEL------EELLEKLK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1399 VHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNsnwiAVTSRAEEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLDES 1478
Cdd:COG0419    326 SLEERLEKLEEKLEKLESELEELAEEKNELAK----LLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAEL 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1479 E-------------KKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLMANRGD---------HCRKVVEPKISEL-NH 1535
Cdd:COG0419    402 SaaleeiqeeleelEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAgekcpvcgqELPEEHEKELLELyEL 481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1536 RFAAISHRIKTGKAsipLKELEQFNSDIQKLLEplEAEIQQGVNLKEEDFNKDMSEDNEGTVKELLQRGDNLQQRITDER 1615
Cdd:COG0419    482 ELEELEEELSREKE---EAELREEIEELEKELR--ELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQ 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1616 KREEIKIKQQLLQTKHNALKDLRSQRRKKAL--EISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQ 1693
Cdd:COG0419    557 LKEELRQLEDRLQELKELLEELRLLRTRKEEleELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEELE 636
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1694 KKKEELNAVRRQAEGLSEDgaamaveptQIQLSKRWREIESKFAQFRRLNFAQIHTVHEESVVAMTEDMPLEISYVPSTY 1773
Cdd:COG0419    637 SELEKLNLQAELEELLQAA---------LEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELEEL 707
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953419023 1774 LTEITHVSQALSEVEELLNAPDLCAQDFEDLFKQEESLKNIKDSLQQISGRIDIIHN 1830
Cdd:COG0419    708 LKKLGEIEQLIEELESRKAELEELKKELEKLEKALELLEELREKLGKAGLRADILRN 764
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1940-2721 5.81e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 49.33  E-value: 5.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1940 EEIIQQSSKTDASILQEKLGSLNL--RWQEVCKQLAERKKRLEEQKNILSEFQRDVNEfvlwLEEADNVANiplepgNEQ 2017
Cdd:COG1196    147 EEIINAKPEERRKLIEEAAGVSKYkeRKEEAERKLERTEENLERLEDLLEELEKQLEK----LERQAEKAE------RYQ 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2018 QLKEKLE--QVKLLAEELplrQGILKQLNETGGTVLvsapLSPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKD 2095
Cdd:COG1196    217 ELKAELRelELALLLAKL---KELRKELEELEEELS----RLEEELEELQEELEEAEKEIEELKSELEELREELEELQEE 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2096 LGQLEEQLNHLLLWLSPIRNQLEIYNQPNQTGPFDIKEIEVAVQAKQPDVEGILSKGQHLYKEKPATQPAKRKLEDLSSD 2175
Cdd:COG1196    290 LLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSA 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2176 WKV-VTQLLQELRAKqpgpapgLTTVRAppsqTVTLVTQPAVTKETAISKLEMPSSLLLEvpALADFNRAWTELTDWLSL 2254
Cdd:COG1196    370 LLEeLEELFEALREE-------LAELEA----ELAEIRNELEELKREIESLEERLERLSE--RLEDLKEELKELEAELEE 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2255 LDRviksqrvmvgDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQ----NLKNKTSNQEARTiitDRIERIQSQWDEV 2330
Cdd:COG1196    437 LQT----------ELEELNEELEELEEQLEELRDRLKELERELAELQeelqRLEKELSSLEARL---DRLEAEQRASQGV 503
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2331 QEHLQNRRQ-------QLNEMLKDSTQWLEAKE------------EAEQVLGQARAKLESwKEAPYTVDAIQKKITETKQ 2391
Cdd:COG1196    504 RAVLEALESglpgvygPVAELIKVKEKYETALEaalgnrlqavvvENEEVAKKAIEFLKE-NKAGRATFLPLDRIKPLRS 582
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2392 LAKDLRQWQInvDVANDL-----ALKLLRDYSADDTRKVHMITENINASWA-SIHKRLSEREAALEETHRLL------QQ 2459
Cdd:COG1196    583 LKSDAAPGFL--GLASDLidfdpKYEPAVRFVLGDTLVVDDLEQARRLARKlRIKYRIVTLDGDLVEPSGSItggsrnKR 660
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2460 FPLDLEKFLAWLTEA-ETTANVLQDATHKERLLEDSkgVRELMKQWQDLQGEIEAHTDIYHNLDENGQKVLRSLE-GSDD 2537
Cdd:COG1196    661 SSLAQKRELKELEEElAELEAQLEKLEEELKSLKNE--LRSLEDLLEELRRQLEELERQLEELKRELAALEEELEqLQSR 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2538 AALLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLV---WLQLKDDELSRQApiggdfpavQKQNDVH 2614
Cdd:COG1196    739 LEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEkrqALQEELEELEEEL---------EEAERRL 809
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2615 RAFKRELKTKEPVIMSTLETVRiFLTEQPLEGLEKLYQEPRELppeERAQNVTRLLRKQAEEVNTQWEKLNVH------- 2687
Cdd:COG1196    810 DALERELESLEQRRERLEQEIE-ELEEEIEELEEKLDELEEEL---EELEKELEELKEELEELEAEKEELEDElkeleee 885
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1953419023 2688 SADWQRKIDEALERLQELQEATDELDLKLRQAEV 2721
Cdd:COG1196    886 KEELEEELRELESELAELKEEIEKLRERLEELEA 919
SPEC smart00150
Spectrin repeats;
1988-2090 6.21e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.63  E-value: 6.21e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  1988 EFQRDVNEFVLWLEEADNVANIPLEPGNEQQLKEKLEQVKLLAEELPLRQGILKQLNETGGTVLVSaplSPEEQDKLENK 2067
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1953419023  2068 LKQTNLQWIKVSRNLPEKQEEIE 2090
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1042-1139 6.65e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 6.65e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  1042 HELLSYLEKANKWLSEVEVKLKTTE--NISGGAEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGGVMD-ELINEELE 1118
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDlgKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDaEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1953419023  1119 TFNSRWRELHEEAVRRQKLLE 1139
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1526-2033 1.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1526 VEPKISELNHRFAAISHRIKtgKASIPLKELEQFNSDIQKLLEPLEA--EIQQGVNLKEEDFNKDMSEDNEgTVKELLQR 1603
Cdd:PRK03918   191 IEELIKEKEKELEEVLREIN--EISSELPELREELEKLEKEVKELEElkEEIEELEKELESLEGSKRKLEE-KIRELEER 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1604 GDNLQQRITD-ERKREEIKiKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPrdE 1682
Cdd:PRK03918   268 IEELKKEIEElEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL--K 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1683 RKIKEIDRELQKKK------EELNAVRRQAEGLSEDGAAMAVEPTQIQL---SKRWREIESKFAQFRRlNFAQIHTVHEE 1753
Cdd:PRK03918   345 KKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELeelEKAKEEIEEEISKITA-RIGELKKEIKE 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1754 SVVAM-----------------TEDMPLEISyvpSTYLTEITHVSQALSEVEELLnapdlcaqdfEDLFKQEESLKNIkd 1816
Cdd:PRK03918   424 LKKAIeelkkakgkcpvcgrelTEEHRKELL---EEYTAELKRIEKELKEIEEKE----------RKLRKELRELEKV-- 488
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1817 slqqISGRIDIIHNKKTAAlhsatpaERAKLQEALSRLDFqwERVNNMYKDrqgrFDRSVEKWRRFHYDMKILNQWLTEA 1896
Cdd:PRK03918   489 ----LKKESELIKLKELAE-------QLKELEEKLKKYNL--EELEKKAEE----YEKLKEKLIKLKGEIKSLKKELEKL 551
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1897 EQFLKKTQIPENwEHAKYKWYLKELQDGIGQR--------QSVVRVLNATGEEIIQ-QSSKTDASILQEKLGSLNLRWQE 1967
Cdd:PRK03918   552 EELKKKLAELEK-KLDELEEELAELLKELEELgfesveelEERLKELEPFYNEYLElKDAEKELEREEKELKKLEEELDK 630
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1968 VCKQLAERKKRLEEQKNILSEFQRDVNEfvlwlEEADNVANIPLEPGNE--------QQLKEKLEQVKLLAEEL 2033
Cdd:PRK03918   631 AFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEYLELSRElaglraelEELEKRREEIKKTLEKL 699
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
689-1369 1.07e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 48.17  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  689 HFNQVFADVQAREKELQTIFDSLPPMRYQETMSTILTWIQQSETKLSIPQVTVTEYDIMEQRLGELQALQSSLQEQQNGL 768
Cdd:pfam15921  107 YLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLNDSNTQIEQLRKMMLSHEGVL 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  769 NYLSTTV---KEMSKK-----------------APLSDISRKYQSEFEEIEGRWKKLSSQLveHCQKLEEQMAKLRKIQN 828
Cdd:pfam15921  187 QEIRSILvdfEEASGKkiyehdsmstihfrslgSAISKILRELDTEISYLKGRIFPVEDQL--EALKSESQNKIELLLQQ 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  829 HIKTLKKWITEVDVFLKeewpalGDSEILKRQLKQCRLLVNDIQTIQPslNSVNEGAQKMKNEAEPE-FAGRLETELREL 907
Cdd:pfam15921  265 HQDRIEQLISEHEVEIT------GLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLEsTVSQLRSELREA 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  908 NTQWDymcrqvyarkealkgglDKTVSLQKDLSEMHEWMTQAEEEYLERDFEY-KTPDELQTAVEEM-KRAKEEAQQKEA 985
Cdd:pfam15921  337 KRMYE-----------------DKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADLhKREKELSLEKEQ 399
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  986 KVKLLTESVNSVIAQAPpaaqeaLKKELDTLTTNYQWL------------------CTRLNGKCKTLEEVWACWHELLSY 1047
Cdd:pfam15921  400 NKRLWDRDTGNSITIDH------LRRELDDRNMEVQRLeallkamksecqgqmerqMAAIQGKNESLEKVSSLTAQLEST 473
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1048 LEKANKWLSEVEVKLKTTENISGGAEEIAEVLDSLENLMQHSEDNPNQIRilAQTLTDGGVMDELINEE--LETFNSRWR 1125
Cdd:pfam15921  474 KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR--SRVDLKLQELQHLKNEGdhLRNVQTECE 551
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1126 ELHEEAVRRQKLLE---QSIQS-------------AQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQkiQSD 1189
Cdd:pfam15921  552 ALKLQMAEKDKVIEilrQQIENmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR--VSD 629
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1190 LTSHEISL-----EEMKKHNQGKETAQRVLSQIDVAQKKLQDVSMKFRLFQKpaNFEQRLQESKMILDEVKMHLPAletk 1264
Cdd:pfam15921  630 LELEKVKLvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR--NFRNKSEEMETTTNKLKMQLKS---- 703
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1265 sveqevVQSQLNHCVNLYKSLsEVKSEVEMVIKTGRQivqkkqtenpkeldERVTALKLHYNELGAKVTERKQQLEKCLK 1344
Cdd:pfam15921  704 ------AQSELEQTRNTLKSM-EGSDGHAMKVAMGMQ--------------KQITAKRGQIDALQSKIQFLEEAMTNANK 762
                          730       740
                   ....*....|....*....|....*
gi 1953419023 1345 LSRKMRKEMNALTEWLAATDMELTK 1369
Cdd:pfam15921  763 EKHFLKEEKNKLSQELSTVATEKNK 787
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2241-2343 1.13e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.85  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2241 FNRAWTELTDWLSLLDRVIKSQRvMVGDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2320
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 1953419023 2321 ERIQSQWDEVQEHLQNRRQQLNE 2343
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
610-820 1.18e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.28  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  610 QLQQLEQMTTTAENWLK------TQPTTTSEPTAIKSQLKICKDEINRLSALQPQIERLKIQSIALKEKGQGpmflDADF 683
Cdd:cd00176      1 KLQQFLRDADELEAWLSekeellSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP----DAEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  684 V-----AFTNHFNQVFADVQAREKELQtifDSLPPMRYQETMSTILTWIQQSETKLSiPQVTVTEYDIMEQRLGELQALQ 758
Cdd:cd00176     77 IqerleELNQRWEELRELAEERRQRLE---EALDLQQFFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELE 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953419023  759 SSLQEQQNGLNYLSTTVKEMSKKAPLSDiSRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQM 820
Cdd:cd00176    153 EELEAHEPRLKSLNELAEELLEEGHPDA-DEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
350-1214 1.26e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  350 KEDAVNKIHTTgfkdqsevLSNLQKLAVLKTDLEKKKQTMDKLCSLNQDLLsALKNTVVAHKMEAWldnfAQRWDNLVQK 429
Cdd:TIGR02168  174 RKETERKLERT--------RENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELELALL----VLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  430 LEKSSAQISQAVT-----TTQPSLTQTTVMETVTMVTTREHiLVKHAQEELPPPPPQKKR---QIIVDSEIRKRLDVDIT 501
Cdd:TIGR02168  241 LEELQEELKEAEEeleelTAELQELEEKLEELRLEVSELEE-EIEELQKELYALANEISRleqQKQILRERLANLERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  502 ELHSWITRSEAVLQSPEFAIYRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLN 581
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  582 SRwiefCQLLSERLNWLEYQNNIitfyNQLQQLEQMTTTAENWLKTQPTTTSEPTAIKSQLKICKDE-INRLSALQPQIE 660
Cdd:TIGR02168  400 NE----IERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERlEEALEELREELE 471
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  661 RLKIQSIALKEKgqgpmfldadfvaftnhfnqvFADVQAREKELQTIFDSLppMRYQETMSTIltWIQQSETKLSIPQVT 740
Cdd:TIGR02168  472 EAEQALDAAERE---------------------LAQLQARLDSLERLQENL--EGFSEGVKAL--LKNQSGLSGILGVLS 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  741 vteyDIMEQRLGELQALQSSLQEqqnGLNYLSTTVKEMSKKA---------------PLSDISrkyQSEFEEIEGRWKKL 805
Cdd:TIGR02168  527 ----ELISVDEGYEAAIEAALGG---RLQAVVVENLNAAKKAiaflkqnelgrvtflPLDSIK---GTEIQGNDREILKN 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  806 SSQLVEHCQKLEEQMAKLRK--------------IQNHIKTLKK------WITEVDVFLKEEW-----PALGDSEILKRQ 860
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRKalsyllggvlvvddLDNALELAKKlrpgyrIVTLDGDLVRPGGvitggSAKTNSSILERR 676
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  861 --LKQCRllvNDIQTIQPSLNSVNEGAQKMKNEAEpefagRLETELRELNTQWDYMCRQVYARKEALKGGLDKTVSLQKD 938
Cdd:TIGR02168  677 reIEELE---EKIEELEEKIAELEKALAELRKELE-----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  939 LSEMHEWMTQAEEEYLERDfeyktpDELQTAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPaaqeaLKKELDTLTT 1018
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELE------ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-----LRAELTLLNE 817
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1019 NYQwlctrlngkcktleevwacwhellsylekankwlsevevklKTTENISGGAEEIAEVLDSLENLMQHSEDNPNQIRI 1098
Cdd:TIGR02168  818 EAA-----------------------------------------NLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1099 LAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKvdaAQ 1178
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL---EG 933
                          890       900       910
                   ....*....|....*....|....*....|....*..
gi 1953419023 1179 MPQEAQKIQSDLTS-HEISLEEMKKHNQGKETAQRVL 1214
Cdd:TIGR02168  934 LEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEA 970
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
484-1353 1.66e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.79  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  484 RQIIVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIYRKEGNFSDLKEkvnaiEREKAEKFRKLQDASRSAQ------ 557
Cdd:COG1196    158 RKLIEEAAGVSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLER-----QAEKAERYQELKAELRELElallla 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  558 ----------ALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSE-RLNWLEYQNNIITFYNQLQQLEQMTTTAENWLK 626
Cdd:COG1196    233 klkelrkeleELEEELSRLEEELEELQEELEEAEKEIEELKSELEElREELEELQEELLELKEEIEELEGEISLLRERLE 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  627 tqptttSEPTAIKSQLKICKDEINRLSALQPQIERLKIQSIAL--------KEKGQGPMFLDADFVAFTNHFNQVFADVQ 698
Cdd:COG1196    313 ------ELENELEELEERLEELKEKIEALKEELEERETLLEELeqllaeleEAKEELEEKLSALLEELEELFEALREELA 386
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  699 AREKELqtifdslppMRYQETMSTILTWIQQSETKLSipqvtvTEYDIMEQRLGELQALQSSLQEQQNGLNYLSTTVKE- 777
Cdd:COG1196    387 ELEAEL---------AEIRNELEELKREIESLEERLE------RLSERLEDLKEELKELEAELEELQTELEELNEELEEl 451
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  778 MSKKAPLSDISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQN---------------------HIKTLKKW 836
Cdd:COG1196    452 EEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGvravlealesglpgvygpvaeLIKVKEKY 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  837 ITEVDVFLKE--EWPALGDSEILKR---QLKQCR------LLVNDIQTIQPSLNSVNEGAQKMKNEAEpEFAGRLETELR 905
Cdd:COG1196    532 ETALEAALGNrlQAVVVENEEVAKKaieFLKENKagratfLPLDRIKPLRSLKSDAAPGFLGLASDLI-DFDPKYEPAVR 610
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  906 elntqwdYMCRQVY-------ARKEA-LKGGLDKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQTAVEEMKRAK 977
Cdd:COG1196    611 -------FVLGDTLvvddleqARRLArKLRIKYRIVTLDGDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQL 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  978 EEAQQKEAKVKLLTESVNSVIaqappaaqEALKKELDTLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLSE 1057
Cdd:COG1196    684 EKLEEELKSLKNELRSLEDLL--------EELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEE 755
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1058 VEVKLKTTEnisggaEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDggvmdelINEELETFNSRWRELHEEAVRRQKL 1137
Cdd:COG1196    756 LQERLEELE------EELESLEEALAKLKEEIEELEEKRQALQEELEE-------LEEELEEAERRLDALERELESLEQR 822
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1138 LEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYiADKVDAAQMpqEAQKIQSDLTSHEislEEMKKHNQGKETAQRvlsQI 1217
Cdd:COG1196    823 RERLEQEIEELEEEIEELEEKLDELEEELEEL-EKELEELKE--ELEELEAEKEELE---DELKELEEEKEELEE---EL 893
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1218 DVAQKKLQDVSmkfrlfQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEvvqsQLNHCVNLYKSLSEVKSEVEMvik 1297
Cdd:COG1196    894 RELESELAELK------EEIEKLRERLEELEAKLERLEVELPELEEELEEEY----EDTLETELEREIERLEEEIEA--- 960
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023 1298 tgRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEM 1353
Cdd:COG1196    961 --LGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKET 1014
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
969-1827 1.90e-04

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: 47.66  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  969 AVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPAAQEALKKELDTLTTNYQWLCTRLngkcktlEEVWACWHELLSYL 1048
Cdd:pfam02463  163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL-------EEEYLLYLDYLKLN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1049 EKANKWLSEVEVKLKTTENISGGAEEIAEvldslENLMQHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRwRELH 1128
Cdd:pfam02463  236 EERIDLLQELLRDEQEEIESSKQEIEKEE-----EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRK 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1129 EEAVRRQKLLEQSIQSAQEIEKslhLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKhnqgKE 1208
Cdd:pfam02463  310 VDDEEKLKESEKEKKKAEKELK---KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK----LE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1209 TAQRVLSQIDVAQKKLQDVSMKfrlfqKPANFEQRLQESKMILDEVKmHLPALETKSVEQEVVQSQLNHcvnlyksLSEV 1288
Cdd:pfam02463  383 SERLSSAAKLKEEELELKSEEE-----KEAQLLLELARQLEDLLKEE-KKEELEILEEEEESIELKQGK-------LTEE 449
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1289 KSEVEMVIKT-GRQIVQKKQTENPKELdervtalklhynelgakvtERKQQLEKCLKLSRKMRKEMNALTEWLAATDMEL 1367
Cdd:pfam02463  450 KEELEKQELKlLKDELELKKSEDLLKE-------------------TQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1368 TKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEALKTVLGKKEmLVEDKLSLLNSNWIAVTSRAEEWLNLL 1447
Cdd:pfam02463  511 VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE-RQKLVRALTELPLGARKLRLLIPKLKL 589
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1448 LEYQKHMENFDQNVDYITNWIIQADALLDESEKKKPQQKEDILKRLKAEMNDIRpkVDSTRDQAANLMANRGDHCRKVVE 1527
Cdd:pfam02463  590 PLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA--KESGLRKGVSLEEGLAEKSEVKAS 667
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1528 PKISELNHRFAAISHRIKTGKASIPLKELEQFNSD--IQKLLEPLEAEIQQGVNLKEEDFNKDMSEDNEGTVKELLQRGD 1605
Cdd:pfam02463  668 LSELTKELLEIQELQEKAESELAKEEILRRQLEIKkkEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE 747
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1606 NLQ--QRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRD-- 1681
Cdd:pfam02463  748 EEEeeEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEqe 827
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1682 -ERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEpTQIQLSKRWREIESKFAQFRRLNFAQ--IHTVHEESVVAM 1758
Cdd:pfam02463  828 eKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE-ELLQELLLKEEELEEQKLKDELESKEekEKEEKKELEEES 906
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953419023 1759 TEDMPLE--ISYVPSTYLTEITHVSQALSEVEELLNAPDLCAQDFEDLFKQEESLKNIKDSLQQISGRIDI 1827
Cdd:pfam02463  907 QKLNLLEekENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNL 977
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1117-1717 2.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1117 LETFNSRWRELHE---EAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAayiadkvdaaQMPQEAQKIQSDLTSH 1193
Cdd:PRK03918   157 LDDYENAYKNLGEvikEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN----------EISSELPELREELEKL 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1194 EISLEEMKKHNQGKETAQRVLSQIDVAQKKLqdvsmkfrlfqkpanfEQRLQESKMILDEVKMHLPALETKsveqevvqs 1273
Cdd:PRK03918   227 EKEVKELEELKEEIEELEKELESLEGSKRKL----------------EEKIRELEERIEELKKEIEELEEK--------- 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1274 qlnhcVNLYKSLSEVKSEVEMVIKTGRQIVQKKQteNPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEM 1353
Cdd:PRK03918   282 -----VKELKELKEKAEEYIKLSEFYEEYLDELR--EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1354 NALTEWLAATDMELTKRSAVEGMPSNLdsevawgkaTQKEIEKQKVHLKSV----TEVGEALKTVLGKKEMLvEDKLSLL 1429
Cdd:PRK03918   355 EELEERHELYEEAKAKKEELERLKKRL---------TGLTPEKLEKELEELekakEEIEEEISKITARIGEL-KKEIKEL 424
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1430 NSNWIAVTS------------RAEEWLNLLLEYQKHMENFDQNVdyitnwiiqadALLDESEKKKPQQKEDILKRLKAEM 1497
Cdd:PRK03918   425 KKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKEL-----------KEIEEKERKLRKELRELEKVLKKES 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1498 NDIRPKvdSTRDQAANLMANRGDHCRKVVEPKISE---LNHRFAAISHRIKTGKASipLKELEQFNSDIQKLLEPLEAEI 1574
Cdd:PRK03918   494 ELIKLK--ELAEQLKELEEKLKKYNLEELEKKAEEyekLKEKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE 569
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1575 QQGVNLKEEDFNKDMS--EDNEGTVKEL---------LQRGDNLQQRITDERKREEIKIKQQL--LQTKHNALKDLRSqr 1641
Cdd:PRK03918   570 EELAELLKELEELGFEsvEELEERLKELepfyneyleLKDAEKELEREEKELKKLEEELDKAFeeLAETEKRLEELRK-- 647
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953419023 1642 RKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEprDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMA 1717
Cdd:PRK03918   648 ELEELEKKYSEEEYEELREEYLELSRELAGLRAELEE--LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
753-1358 2.78e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.02  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  753 ELQALQSSLQEQQNGLNYLSTTVKEMSKKA-PLSDISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQNHIK 831
Cdd:COG1196    254 ELEELQEELEEAEKEIEELKSELEELREELeELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIE 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  832 TLKKWITEVDVFLKEewpalgdseiLKRQLKQCRLLVNDIQTIQPSL---------NSVNEGAQKMKNEAEPEF-AGRLE 901
Cdd:COG1196    334 ALKEELEERETLLEE----------LEQLLAELEEAKEELEEKLSALleeleelfeALREELAELEAELAEIRNeLEELK 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  902 TELRELNTQWDYMCRQVYARKEALKGGLDKTVSLQKDLSEMHEWMTQAEEEYLE-RDFEYKTPDELQTAVEEMKRAKEEA 980
Cdd:COG1196    404 REIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEElRDRLKELERELAELQEELQRLEKEL 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  981 QQKEAKvkLLTESVNSVIAQAPPAAQEALKKEL--------DTLTTNYQW-------LCTRLNGKCKTLEEVWAcwhELL 1045
Cdd:COG1196    484 SSLEAR--LDRLEAEQRASQGVRAVLEALESGLpgvygpvaELIKVKEKYetaleaaLGNRLQAVVVENEEVAK---KAI 558
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1046 SYLEKAN------KWLSEVEVKLKTTENISGGAEEIAE---------------------VLDSLENLMQHSEDNPNQIRI 1098
Cdd:COG1196    559 EFLKENKagratfLPLDRIKPLRSLKSDAAPGFLGLASdlidfdpkyepavrfvlgdtlVVDDLEQARRLARKLRIKYRI 638
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1099 LA---QTLTDGGVM--DELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLaayiadk 1173
Cdd:COG1196    639 VTldgDLVEPSGSItgGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQL------- 711
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1174 vDAAQMpqEAQKIQSDLTSHEISLEEMKKH-NQGKETAQRVLSQIDVAQKKLQDVSMK-FRLFQKPANFEQRLQESKMIL 1251
Cdd:COG1196    712 -EELER--QLEELKRELAALEEELEQLQSRlEELEEELEELEEELEELQERLEELEEElESLEEALAKLKEEIEELEEKR 788
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1252 DEVKMHLPALETKSVEQEVVQSQLnhcvnlyksLSEVKSEVEMVIKTGRQIVQKKqtENPKELDERVTALKLHYNELGAK 1331
Cdd:COG1196    789 QALQEELEELEEELEEAERRLDAL---------ERELESLEQRRERLEQEIEELE--EEIEELEEKLDELEEELEELEKE 857
                          650       660
                   ....*....|....*....|....*..
gi 1953419023 1332 VTERKQQLEKCLKLSRKMRKEMNALTE 1358
Cdd:COG1196    858 LEELKEELEELEAEKEELEDELKELEE 884
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2059-2813 3.13e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2059 EEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDLGQLEEQLNHLLLWLSPIRNQLEIYNQPNQTGPFDIKEIEVAV 2138
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2139 QAKQPDVEGILSKGQHLYKE----KPATQPAKRKLEDLSSDWKVVTQLLQELRAKQPGPAPGLTTVRAPPSQTVTLVTQP 2214
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2215 AVTKETAISKLEmpsslllevpalaDFNRAWTELTDWLSLLDRVIKSQRV--MVGDLEDINEMIIKQKATLQDLEQRRPQ 2292
Cdd:TIGR02168  399 NNEIERLEARLE-------------RLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEE 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2293 LEELITAAQNLKNKTSNQEARtiITDRIERIQSqwdevqehLQNRRQQLNEMLKdstQWLEAKEEAEQVLGQARAKL--- 2369
Cdd:TIGR02168  466 LREELEEAEQALDAAERELAQ--LQARLDSLER--------LQENLEGFSEGVK---ALLKNQSGLSGILGVLSELIsvd 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2370 ESWKEAPYTV--DAIQKKITETKQLAKDLRQWQINVDV--ANDLALKLLRDYSADDTRKVHMITENINASWASIHKRLSE 2445
Cdd:TIGR02168  533 EGYEAAIEAAlgGRLQAVVVENLNAAKKAIAFLKQNELgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2446 reaaleethrllqQFPLDLEKFLAWLTEAETTANVLQDA---THKERLL------------------EDSKGVRELMKQW 2504
Cdd:TIGR02168  613 -------------KLRKALSYLLGGVLVVDDLDNALELAkklRPGYRIVtldgdlvrpggvitggsaKTNSSILERRREI 679
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2505 QDLQGEIEAHTDIYHNLDENGQKVLRSL-EGSDDAALLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQEL 2583
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2584 LVWLQLKDDELsrqapiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLEtvRIFLTEQPLEGLEKLYQEPRE-----LP 2658
Cdd:TIGR02168  760 EAEIEELEERL-------------EEAEEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEeaanlRE 824
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2659 PEERAQNVTRLLRKQAEEVNTQWEKLNVHSADWQRKIDEALERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQ 2738
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2739 DHLEKVKALRGEITPLKENvsyVNDLARQLTTLGIQLspynLNTLEDLNTRWKL-LQVA-------------IEDRIRQL 2804
Cdd:TIGR02168  905 ELESKRSELRRELEELREK---LAQLELRLEGLEVRI----DNLQERLSEEYSLtLEEAealenkieddeeeARRRLKRL 977

                   ....*....
gi 1953419023 2805 HEAHRDFGP 2813
Cdd:TIGR02168  978 ENKIKELGP 986
SPEC smart00150
Spectrin repeats;
1269-1340 3.28e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 3.28e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953419023  1269 EVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKkQTENPKELDERVTALKLHYNELGAKVTERKQQLE 1340
Cdd:smart00150   31 ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
3079-3125 3.63e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.52  E-value: 3.63e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1953419023 3079 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRvakgHKMHYPMVEY 3125
Cdd:cd02339      3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2252-2366 4.07e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 4.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2252 LSLLDRVIKSQRVMVG-DLEDINEMIikqkatlQDLEQRRPQLEELITAAQNLKnktsnQEARTIITDRIERIQSQWDEV 2330
Cdd:PRK00409   497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALL-----KEAEKLKEELEEKKEKLQEEE 564
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1953419023 2331 QEHLQNRRQQLNEMLKdstqwlEAKEEAEQVLGQAR 2366
Cdd:PRK00409   565 DKLLEEAEKEAQQAIK------EAKKEADEIIKELR 594
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
751-1617 5.06e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.25  E-value: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  751 LGELQALQSSLQEQQNGLNYLSTTVKEMSKKapLSDISRKYQ---SEFEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKIQ 827
Cdd:COG1196    231 LAKLKELRKELEELEEELSRLEEELEELQEE--LEEAEKEIEelkSELEELREELEELQEELLELKEEIEELEGEISLLR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  828 NHIKTLKKWITEvdvflkeewpALGDSEILKRQLKQCRLLVNDIQTIQPSLNSVNEGAQKMKNEAEPEFAGRLETElrel 907
Cdd:COG1196    309 ERLEELENELEE----------LEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEEL---- 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  908 ntqwdymcrqvYARKEALKGGLDKTVSLQKDLsemhewmtQAEEEYLERDFEYKTpDELQTAVEEMKRAKEEAQQKEAKV 987
Cdd:COG1196    375 -----------EELFEALREELAELEAELAEI--------RNELEELKREIESLE-ERLERLSERLEDLKEELKELEAEL 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  988 KLLTEsvnsviaqappaAQEALKKELDTLTTNYQWLctrlngkCKTLEEVWACWHELLSYLEKANKWLSEVEVKLKTTEN 1067
Cdd:COG1196    435 EELQT------------ELEELNEELEELEEQLEEL-------RDRLKELERELAELQEELQRLEKELSSLEARLDRLEA 495
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1068 ISGGAEEIAEVLDSLENLM--------QHSEDNPNQIRILAQTLtdGGVMDELINEELETfnsrwrelHEEAVrrQKLLE 1139
Cdd:COG1196    496 EQRASQGVRAVLEALESGLpgvygpvaELIKVKEKYETALEAAL--GNRLQAVVVENEEV--------AKKAI--EFLKE 563
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1140 QSIQSAQEIEksLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEI---SLEEMKKHNQGKETAQRVLS- 1215
Cdd:COG1196    564 NKAGRATFLP--LDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTLvvdDLEQARRLARKLRIKYRIVTl 641
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1216 QIDVAQKKlqdVSMKfRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKSLSEVKSEVEMV 1295
Cdd:COG1196    642 DGDLVEPS---GSIT-GGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELR---SLEDLLEELRRQLEEL 714
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1296 iktGRQIVQKKQTENpkELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNALTEWLAATDMELtkrsavEG 1375
Cdd:COG1196    715 ---ERQLEELKRELA--ALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEI------EE 783
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1376 MPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEALKTV----------LGKKEMLVEDKLSLLNSNWIAVTSRAEEWLN 1445
Cdd:COG1196    784 LEEKRQALQEELEELEEELEEAERRLDALERELESLEQRrerleqeieeLEEEIEELEEKLDELEEELEELEKELEELKE 863
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1446 LLLEYQKHMENFDQNVDYITNWIIQADALLDESEKKKPQQKEDIlKRLKAEMNDIRPKVDSTRDQAANLmanrgdhcrkv 1525
Cdd:COG1196    864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEI-EKLRERLEELEAKLERLEVELPEL----------- 931
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1526 vEPKISELNHRFAAISHRIKTGKASIPLKELEQFNsdiqkllepLEAEIQQGVNLKEEDFNKDMSEDNEGTVKELLQRGD 1605
Cdd:COG1196    932 -EEELEEEYEDTLETELEREIERLEEEIEALGPVN---------LRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIE 1001
                          890
                   ....*....|..
gi 1953419023 1606 NLQQRITDERKR 1617
Cdd:COG1196   1002 ELDKEKRERFKE 1013
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
747-1256 5.10e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 45.91  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  747 MEQRLGELQALQSSLQEQQNglnylSTTVKEMSKKAPLSDISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMAKLRKI 826
Cdd:COG0419    334 LEEKLEKLESELEELAEEKN-----ELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEI 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  827 QNHIKTLKKWITEVDVFLKEEWPALGDSEILKRQLKQCRLLVNDIQTIQ---PSLNsvnegaQKMKNEAEPEFAGRLETE 903
Cdd:COG0419    409 QEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGekcPVCG------QELPEEHEKELLELYELE 482
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  904 LRELNTQWDYMCRQVYARKEALKggLDKTVSLQKDLSEMHEWMTQAEEEYLERDFEyktpdELQTAVEEMKRAKEEAQQK 983
Cdd:COG0419    483 LEELEEELSREKEEAELREEIEE--LEKELRELEEELIELLELEEALKEELEEKLE-----KLENLLEELEELKEKLQLQ 555
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  984 EAKVKLltesvnsviaqappaaqEALKKELDTLTTNYQwlctRLNGKCKTLEEvwacwhellsyLEKANKWLSEVEVKLK 1063
Cdd:COG0419    556 QLKEEL-----------------RQLEDRLQELKELLE----ELRLLRTRKEE-----------LEELRERLKELKKKLK 603
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1064 ttenisggaeEIAEVLDSLENLMQ--HSEDNPNQIRILAQTLTDggvMDELINEELETFNSRWRELHEEAVRRQKLLEQS 1141
Cdd:COG0419    604 ----------ELEERLSQLEELLQslELSEAENELEEAEEELES---ELEKLNLQAELEELLQAALEELEEKVEELEAEI 670
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1142 IQSAQEIEKSLHLIQESLssidkqlaayiadkvDAAQMPQEAQKIQSDLtshEISLEEMKKHNQGKETAQRVLSQIDVAQ 1221
Cdd:COG0419    671 RRELQRIENEEQLEEKLE---------------ELEQLEEELEQLREEL---EELLKKLGEIEQLIEELESRKAELEELK 732
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1953419023 1222 KKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM 1256
Cdd:COG0419    733 KELEKLEKALELLEELREKLGKAGLRADILRNLLA 767
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
748-1246 5.40e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  748 EQRLGELQALQSSLQEQQNGLNYLSTTVKEMSKkapLSDISRKYQSEFEEIEGRWKKLSSQ---LVEHCQKLEEQMAKLR 824
Cdd:PRK03918   265 EERIEELKKEIEELEEKVKELKELKEKAEEYIK---LSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  825 KIQNHIKTLKKWITEvdvfLKEEWPALGDSEILKRQLKQC--RLLVNDIQTIQPSLnsvnEGAQKMKNEAEPEFA----- 897
Cdd:PRK03918   342 ELKKKLKELEKRLEE----LEERHELYEEAKAKKEELERLkkRLTGLTPEKLEKEL----EELEKAKEEIEEEISkitar 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  898 -GRLETELRELNTQWdymcrqvyarkEALKGGLDKTVSLQKDLSEMH--EWMTQAEEEYLERDFEYKTPDELQTAVEEMK 974
Cdd:PRK03918   414 iGELKKEIKELKKAI-----------EELKKAKGKCPVCGRELTEEHrkELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  975 RAKEEAQQKEAKVKLLTESVNSVIAQAPPAAQEALkKELDTLTTNYQWLCTRLN---GKCKTLEEVwacwhelLSYLEKA 1051
Cdd:PRK03918   483 RELEKVLKKESELIKLKELAEQLKELEEKLKKYNL-EELEKKAEEYEKLKEKLIklkGEIKSLKKE-------LEKLEEL 554
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1052 NKWLSEVEVKLKTTEnisggaEEIAEVLDSLENLMQHSEDNpnqirilaqtltdggvmDELINEELETFNSRWREL---H 1128
Cdd:PRK03918   555 KKKLAELEKKLDELE------EELAELLKELEELGFESVEE-----------------LEERLKELEPFYNEYLELkdaE 611
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1129 EEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAA--YIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHnqg 1206
Cdd:PRK03918   612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEleKKYSEEEYEELREEYLELSRELAGLRAELEELEKR--- 688
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1953419023 1207 KETAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQE 1246
Cdd:PRK03918   689 REEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE 728
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
3079-3124 5.82e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 40.27  E-value: 5.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953419023 3079 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVE 3124
Cdd:cd02345      3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
1050-1431 6.11e-04

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 45.62  E-value: 6.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1050 KANKWLSEVEVKLKTTEnisggaEEIAEVLDSLENLMQHSEDNPNQIRILaqtltdggvmdelineeletfnsrwRELHE 1129
Cdd:pfam06160   83 KAKKALDEIEELLDDIE------EDIKQILEELDELLESEEKNREEVEEL-------------------------KDKYR 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1130 EAvrRQKLLEQSIQSAQEIEKslhlIQESLSSIDKQLAAYiaDKVDAAQMPQEAQKIQSDLTSHEISLEE-MKKHNQGKE 1208
Cdd:pfam06160  132 EL--RKTLLANRFSYGPAIDE----LEKQLAEIEEEFSQF--EELTESGDYLEAREVLEKLEEETDALEElMEDIPPLYE 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1209 TAQRV----LSQIDVAQKKLQDvsMKFRLfqKPANFEQRLQESKMILDEVKMHLPALETKSVEQEV--VQSQLNHcvnLY 1282
Cdd:pfam06160  204 ELKTElpdqLEELKEGYREMEE--EGYAL--EHLNVDKEIQQLEEQLEENLALLENLELDEAEEALeeIEERIDQ---LY 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1283 KSL-SEVKS--EVEMVIKTGRQIVQKKQTENpKELDERVTALKLHYnELGAKVTERKQQLEkclklsrkmrKEMNALTEW 1359
Cdd:pfam06160  277 DLLeKEVDAkkYVEKNLPEIEDYLEHAEEQN-KELKEELERVQQSY-TLNENELERVRGLE----------KQLEELEKR 344
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953419023 1360 LAATDMELTKRSAVEgmpSNLDSEVAWGKATQKEIEKQKVHLKsvtevgEALKTvLGKKEMLVEDKLSLLNS 1431
Cdd:pfam06160  345 YDEIVERLEEKEVAY---SELQEELEEILEQLEEIEEEQEEFK------ESLQS-LRKDELEAREKLDEFKL 406
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1125-1995 9.04e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.09  E-value: 9.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1125 RELHEEA-------VRRQKLlEQSIQSAQEIEKSLHLIQESLSSIDKQLAayiadkvDAAQMPQEAQKIQSDLTSHEISL 1197
Cdd:COG1196    158 RKLIEEAagvskykERKEEA-ERKLERTEENLERLEDLLEELEKQLEKLE-------RQAEKAERYQELKAELRELELAL 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1198 --EEMKKHNQGKETAQRVLSQIdvaQKKLQDVSMKFRlfqkpaNFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQL 1275
Cdd:COG1196    230 llAKLKELRKELEELEEELSRL---EEELEELQEELE------EAEKEIEELKSELEELREELEELQEELLELKEEIEEL 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1276 NHCVNLYKSLSEvKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKmrkemna 1355
Cdd:COG1196    301 EGEISLLRERLE-ELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLE------- 372
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1356 ltewlaatdmeltkrsAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIA 1435
Cdd:COG1196    373 ----------------ELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEE 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1436 VTSRAEEWLNLLLEYQKHMENFDQNVDYITNWIIQADALLD--ESEKKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAAN 1513
Cdd:COG1196    437 LQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQrlEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1514 LMANRGDHCRkvVEPKISEL------NHRFAAISHRIKTGKASIplKELEQFNSDIQKLLePLEaEIQQGVNLKEEDFNk 1587
Cdd:COG1196    517 VYGPVAELIK--VKEKYETAleaalgNRLQAVVVENEEVAKKAI--EFLKENKAGRATFL-PLD-RIKPLRSLKSDAAP- 589
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1588 dmseDNEGTVKELLQRGDNLQ-------------QRITDERKREEIKIKQQLLQTKHNALKDLR------SQRRKKALEI 1648
Cdd:COG1196    590 ----GFLGLASDLIDFDPKYEpavrfvlgdtlvvDDLEQARRLARKLRIKYRIVTLDGDLVEPSgsitggSRNKRSSLAQ 665
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1649 SHQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQlsKR 1728
Cdd:COG1196    666 KRELKELEEELAELEAQLEKLEEELKSL-----KNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQ--SR 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1729 WREIESKFAQFRR-LNFAQIHTVHEESVVAMTEDMPLEIsyvpSTYLTEITHVSQALSEV-----EELLNAPDLCAQDFE 1802
Cdd:COG1196    739 LEELEEELEELEEeLEELQERLEELEEELESLEEALAKL----KEEIEELEEKRQALQEEleeleEELEEAERRLDALER 814
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1803 DLFKQEESLKNIKDSLQQISGRIDIIHNKKTAALHsatpaERAKLQEALSRLDFQWERVNNMYKDRQGRFDRSVEKWRRF 1882
Cdd:COG1196    815 ELESLEQRRERLEQEIEELEEEIEELEEKLDELEE-----ELEELEKELEELKEELEELEAEKEELEDELKELEEEKEEL 889
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1883 hydMKILNQWLTEAEQFLKKTQIPENwehaKYKWYLKELQDGIGQRQSVVRVLNATGEEIIQQSSKTDASILQEK---LG 1959
Cdd:COG1196    890 ---EEELRELESELAELKEEIEKLRE----RLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEieaLG 962
                          890       900       910
                   ....*....|....*....|....*....|....*.
gi 1953419023 1960 SLNLRwqeVCKQLAERKKRLEEQKNILSEFQRDVNE 1995
Cdd:COG1196    963 PVNLR---AIEEYEEVEERYEELKSQREDLEEAKEK 995
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
748-1521 9.34e-04

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: 45.35  E-value: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  748 EQRLGELQALQSSLQEQQNG---LNYLSTTVKEMSKKAPLSDISRKYQSEFEEIEGRWK-KLSSQLVEHCQKLEEQMAKL 823
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELlKLERRKVDDEEKLKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  824 RKIQNHIKTLKKWITEVDVFLKEEWPALGDSEILKRQLKQCRLlvndiqtiqpsLNSVNEGAQKMKNEAEPEFAGRLETE 903
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE-----------KLEQLEEELLAKKKLESERLSSAAKL 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  904 LRELNTQWDYMCRQVYARKEALKGGLDKTVSLQKDLSEMHEwmtqAEEEYLERDFEYKTPDELQTAVEEMKRAKEEAQQK 983
Cdd:pfam02463  393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE----EEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  984 EAKVKLLTESVNSVIAQAPPAAQEALKKELDTLTTNYQWLCTRLNGKCKTLEEVwacwhELLSYLEKANKWLSEVEVKLK 1063
Cdd:pfam02463  469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGG-----RIISAHGRLGDLGVAVENYKV 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1064 TTENISGGAEEIAEVLDSLENLMQHSEDNPNQIRILAQTLTDGGVMDELINEELET--------FNSRWRELHEEAVRRQ 1135
Cdd:pfam02463  544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIdpilnlaqLDKATLEADEDDKRAK 623
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1136 KLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKV-------DAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKE 1208
Cdd:pfam02463  624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSevkaslsELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1209 TAQRV-LSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKmiLDEVKMHLPALETKSVEQEVVQSQLnhcvnlyksLSE 1287
Cdd:pfam02463  704 KEQREkEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK--IDEEEEEEEKSRLKKEEKEEEKSEL---------SLK 772
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1288 VKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKlhynelgAKVTERKQQLEKCLKLSRKMRKEMNALTEWLAATDMEL 1367
Cdd:pfam02463  773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE-------EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1368 TKRSAvegmpSNLDSEVAWGKATQKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLNLL 1447
Cdd:pfam02463  846 QKLEK-----LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIE 920
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953419023 1448 LEYQKHMENFDQNVDYITNWIIQADALLDESEKKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLMANRGDH 1521
Cdd:pfam02463  921 ERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1552-2107 9.69e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 45.14  E-value: 9.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1552 PLKELEQFNSDIQKLLEPLEaEIQQGVNLKEEDFNKDMSEdnEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTK 1630
Cdd:COG0419    275 ELRELERLLEELEEKIERLE-ELEREIEELEEELEGLRAL--LEELEELLEKLKSLEERLEKlEEKLEKLESELEELAEE 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1631 HNALKDLRsQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEgls 1710
Cdd:COG0419    352 KNELAKLL-EERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELE--- 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1711 edgaamaveptqiQLSKRWREIESKFAQFRRLnfaqihtvheesvvamtedmpleisyvpstylteithvSQALSEVEEL 1790
Cdd:COG0419    428 -------------ELEEEIKKLEEQINQLESK--------------------------------------ELMIAELAGA 456
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1791 LNAPDLCAQDFEDLfKQEESLKNIKDSLQQISGRIDIIHNKKTAAlhsatpAERAKLQEALSRLDFQWERVNNMYKDRQG 1870
Cdd:COG0419    457 GEKCPVCGQELPEE-HEKELLELYELELEELEEELSREKEEAELR------EEIEELEKELRELEEELIELLELEEALKE 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1871 RFDRSVEKWRRF--HYDMKILNQWLTEAEQFLKK-----TQIPENWEHAKYKWYLKELQDGIGQRQsvvRVLNATGEEII 1943
Cdd:COG0419    530 ELEEKLEKLENLleELEELKEKLQLQQLKEELRQledrlQELKELLEELRLLRTRKEELEELRERL---KELKKKLKELE 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1944 QQSSKTDASILQEKLGSLNLRWQEVCKQLAERKKRLEEQKNILSEFQRDVNEFVLWLEE-ADNVANIPLEPGNEQQLKEK 2022
Cdd:COG0419    607 ERLSQLEELLQSLELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVEElEAEIRRELQRIENEEQLEEK 686
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2023 LEQVKLLAEELPLRQ----GILKQLNETGGTV--LVSAPLSPEEQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDL 2096
Cdd:COG0419    687 LEELEQLEEELEQLReeleELLKKLGEIEQLIeeLESRKAELEELKKELEKLEKALELLEELREKLGKAGLRADILRNLL 766
                          570
                   ....*....|.
gi 1953419023 2097 GQLEEQLNHLL 2107
Cdd:COG0419    767 AQIEAEANEIL 777
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
728-1223 9.77e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 45.14  E-value: 9.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  728 QQSETKLSIPQVTVTEYDIMEQRLGELQALQSSLQEQQNGLNYLSTTVKEMSKKAPLSDISRKYQSEFEEIEGRWKKLSS 807
Cdd:COG0419    250 RLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEE 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  808 QLVEHCQKLEEQMAKLRKIQNHIKTLKKWITEVDVFLKEEWPALgDSEILKRQLKQCRLLVNDIQ--TIQPSLNSVNEGA 885
Cdd:COG0419    330 RLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEEL-EKELEKALERLKQLEEAIQElkEELAELSAALEEI 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  886 QKMKNEAEPEFAGrLETELRELNTQWDYM------CRQVYARKEALKGGLDK-----------------------TVSLQ 936
Cdd:COG0419    409 QEELEELEKELEE-LERELEELEEEIKKLeeqinqLESKELMIAELAGAGEKcpvcgqelpeehekellelyeleLEELE 487
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  937 KDLSEmHEWMTQAEEEYLERDFEYKTPDELQT--------AVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPAAQEA 1008
Cdd:COG0419    488 EELSR-EKEEAELREEIEELEKELRELEEELIelleleeaLKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLED 566
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1009 LKKELDTLTTNYqwlcTRLNGKCKTLEEVWACWHELLSYLEKANKWLSEVEVKLKTTEnISGGAEEIAEVLDSLENLMQH 1088
Cdd:COG0419    567 RLQELKELLEEL----RLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLE-LSEAENELEEAEEELESELEK 641
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1089 SEDNPNQIRILAQTLtdggvmdELINEELETFNSRWRELHEEAVRRQKLLEQSiQSAQEIEKSLHLIQESLSSIDKQLAA 1168
Cdd:COG0419    642 LNLQAELEELLQAAL-------EELEEKVEELEAEIRRELQRIENEEQLEEKL-EELEQLEEELEQLREELEELLKKLGE 713
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953419023 1169 YIadkvdaaqmpQEAQKIQSDLTSHEISLEEMKKHNQGKETAQRVLSQIDVAQKK 1223
Cdd:COG0419    714 IE----------QLIEELESRKAELEELKKELEKLEKALELLEELREKLGKAGLR 758
SPEC smart00150
Spectrin repeats;
2339-2451 1.21e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.78  E-value: 1.21e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2339 QQLNEMLKDSTQWLEAKEeaeqvlgqaraKLESWKEAPYTVDAIQKKITETKQLAKDLRQWQINVDVANDLALKLLRDyS 2418
Cdd:smart00150    1 QQFLRDADELEAWLEEKE-----------QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-G 68
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1953419023  2419 ADDTRKVHMITENINASWASIHKRLSEREAALE 2451
Cdd:smart00150   69 HPDAEEIEERLEELNERWEELKELAEERRQKLE 101
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1041-1707 1.34e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1041 WHELLSYLEKANKWLSEVEVKLKTTENisgGAEEIAEVLDSLENLMQHSEDNPNQIRI-LAQTLTDGgvmDELINEELET 1119
Cdd:pfam05483   80 YSKLYKEAEKIKKWKVSIEAELKQKEN---KLQENRKIIEAQRKAIQELQFENEKVSLkLEEEIQEN---KDLIKENNAT 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1120 fnSRWRELHEEAVRRQKllEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQ-KIQSDLTSHEISLE 1198
Cdd:pfam05483  154 --RHLCNLLKETCARSA--EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEE 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1199 EMKKHNQGKET-AQRVLSQIDVAQKKLQDVSmkFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNH 1277
Cdd:pfam05483  230 EYKKEINDKEKqVSLLLIQITEKENKMKDLT--FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1278 CVNLYKSLSEvksEVEMVIKTGRQIVQKKQTENpKELDERVTALKLHYNELGAKVTerkqQLEKCLKlSRKMRKEMNAlt 1357
Cdd:pfam05483  308 SMSTQKALEE---DLQIATKTICQLTEEKEAQM-EELNKAKAAHSFVVTEFEATTC----SLEELLR-TEQQRLEKNE-- 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1358 EWLAATDMELTKRSavegmpSNLDSEVAWGKATQKEIEKqkvhlksvtevgeaLKTVLGKKEMLVEDKlSLLNSNWIAVT 1437
Cdd:pfam05483  377 DQLKIITMELQKKS------SELEEMTKFKNNKEVELEE--------------LKKILAEDEKLLDEK-KQFEKIAEELK 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1438 SRAEEWLNLLLEYQKHMENFDQNVDYITNwiiqadalldeSEKKKPQQKEDILKRLKAEmndirpKVDSTRDQAanlman 1517
Cdd:pfam05483  436 GKEQELIFLLQAREKEIHDLEIQLTAIKT-----------SEEHYLKEVEDLKTELEKE------KLKNIELTA------ 492
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1518 rgdHCRKVvepkiselnhrfaAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkdMSEDNEGTV 1597
Cdd:pfam05483  493 ---HCDKL-------------LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN--LRDELESVR 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1598 KELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLP 1677
Cdd:pfam05483  555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
                          650       660       670
                   ....*....|....*....|....*....|
gi 1953419023 1678 EPRDERKIKEIDRELQKKKEELNAVRRQAE 1707
Cdd:pfam05483  635 EIKVNKLELELASAKQKFEEIIDNYQKEIE 664
SPEC smart00150
Spectrin repeats;
2575-2696 1.47e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.39  E-value: 1.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  2575 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 2654
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1953419023  2655 relppeeraqnvtrlLRKQAEEVNTQWEKLNVHSADWQRKID 2696
Cdd:smart00150   75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
PRK01156 PRK01156
chromosome segregation protein; Provisional
1113-1623 1.87e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1113 INEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEIEKSLHLIQESLSSIDKQLAAYIADKVDAAQMPQEAQKIQSDLTS 1192
Cdd:PRK01156   244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1193 HEIS---LEEMKKHNQGKETAQRVLSQIDVAQKKLQDVSMKFRLFQKpaNFEQ----RLQESKMILDEVKMHLPALETKS 1265
Cdd:PRK01156   324 YHAIikkLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK--SIESlkkkIEEYSKNIERMSAFISEILKIQE 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1266 VEQEVVQSQLNHcvnLYKSLSEVKSEVEMVIKTGRQIVQKKQ--TENPKEL--------------DERVTALKLHYNELG 1329
Cdd:PRK01156   402 IDPDAIKKELNE---INVKLQDISSKVSSLNQRIRALRENLDelSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKK 478
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1330 AKVTERKQQLEKCLKLSRKMRKEMNALTEWLAATDMELTKrsavegmpsNLDSEVAWGKATQKEIEKQKVHLKSVTEVGE 1409
Cdd:PRK01156   479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSI---------NEYNKIESARADLEDIKIKINELKDKHDKYE 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1410 ALKTVLgkKEMLVEDklsllnsnwiaVTSRAEEWLNLLLEYQK-HMENFDQNVDYITNWIIQADALLDESEKKKPQQK-- 1486
Cdd:PRK01156   550 EIKNRY--KSLKLED-----------LDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsy 616
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1487 -EDILKRLKAEMNDIRPKVDSTRDQAANLMANRGdhcrkvvepKISELNHRFAAISHRIKTgkasipLKELEQFNSDIQK 1565
Cdd:PRK01156   617 iDKSIREIENEANNLNNKYNEIQENKILIEKLRG---------KIDNYKKQIAEIDSIIPD------LKEITSRINDIED 681
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953419023 1566 LLEPLEAEIQqgvnlkeeDFNKDMSEdNEGTVKELLQRGDNLQQRITDERKREEIKIK 1623
Cdd:PRK01156   682 NLKKSRKALD--------DAKANRAR-LESTIEILRTRINELSDRINDINETLESMKK 730
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
469-840 2.13e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.93  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  469 KHAQEELPPPPPQKKRQIIVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIYRKEGNFSDLKEKVNAIEREKAEKFRK 548
Cdd:COG1196    659 KRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSR 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  549 LQDASRSAQALVEQMVNegvNADSIKQASEQLNSrwiefcqlLSERLNWLE-YQNNIITFYNQLQQLEQMTTTAENWLKT 627
Cdd:COG1196    739 LEELEEELEELEEELEE---LQERLEELEEELES--------LEEALAKLKeEIEELEEKRQALQEELEELEEELEEAER 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  628 QPTTTSEptAIKSQLKICKDEINRLSALQPQIERLKIQSIALKEKGQgpmFLDADFVAFTNHFNQVFADVQAREKELQTI 707
Cdd:COG1196    808 RLDALER--ELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE---ELEKELEELKEELEELEAEKEELEDELKEL 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  708 FDSLppMRYQETMSTILTWIQQSETKLSIPQVTVTEYDIMEQRL-GELQALQSSLQEQqnGLNYLSTTVKEMSKKAP--- 783
Cdd:COG1196    883 EEEK--EELEEELRELESELAELKEEIEKLRERLEELEAKLERLeVELPELEEELEEE--YEDTLETELEREIERLEeei 958
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953419023  784 --LSDISRKYQSEFEEIEGRWKKLSSQLvehcqklEEQMAKLRKIQNHIKTLKKWITEV 840
Cdd:COG1196    959 eaLGPVNLRAIEEYEEVEERYEELKSQR-------EDLEEAKEKLLEVIEELDKEKRER 1010
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
3081-3123 2.45e-03

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 38.01  E-value: 2.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1953419023 3081 ICKEC--PIIGFRYRSLKHFNYDICQSCffsgrVAKG-HKMHyPMV 3123
Cdd:cd02340      2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
602-705 2.94e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.61  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  602 NNIITFYNQLQQLEQMTTTAENWLKTQPTTTSePTAIKSQLKICKDEINRLSALQPQIERLKIQSIAL-KEKGQGPMFLD 680
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*
gi 1953419023  681 ADFVAFTNHFNQVFADVQAREKELQ 705
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLE 104
PTZ00121 PTZ00121
MAEBL; Provisional
1476-1925 4.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1476 DESEKKKPQQKEDILKRLKAEMNDIRPKVDSTRDQAANLmANRGDHCRKVVEPKISELNHRFAAisHRIKtgKASIPLKE 1555
Cdd:PTZ00121  1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA-KKKAEEKKKADEAKKKAEEDKKKA--DELK--KAAAAKKK 1419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1556 LEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMSE----DNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKH 1631
Cdd:PTZ00121  1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1632 NALKDlRSQRRKKALEISHQwyQYKRQADDLLKCLDdiEKKLASLPEPRDERKIKEIDR-ELQKKKEELNAV--RRQAEG 1708
Cdd:PTZ00121  1500 DEAKK-AAEAKKKADEAKKA--EEAKKADEAKKAEE--AKKADEAKKAEEKKKADELKKaEELKKAEEKKKAeeAKKAEE 1574
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1709 LSEDGAAMAVEPTQIQlSKRWREIESKFAQFRRLNFAQIHTVHEESVVA----MTEDMPLEISYVPSTYLTEITHVSQAL 1784
Cdd:PTZ00121  1575 DKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1785 SEVEE-LLNAPDLCAQDFEDLFKQEESLKNIKDslqqisgridiihnKKTAALHSATPAERAKLQEALSRLDFQWERVNN 1863
Cdd:PTZ00121  1654 KAEEEnKIKAAEEAKKAEEDKKKAEEAKKAEED--------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953419023 1864 MYKDRQGRFDRSVEKWRRFHYDMKILNQWLTEAEQFLKKTQIPENWEHAKYKWYLKELQDGI 1925
Cdd:PTZ00121  1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1391-1711 4.15e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 4.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1391 QKEIEKQKVHLKSVTEVGEALKTVLGKKEMLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMENFDQNVDYITNWIIQ 1470
Cdd:TIGR04523  213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1471 ADALLDESEKKKpqqKEDILKRLKAEMNDIRPKVDSTRDQAANlmanrgdhcrkvVEPKISELNHRFAAISHRiktgkas 1550
Cdd:TIGR04523  293 LKSEISDLNNQK---EQDWNKELKSELKNQEKKLEEIQNQISQ------------NNKIISQLNEQISQLKKE------- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1551 ipLKELEQFNSDIQKLLEPLEAEIQQgvNLKEEDFNKDMSEDNEGTVKELLQRGDNLQQriTDERKREEIKIKQQLLQTK 1630
Cdd:TIGR04523  351 --LTNSESENSEKQRELEEKQNEIEK--LKKENQSYKQEIKNLESQINDLESKIQNQEK--LNQQKDEQIKKLQQEKELL 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1631 HNALKDLRSQRRKKALEIS---HQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEID-------RELQKKKEELN 1700
Cdd:TIGR04523  425 EKEIERLKETIIKNNSEIKdltNQDSVKELIIKNLDNTRESLETQLKVL-----SRSINKIKqnleqkqKELKSKEKELK 499
                          330
                   ....*....|.
gi 1953419023 1701 AVRRQAEGLSE 1711
Cdd:TIGR04523  500 KLNEEKKELEE 510
SPEC smart00150
Spectrin repeats;
334-432 4.33e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 4.33e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023   334 QRFTEEQCLFSAWLSEKEDAVNkiHTTGFKDQSEVLSNLQKLAVLKTDLEKKKQTMDKLCSLNQDLLSalKNTVVAHKME 413
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA--SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIE 76
                            90
                    ....*....|....*....
gi 1953419023   414 AWLDNFAQRWDNLVQKLEK 432
Cdd:smart00150   77 ERLEELNERWEELKELAEE 95
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
1-17 5.05e-03

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 39.14  E-value: 5.05e-03
                           10
                   ....*....|....*..
gi 1953419023    1 MYITSLFQVLPQQVSIE 17
Cdd:cd21233     95 MYVTSLFQVLPQQVSIE 111
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
499-599 5.74e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.84  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023  499 DITELHSWITRSEAVLQSPEFAiyRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEqmvNEGVNADSIKQASE 578
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYG--KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 1953419023  579 QLNSRWIEFCQLLSERLNWLE 599
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2016-2653 5.80e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 42.44  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2016 EQQLKEKLEQVKLLAEELPLRQGILKQLNETGGTVLvsaplspeeQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKD 2095
Cdd:COG0419    173 SELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEAL---------EEELKELKKLEEIQEEQEEEELEQEIEALEERLAE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2096 LGQLEEQLNHLLLWLSPIRNQLEIYNQPNQTgpfDIKEIEVAVQAKQPDVEGiLSKGQHLYKEkpatqpAKRKLEDLSSD 2175
Cdd:COG0419    244 LEEEKERLEELKARLLEIESLELEALKIREE---ELRELERLLEELEEKIER-LEELEREIEE------LEEELEGLRAL 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2176 WKVVTQLLQELRAKQpGPAPGLTTVRAPPSQTVTLVTQPAVTKETAISKLEMPSSLLLE------VPALADFNRAWTELT 2249
Cdd:COG0419    314 LEELEELLEKLKSLE-ERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEelekelEKALERLKQLEEAIQ 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2250 DWLSLLDRVIKsqrvmvgDLEDINEMIIKQKATLQDLEQRRPQLEELITAAQNLKNKTSNQEARTII------------- 2316
Cdd:COG0419    393 ELKEELAELSA-------ALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAElagagekcpvcgq 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2317 ------TDRIERIQSQW---DEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEApyTVDAIQKKIT 2387
Cdd:COG0419    466 elpeehEKELLELYELEleeLEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEE--KLEKLENLLE 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2388 ETKQLAKDLRQWQINVDVANdlALKLLRDYSADDTRkvHMITENINASWASIHKRLSEREAALEETHRLLQQFPlDLEKF 2467
Cdd:COG0419    544 ELEELKEKLQLQQLKEELRQ--LEDRLQELKELLEE--LRLLRTRKEELEELRERLKELKKKLKELEERLSQLE-ELLQS 618
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2468 LAWLTEAETTANVLQDATHKERLLEDSKGVRELMKQW-QDLQGEIEAHTDIYHNLDENGQKVLRSLEGSDDAALLQRRLD 2546
Cdd:COG0419    619 LELSEAENELEEAEEELESELEKLNLQAELEELLQAAlEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELE 698
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2547 NMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQEllvwLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEP 2626
Cdd:COG0419    699 QLREELEELLKKLGEIEQLIEELESRKAELEELKKE----LEKLEKALELLEELREKLGKAGLRADILRNLLAQIEAEAN 774
                          650       660
                   ....*....|....*....|....*..
gi 1953419023 2627 VIMSTLETVRIFLTEQPLEGLEKLYQE 2653
Cdd:COG0419    775 EILSKLSLNRYDLRRLTIRKDGNGGLV 801
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1605-2388 7.73e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1605 DNLQqRITDERKreEIKIKQQLLQT---KHNALKDLRSQRRKKALEIshqwyqYKRQADDLLKCLDDIEKKLASLpeprd 1681
Cdd:TIGR02168  186 ENLD-RLEDILN--ELERQLKSLERqaeKAERYKELKAELRELELAL------LVLRLEELREELEELQEELKEA----- 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1682 ERKIKEIDRELQKKKEELNAVRRQAEGLSE--DGAAMAVEPTQIQLSKRWREIESKFAQFRRL--NFAQIHTVHEESVVA 1757
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEeiEELQKELYALANEISRLEQQKQILRERLANLerQLEELEAQLEELESK 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1758 MTEDMPL--EISYVPSTYLTEITHVSQALSE----VEELLNAPDLCAQDFE-------DLFKQEESLKN----IKDSLQQ 1820
Cdd:TIGR02168  332 LDELAEElaELEEKLEELKEELESLEAELEEleaeLEELESRLEELEEQLEtlrskvaQLELQIASLNNeierLEARLER 411
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1821 ISGRIDIIHNKKTAALHSATPAERAKLQEALSRLD-------FQWERVNNMYKDRQGRFDRSVEKWRRFHYDMKILNQWL 1893
Cdd:TIGR02168  412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEeeleelqEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1894 TEAE----QFLKKTQIPENWEHAKykwylKELQDGIGQRQSVVRV-------LNATGEEIIQ-------QSSKTDASIL- 1954
Cdd:TIGR02168  492 DSLErlqeNLEGFSEGVKALLKNQ-----SGLSGILGVLSELISVdegyeaaIEAALGGRLQavvvenlNAAKKAIAFLk 566
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 1955 QEKLGSLN------LRWQEVCKQLAERKKRLEEQKNILSEFQRDVNEFVLWLEE-------ADNVANiplepGNEQQLKE 2021
Cdd:TIGR02168  567 QNELGRVTflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDN-----ALELAKKL 641
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2022 KLEQVKL-LAEELPLRQGILkqlneTGGTVLVSA-PLSPE-EQDKLENKLKQTNLQWIKVSRNLPEKQEEIEAHVKDLGQ 2098
Cdd:TIGR02168  642 RPGYRIVtLDGDLVRPGGVI-----TGGSAKTNSsILERRrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2099 LEEQLNHLLLWLSPIRNQLEIYNQPNQTGPFDIKEIEVAVQAKQPDVEGILSKgqhLYKEKPATQPAKRKLEDLSSDWKV 2178
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQ 793
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2179 VTQLLQELRakqpgpapglttvrappsqtvtlvtqpavtkeTAISKLEMpsslllevpALADFNRAWTELTDWLSLLDRV 2258
Cdd:TIGR02168  794 LKEELKALR--------------------------------EALDELRA---------ELTLLNEEAANLRERLESLERR 832
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2259 IKSQRVMvgdLEDINEMIIKQKATLQDLEQRRPQLEELITAAqnlknktsnQEARTIITDRIERIQSQWDEVQEHLQNRR 2338
Cdd:TIGR02168  833 IAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEEL---------ESELEALLNERASLEEALALLRSELEELS 900
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953419023 2339 QQLNEMLKDSTQWLEAKEEAEQVLGQARAKLEswkEAPYTVDAIQKKITE 2388
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSE 947
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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