|
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
|
|
|
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
|
| 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
|
|
|