|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
307-413 |
2.36e-59 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 200.31 E-value: 2.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 386
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQ--SNRENLENAFNVAEKEFGVTRLL 78
|
90 100
....*....|....*....|....*..
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21189 79 DPEDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
4836-4908 |
4.12e-43 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 152.60 E-value: 4.12e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143463340 4836 EKITHEIELQKKTCSCCTPYQIEKISENHYRFGDTHIKRMVRILRSTVMVRVGGGWESLDEFLHKHDPCRAKG 4908
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
4838-4906 |
2.41e-33 |
|
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.
Pssm-ID: 460480 Cd Length: 69 Bit Score: 124.63 E-value: 2.41e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463340 4838 ITHEIELQKKTCSCCTPYQIEKISENHYRFGDTHIKRMVRILRSTVMVRVGGGWESLDEFLHKHDPCRA 4906
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
935-999 |
3.98e-26 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 103.88 E-value: 3.98e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 935 PLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIP 999
Cdd:pfam17902 1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
307-413 |
7.76e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.98 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGY-PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLNNAFAAADREFGVER- 384
Cdd:pfam00307 2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPKv 81
|
90 100
....*....|....*....|....*....
gi 1143463340 385 LLDAEDVdtNNPDEKSIITYVSSLYNALP 413
Cdd:pfam00307 82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
310-408 |
4.02e-20 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 88.14 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 310 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS--DSVSNTERLNNAFAAADREFGVERLLD 387
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1143463340 388 AEDVDTNNPDEKSIITYVSSL 408
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3879-4084 |
3.30e-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: 89.43 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLLKMspvEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAADAPPHlAATVRQP 3958
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST---DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3959 VADLNTRWSRLNAALAEREHKLENLMLQMGKLAStIAQLTAWMDKTRATLKDIAPPKnavNLRDIEIAQCKLVVLSNDIH 4038
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1143463340 4039 AHQDSVNAVNRAAQKYIQTSG-ALDAETSDSLKSMNLKWEDIQKVLE 4084
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAE 203
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4103-4308 |
2.89e-18 |
|
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: 86.73 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4103 EVEKWQRWLEETESALLSTKPtGGLPETAEFQLDEFKALKLDVEHNASPLEAhLHATEQHLKEEPQDADTWLSKTHGAMK 4182
Cdd:cd00176 8 DADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEA-LNELGEQLIEEGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4183 TKWNKVKELLVDREKKLQVAYEQAVALESALnDMEDWIIAAERKLTDQPSISRLPDViEKQLAEHESWMEEVAGRKMAMT 4262
Cdd:cd00176 86 QRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEPRLK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1143463340 4263 KHQASGVHMQYYCEKKDAIPIKNRLVSLKHRVEKISGRTAERAKQL 4308
Cdd:cd00176 164 SLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4427-4626 |
4.31e-18 |
|
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: 86.35 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4427 FEESMNDLESWVDDELERYQKAEHEpvfADIDGVRALVDEESRRSAERKTKENGVKTVVKKADALMASGVDEKDSIAQAK 4506
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYG---DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4507 ERLVEKWNQVEEAARHRGNSIKEAEQAAEEFDaKTHALLDWLAVEEQKLKASG-----------LDEVEGVKQEMDEAKG 4575
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDlgkdlesveelLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 4576 RYQECLKKGEEILSKCQPAAEPILRNWMRVVEARWKEVSEKVDEREFTLLE 4626
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2999-3216 |
1.94e-16 |
|
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: 81.34 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2999 QQGKVEDAYRALLNWLEETEEMMeNRKKPSADAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEASSDEEKkaL 3078
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3079 GNKNAQIEDRYKDLLNSAVDRQRKLLDAVDLAERLQEVTIpLDSWLQSADKRLQALAKVPiTVEKAEEMIGEQEALQDEL 3158
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1143463340 3159 EHKSDDLKDVLEIAPMLASLVSVEDANSISGQVNQLEARARALDAGITNMRPLLESFL 3216
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
307-427 |
2.08e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 86.53 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGY-PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIssDSVSNTERLNN--AFAAADREFGVE 383
Cdd:COG5069 125 TKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVL--DLQKKNKALNNfqAFENANKVIGIA 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1143463340 384 RLLDAEDV-DTNNPDEKSIITYVSSLYNAL----PHEPEMSRLQKVQEE 427
Cdd:COG5069 203 RLIGVEDIvNVSIPDERSIMTYVSWYIIRFglleKIDIALHRVYRLLEA 251
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
760-933 |
5.93e-16 |
|
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: 80.18 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 760 LIAFVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVY 839
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 840 LRQMQSQWDWLLALSKCLEEHLRDALNLKSFMEEASDAEAWIQEQSVRLENNYNRTDfsLEEGERFLRELDEIKEILNKY 919
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAH 158
|
170
....*....|....
gi 1143463340 920 HQVLMALTERCASI 933
Cdd:cd00176 159 EPRLKSLNELAEEL 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2320-3042 |
2.11e-15 |
|
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: 84.34 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2320 VEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLKS 2399
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2400 RFGGVDKALEKLKgilEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNS 2479
Cdd:TIGR02168 328 LESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2480 AENELElaaPIAAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEELKKKPDAELKKKLELLYQKWPKALGAARDRK 2559
Cdd:TIGR02168 405 LEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2560 DLVSKAGDLVkqfgDQVQALEQRLQGDQAELDELLASDK---AHDPEVCDALKL-------VELTMARRLAD--VDALNA 2627
Cdd:TIGR02168 482 RELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsGILGVLSELISVdegyeaaIEAALGGRLQAvvVENLNA 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2628 VMNRIESSAPgpdaNRLRRRADTLSDDAKGMAKKARTAADLAQRkqglaKKFERLCDEVSQFTENQKAEIQD-----AIE 2702
Cdd:TIGR02168 558 AKKAIAFLKQ----NELGRVTFLPLDSIKGTEIQGNDREILKNI-----EGFLGVAKDLVKFDPKLRKALSYllggvLVV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2703 KDLLNAERVQSKLNKI-------DDFWS-----------------SNSRELKNVGDEI-----KIDATPEDAQAVDTKLA 2753
Cdd:TIGR02168 629 DDLDNALELAKKLRPGyrivtldGDLVRpggvitggsaktnssilERRREIEELEEKIeeleeKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2754 ELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKINSLVAEIADLDPIGRS-RDELQKQKKEVVELAGDLGSAQ 2832
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2833 TKMLELGAEWEaALGAGIVAQpvfemnRAATDELNKLAARAGKRLAQREKKITETEDEIDKLHADADQIVGALEAIAKD- 2911
Cdd:TIGR02168 789 AQIEQLKEELK-ALREALDEL------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEi 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2912 EALQGAPSQLLDP-KQVSEKVRQLKESLKPVGEKMDAFNTDckllIKTAgpESDTKELDSLLKKVGDAYSDVVGKVSDKE 2990
Cdd:TIGR02168 862 EELEELIEELESElEALLNERASLEEALALLRSELEELSEE----LREL--ESKRSELRRELEELREKLAQLELRLEGLE 935
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 2991 MSVDaavQQQGKVEDAYRALLnwleetEEMMENRKKPSADAKVAKAQLHDYE 3042
Cdd:TIGR02168 936 VRID---NLQERLSEEYSLTL------EEAEALENKIEDDEEEARRRLKRLE 978
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1633-2483 |
1.77e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1633 RIDEARFEAKSLMDEV-------IREESRLKtigaSVLKIEQEISAMRDDVRASgstddvgiSVDEVYETRRRVEDDYMQ 1705
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAkktetgkAEEARKAE----EAKKKAEDARKAEEARKAE--------DARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1706 LLRQCQDLISFQNRLHAMNDEHSEQARRADEWLQMLQ-NDVEDVDQDPRFQRDEDrIQRIEELNRMA-AGGSSQLDDAEQ 1783
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAEDARKAEAARKAEE-ERKAEEARKAEdAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1784 ASRRLLTALEGTNVANDVRARHEELANLRRGKHQKVIDRlsqnmmeaASRKAEAEGVKQAVENLRQWSEQTAQRTRQPVQ 1863
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--------AEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1864 LpltELDLHEARKDEQvLHGEIENRLALIEELEKKAADVGDHASLAELQECKMKLKRSNSDLKGLRDnifdainglQTVN 1943
Cdd:PTZ00121 1307 A---KKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1944 SEGETLSRAVDSAGAKIRSARlpEAQSEVEALQDQADNLERITNNLCNIPNVTRTEPVIQKSKDLRKRVDSCAQELDARm 2023
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK- 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2024 gKLAElESLDAEfdGAKNKLSSFIGAFDDELKGLEKVSIDK-EKLAEQRRQTQDLVDKHSEGNAILDDVEAIAQKVTAED 2102
Cdd:PTZ00121 1451 -KKAE-EAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2103 PSKTGSAQKSVGELGARLQRQASELKaRGDKINKLDSKATSFAESEAAVLGYIEKQKDQLSTgfpvPATKEGVKSQLLDL 2182
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK----KAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2183 ERMNKTGKEEQRRVDDARHSARELAREASVEKEVQDMNQREKKlldewedladqfdavrsRANKAEQVLNEcaqmEKYIG 2262
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-----------------EKKKAEELKKA----EEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2263 AKKnmlegigapSTEPGVAKANRAQIQSMKAETEGEKSALEHVNSLANEliadgGANVEELMKKMDRLNRKWHSLESGLD 2342
Cdd:PTZ00121 1661 IKA---------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKAEELKKAEE 1726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2343 ENAGRVEEAAKLGQELKDIQKELRKELGElesnvekasamssndiGDQLATLDSLKsrfggvDKALEKLKGILEATEELE 2422
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEE----------------KKKIAHLKKEE------EKKAEEIRKEKEAVIEEE 1784
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 2423 VDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENE 2483
Cdd:PTZ00121 1785 LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3434-3653 |
3.79e-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: 74.79 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3434 RAVLDDLQYLIEWFSAArERILEGAPPSLDLEVLKSQLKHQRITNEEASANKVQFRNVAGEAKKVARqlgmEGNEANEKI 3513
Cdd:cd00176 3 QQFLRDADELEAWLSEK-EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE----EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3514 SDTVDEGKELVEEVMALCADRTETLERALALMEQLtSQFDELNKWLDQMDAELQASPSVTTATpaaELREMHDHNEELAR 3593
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLE---SVEELLKKHKELEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3594 MVAAYRPIIEGFKSDVGSLHEVLAEDQAPLLESVAGELVQGYEEVREAVRARGHAIDNMM 3653
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2320-2894 |
4.96e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2320 VEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASA---MSSNDIGDQLATLDS 2396
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2397 LKSRFGGVDKALEKLKG-ILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIG 2475
Cdd:COG1196 307 LEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2476 TVNSAENE-LELAAPIAAESLKLADELKRAEELFQKLIENEGDvsLIRAKVAEELKKKPDAELKKKLELLYQKwpkALGA 2554
Cdd:COG1196 387 ELLEALRAaAELAAQLEELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEEE---EEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2555 ARDRKDLVSKAgdlvKQFGDQVQALEQRLQGDQAELDELLASDKAHDPEVCDALKLVELTMARRLA-DVDALNAVMNRIE 2633
Cdd:COG1196 462 LELLAELLEEA----ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2634 SSAPGPDANRLRRRADTLSDDAkgmakkARTAADLAQRKQGLAKKFERLCDEVSQFTENQKAEIQDAIEKDLLNAERVQS 2713
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVA------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2714 KLNKIDDFWSSNSRELKNVGDEIKIDATPEDAQAVDTKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGK 2793
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2794 INSLVAEIADLDpigRSRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEAALgagivaqpvfEMNRAATDELNKLAARA 2873
Cdd:COG1196 692 ELELEEALLAEE---EEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL----------LEEEELLEEEALEELPE 758
|
570 580
....*....|....*....|.
gi 1143463340 2874 GKRLAQREKKITETEDEIDKL 2894
Cdd:COG1196 759 PPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2171-3051 |
1.50e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2171 TKEGVKSQLLDLERMNKTGKE------EQRRVDDARHSARELAREASVEKEVQDMNQREKKLLDEWEDLADQFDAVR--S 2242
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDfdfdakEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARkaE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2243 RANKAEQVLNecAQMEKYIGAKKNMLEG----IGAPSTEPGVAKANRAQIQSMKAEtegEKSALEHVNSLANELIADGGA 2318
Cdd:PTZ00121 1138 DARKAEEARK--AEDAKRVEIARKAEDArkaeEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAARKAEEER 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2319 NVEELMKKMDRlnRKWHSLESGldENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLK 2398
Cdd:PTZ00121 1213 KAEEARKAEDA--KKAEAVKKA--EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2399 SRFGGVDKALEKLKGILEATEELEvDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVN 2478
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2479 SAENELELAAPIAAESLKLADELKRAEELFQKLIENEgdvsliraKVAEELKKKpdAELKKKLEllyqkwpkalgAARDR 2558
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK--------KKADELKKA--AAAKKKAD-----------EAKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2559 KDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDELLASdKAHDPEVCDALKlveltmarrladvdalnavmnriESSAPG 2638
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK-KAEEAKKADEAK-----------------------KKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2639 PDANRLRRRAdtlsDDAKGMAKKARTAADlAQRKQGLAKKFE--RLCDEVSQFTENQKA-EIQDAIEKDLLNAERVQSKL 2715
Cdd:PTZ00121 1483 KKADEAKKKA----EEAKKKADEAKKAAE-AKKKADEAKKAEeaKKADEAKKAEEAKKAdEAKKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2716 NKIDDfwsSNSRELKNVGDEikiDATPEDAQAVDTKLAELQAGIDGLLATLQEQNVHLEE-KREQANRVQSESQKAAGKI 2794
Cdd:PTZ00121 1558 KKAEE---KKKAEEAKKAEE---DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEE 1631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2795 NSLVAEIadldpigRSRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEaalgagivAQPVFEMNRAATDElnKLAARAG 2874
Cdd:PTZ00121 1632 KKKVEQL-------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--------KKKAEEAKKAEEDE--KKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2875 KRLAQREKKITE----TEDEIDKLH----ADADQIVGALEAIAKDEALQGAPSQLLDPKQVSEKVRQLKeslKPVGEKMD 2946
Cdd:PTZ00121 1695 KKEAEEAKKAEElkkkEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK---KEEEKKAE 1771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2947 AFNTDCKLLIKTAGPESDTKELDSLLKKVGDAYSDVvgkvsdkemsvdAAVQQQGKVEDAYrallnwLEETEEMMENRKK 3026
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF------------ANIIEGGKEGNLV------INDSKEMEDSAIK 1833
|
890 900
....*....|....*....|....*
gi 1143463340 3027 PSADAKvaKAQLHDYEVLMKHVEDK 3051
Cdd:PTZ00121 1834 EVADSK--NMQLEEADAFEKHKFNK 1856
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1816-2484 |
1.69e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1816 HQKVIDRLSQNMMEAASRKAEAEGVKQAVENLRQWSEQTAQRTRQPVQLPLTELDLHEARKD------------------ 1877
Cdd:pfam15921 101 HEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEdmledsntqieqlrkmml 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1878 --EQVLHgeiENRLALIEELEKKAADVGDHASLAELQECKMK------LKRSNSDLKGLRDNIFDAINGLQTVNSEGETL 1949
Cdd:pfam15921 181 shEGVLQ---EIRSILVDFEEASGKKIYEHDSMSTMHFRSLGsaiskiLRELDTEISYLKGRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1950 -----------------SRAVDSAG--AKIRSAR--LPEAQSEVEALQDQADNLERITnnLCNIPNVTRTepVIQKSKDL 2008
Cdd:pfam15921 258 ielllqqhqdrieqlisEHEVEITGltEKASSARsqANSIQSQLEIIQEQARNQNSMY--MRQLSDLEST--VSQLRSEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2009 R--KRV-DSCAQELDARMgKLAELESLDAEFDgaKNKLSSFIGAFDDELKGLEKVSIDKEK-LAEQRRQTQDLVDKHSeG 2084
Cdd:pfam15921 334 ReaKRMyEDKIEELEKQL-VLANSELTEARTE--RDQFSQESGNLDDQLQKLLADLHKREKeLSLEKEQNKRLWDRDT-G 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2085 NAI--------LDDVEAIAQKVTAedpskTGSAQKSvgELGARLQRQASELKARGDKINKLdSKATSFAESeaavlgyie 2156
Cdd:pfam15921 410 NSItidhlrreLDDRNMEVQRLEA-----LLKAMKS--ECQGQMERQMAAIQGKNESLEKV-SSLTAQLES--------- 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2157 kqkdqlstgfpvpaTKEGVKSQLLDLERMNKTGKEEQRRVDDARHSARELARE-ASVEKEVQDMNQREKKLLDEWEDLAD 2235
Cdd:pfam15921 473 --------------TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAiEATNAEITKLRSRVDLKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2236 QFDAVRSRANKAEQVLNECAQMEKYIGAKK----NMLEGIGAPSTEPGVAKANRAQIQSmkaETEGEKSALEHVNSLANE 2311
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRqqieNMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEFKILKDK 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2312 liadGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQL 2391
Cdd:pfam15921 616 ----KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2392 ATLDSLKSRFGGVDKALEKLKGILEATEELEVDATNRA-EIQEQLETTQKKADELERKIENVKKAALNAQNEG--LELEK 2468
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhfLKEEK 771
|
730
....*....|....*..
gi 1143463340 2469 -KLDELIGTVNSAENEL 2484
Cdd:pfam15921 772 nKLSQELSTVATEKNKM 788
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3659-3873 |
1.87e-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: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3659 FGERLETLVANLQGAADRLRENEGISaDPSVLESRLAENRSIVESLRDKQNAYDALKQTASELLASAPEgdaAAGDVENK 3738
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP---DAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3739 LNRLEKLWKEIEREAVDRGVLLEDVLDKAKHFWsELDSCQKAVDDLRNRLElVEPATGHPEQLADQQEIMAQVASEMERA 3818
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 3819 RPRIEALSIAGKQLADYVPDDEKAVIENQVANVRGGFSTITGLFAEKKRDLIAAM 3873
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2246-2459 |
5.02e-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: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2246 KAEQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVaKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMK 2325
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2326 KMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQkELRKELGELEsnvekaSAMSSNDIGDQLATLDSLKSRFGGVD 2405
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKE------AALASEDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2406 KALEKLKGILEATEEL------EVDATNRAEIQEQLETTQKKADELERKIENVKKAALNA 2459
Cdd:cd00176 153 EELEAHEPRLKSLNELaeelleEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3879-3981 |
5.90e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.04 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLLKMspvEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAADAPPHlAATVRQP 3958
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASE---DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEER 78
|
90 100
....*....|....*....|...
gi 1143463340 3959 VADLNTRWSRLNAALAEREHKLE 3981
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1847-2593 |
1.01e-10 |
|
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: 68.93 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1847 LRQWSEQTAQRTRQPVQLPLTELDLHEARKDEQVLHGEIENRLALIEELEKKAADVGD--HASLAELQECKMKLKRSNSD 1924
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1925 LKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAKIRsarlpEAQSEVEALQDQADNLERITNNLcnipnVTRTEPVIQK 2004
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLE-----ELKEELESLEAELEELEAELEEL-----ESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2005 SKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGAFDDELKGLEKVSIdKEKLAEQRRQTQDLVDKHSEG 2084
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2085 NAILDDV-EAIAQKVTAEDPsktgsaqksvgelgarLQRQASELKARGDKINKLDSKATSFAESEAAVLgyieKQKDQLS 2163
Cdd:TIGR02168 460 EEALEELrEELEEAEQALDA----------------AERELAQLQARLDSLERLQENLEGFSEGVKALL----KNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2164 TGFpvpatkeGVKSQLLdlermnKTGKEEQRRVDDARHSARELA---REASVEKEVQDMNQREKK-----LLDEWEDLAD 2235
Cdd:TIGR02168 520 GIL-------GVLSELI------SVDEGYEAAIEAALGGRLQAVvveNLNAAKKAIAFLKQNELGrvtflPLDSIKGTEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2236 QFDAVRSRANKaEQVLNECAQMEKYIGAKKNMLEGIGApstepGVAKANR-AQIQSMKAETEGEKSALehvnSLANELIA 2314
Cdd:TIGR02168 587 QGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYLLG-----GVLVVDDlDNALELAKKLRPGYRIV----TLDGDLVR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2315 DGGA-NVEELMKKMDRLNRKwhsleSGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAM---SSNDIGDQ 2390
Cdd:TIGR02168 657 PGGViTGGSAKTNSSILERR-----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleeLSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2391 LATLDSLKSRFGGVDKALEKLKG-ILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKK 2469
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKeLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2470 LDELIGTVNSAENELElaapiaAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEElkKKPDAELKKKLELLYQKWP 2549
Cdd:TIGR02168 812 LTLLNEEAANLRERLE------SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL--EELIEELESELEALLNERA 883
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1143463340 2550 KALGAARDRKDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDEL 2593
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4075-4658 |
2.12e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4075 KWEDIQKVlESLAFDMEVAKKEAENVGGEVEKWQRWLEETESALLSTKPTGGLPETAE--FQLDEF-KALKLDVEHNASP 4151
Cdd:PTZ00121 1219 KAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEeaRKADELkKAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4152 LEAHLHATEQHLKEEPQDADTWLSKTHGAMKTKWNKVKELLVDREKKLQVAYEQAVALESALNDMEDWIIAAERKLTDQp 4231
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA- 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4232 siSRLPDVIEKQlAEHESWMEEvAGRKMAMTKHQASGVHmQYYCEKKDAIPIKNRLVSLKHRVE-KISGRTAERAKQLAV 4310
Cdd:PTZ00121 1377 --KKKADAAKKK-AEEKKKADE-AKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4311 TRDEVATWQDGLHDLEHF-ISDVLVKIAPEPNTTsslEKLKAKLEEVK----EAQRDVTAKQTLFDVTRKRGIGLAERAT 4385
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKA---DEAKKKAEEAKkkadEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4386 RSEYKQISMTNEKMS-KKWAEMLKKLRDRLREAEQAVLEGGAFEESMNDLESWVDDELERYQKAEHEPVFADIDGVRALV 4464
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4465 DEESRRSAERKTKENGVKtvvkKADalmasgvDEKDSIAQAKERLVEKWNQVEEAAR-HRGNSIKEAEQAAEEFDAKTHA 4543
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELK----KAE-------EEKKKVEQLKKKEAEEKKKAEELKKaEEENKIKAAEEAKKAEEDKKKA 1677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4544 LLDWLAVEEQKLKASGLDEVEGVKQEMDEAKGRYQECLKKGEEIlskcQPAAEpilRNWMRVVEARWKEVSEKVDEREFT 4623
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL----KKAEE---ENKIKAEEAKKEAEEDKKKAEEAK 1750
|
570 580 590
....*....|....*....|....*....|....*
gi 1143463340 4624 LLEQEQKAKEQNEQIEKlaKFAAQKREELNRMIEQ 4658
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEE--KKAEEIRKEKEAVIEE 1783
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3879-3982 |
8.56e-09 |
|
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 characteriztic 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: 56.17 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLlkmSPVEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAaDAPPHLAATVRQP 3958
Cdd:pfam00435 6 FFRDADDLESWIEEKEALL---SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQER 81
|
90 100
....*....|....*....|....
gi 1143463340 3959 VADLNTRWSRLNAALAEREHKLEN 3982
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4352-4771 |
2.00e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4352 KLEEVKEAQ--RDVTAKQTLFDVTRKRGIGLAERATRSE-------YKQISMTNEKMSKKWAEMLKKLRDRLREAEQAV- 4421
Cdd:PTZ00121 1165 KAEEARKAEdaKKAEAARKAEEVRKAEELRKAEDARKAEaarkaeeERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKk 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4422 LEGGAFEESMNDLESWVDDELERYQKAEHEPVFADIDGVRALvdEESRRSAERKTKENGVKTVVKKADALMASGVDE-KD 4500
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEaKK 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4501 SIAQAKERLVEKWNQVEEAARHRGNSIKEAEQAAEEFD-AKTHALLDWLAVEEQKLKASGLDEVEGVKQEMDEAKGRYQE 4579
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4580 CLKKGEEIlsKCQPAAEPILRNWMRVVEARWKEVSEKVDEREFTLLEQEQKAKEQNEQIEKLAKFAAQKR--EELNRMIE 4657
Cdd:PTZ00121 1403 DKKKADEL--KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkaDEAKKKAE 1480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4658 QppAQDLDTMEQNICDFANLDSELREQQPEVDAACKSAKKGARNPAAEMLSTEWKKlwlDAMGLQSSLDNQKAllEEMKR 4737
Cdd:PTZ00121 1481 E--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KADEAKKAEEKKKA--DELKK 1553
|
410 420 430
....*....|....*....|....*....|....
gi 1143463340 4738 LEGWKWEDWKeRYVEWNDHAKARVNDLFRRIDRL 4771
Cdd:PTZ00121 1554 AEELKKAEEK-KKAEEAKKAEEDKNMALRKAEEA 1586
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4103-4200 |
1.16e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 52.72 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4103 EVEKWQRWLEETEsALLSTKPTGGLPETAEFQLDEFKALKLDVEHNASPLEAHLHATEQHLKEEPQDADTwLSKTHGAMK 4182
Cdd:smart00150 6 DADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLEELN 83
|
90
....*....|....*...
gi 1143463340 4183 TKWNKVKELLVDREKKLQ 4200
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4534-4735 |
1.91e-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: 55.14 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4534 AEEFDAKTHALLDWLAVEEQKLKASG-----------LDEVEGVKQEMDEAKGRYQECLKKGEEILSKCQPAAEPIlRNW 4602
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDygddlesvealLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-QER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4603 MRVVEARWKEVSEKVDEREfTLLEQEQKAKEQNEQIEKLAKFAAQKREELNRmieQPPAQDLDTMEQNICDFANLDSELR 4682
Cdd:cd00176 81 LEELNQRWEELRELAEERR-QRLEEALDLQQFFRDADDLEQWLEEKEAALAS---EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463340 4683 EQQPEVDAACKSAKK------GARNPAAEMLSTEWKKLWLDamgLQSSLDNQKALLEEM 4735
Cdd:cd00176 157 AHEPRLKSLNELAEElleeghPDADEEIEEKLEELNERWEE---LLELAEERQKKLEEA 212
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2337-3030 |
2.82e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2337 LESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLKSRFGGVDKALEKLKGILE 2416
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2417 ATEEL------EVDATNRAEIQEQLETTQKKADELERKIENVKK---------AALNAQNEG---LELEKKLDELIGTVN 2478
Cdd:pfam15921 195 DFEEAsgkkiyEHDSMSTMHFRSLGSAISKILRELDTEISYLKGrifpvedqlEALKSESQNkieLLLQQHQDRIEQLIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2479 SAENELELAAPIAAESLKLADELKRAEELFQKLIEN------------EGDVSLIRAKVAEELKKKPDA--ELKKKLELL 2544
Cdd:pfam15921 275 EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdlESTVSQLRSELREAKRMYEDKieELEKQLVLA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2545 YQKwpkaLGAARDRKDLVSK-AGDLvkqfGDQVQALEQRLQGDQAELDellasdkahdpevcdalklVELTMARRLADVD 2623
Cdd:pfam15921 355 NSE----LTEARTERDQFSQeSGNL----DDQLQKLLADLHKREKELS-------------------LEKEQNKRLWDRD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2624 ALNAVMN---RIESSAPGPDANRLRRRADTLSDDAKGMAKKARTAAdlaqrkQGLAKKFERLCDEVSQFtENQKAEIQDA 2700
Cdd:pfam15921 408 TGNSITIdhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAI------QGKNESLEKVSSLTAQL-ESTKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2701 IEKDLLNAERVQSKLNKIDDFWSSNSRElknvgdEIKIDATpedaqavDTKLAELQAGIDGLLATLQeqnvHLEEKREQA 2780
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEK------ERAIEAT-------NAEITKLRSRVDLKLQELQ----HLKNEGDHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2781 NRVQSESQkaagkinSLVAEIADLDPIgrsRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEAalgagivaqpvfEMN- 2859
Cdd:pfam15921 544 RNVQTECE-------ALKLQMAEKDKV---IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK------------EINd 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2860 -RAATDELNKLAARAGKRLAQREKKITETEDEIDKLHADADQIVGALEAIA--KDEALQGAPSQLLDPKQVSEKVRQLKE 2936
Cdd:pfam15921 602 rRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKqeRDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2937 SLKPVGEKMDAFNTDCKLLIKTAGPESDTKE--LDSLLKKVGDAYSDVVG---KVSDKEMSVDAAvqqQGKVEDAYRALL 3011
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSELEQTRntLKSMEGSDGHAMKVAMGmqkQITAKRGQIDAL---QSKIQFLEEAMT 758
|
730
....*....|....*....
gi 1143463340 3012 NWLEETEEMMENRKKPSAD 3030
Cdd:pfam15921 759 NANKEKHFLKEEKNKLSQE 777
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
763-861 |
4.47e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.18 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 763 FVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVYLRQ 842
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
|
90
....*....|....*....
gi 1143463340 843 MQSQWDWLLALSKCLEEHL 861
Cdd:smart00150 82 LNERWEELKELAEERRQKL 100
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4427-4528 |
5.44e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4427 FEESMNDLESWVDdelERYQKAEHEPVFADIDGVRALVDEESRRSAERKTKENGVKTVVKKADALMASGVDEKDSIAQAK 4506
Cdd:smart00150 3 FLRDADELEAWLE---EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1143463340 4507 ERLVEKWNQVEEAARHRGNSIK 4528
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2043-2510 |
1.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2043 LSSFIGAFDDELKGLEKVS-----IDKEKLAEQRRQTQDLVDKHSEGNAILDDVEAIAQKVtaedpsktgsaqksvgelg 2117
Cdd:COG4717 44 RAMLLERLEKEADELFKPQgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2118 ARLQRQASELKARGDKINKLDSKATSFAESEAAvlgyiekqKDQLStgfPVPATKEGVKSQLLDLERMNKTGKEEQRRVD 2197
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQELEAL--------EAELA---ELPERLEELEERLEELRELEEELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2198 DARHSARELAREASVEKEvqdmnQREKKLLDEWEDLADQFDAVRSRANKAEQVLNEC-------------AQMEKYIGAK 2264
Cdd:COG4717 174 ELQEELEELLEQLSLATE-----EELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqleneleaAALEERLKEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2265 KNMLEGIGA--------------PSTEPGVAKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKMDRL 2330
Cdd:COG4717 249 RLLLLIAAAllallglggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2331 NRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKE--LGELESNVEKASAMSSND---IGDQLATLDSLKSRFGGVD 2405
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAGVEDEEElraALEQAEEYQELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2406 KALEKLKGILEAteelEVDATNRAEIQEQLETTQKKADELERKIENV--KKAALNAQNEGLELEKKLDELIGTVNSAENE 2483
Cdd:COG4717 409 EQLEELLGELEE----LLEALDEEELEEELEELEEELEELEEELEELreELAELEAELEQLEEDGELAELLQELEELKAE 484
|
490 500
....*....|....*....|....*...
gi 1143463340 2484 LELAApIAAESLKLADE-LKRAEELFQK 2510
Cdd:COG4717 485 LRELA-EEWAALKLALElLEEAREEYRE 511
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2144-2351 |
2.91e-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: 51.68 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2144 FAESEAAVLGYIEKQKDQLSTGFPvPATKEGVKSQLLDLERMNKTGKEEQRRVDDARHSARELARE-----ASVEKEVQD 2218
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdaEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2219 MNQREKKLLDEWEDLADQFDavrsRANKAEQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVAKANRaQIQSMKAETEGE 2298
Cdd:cd00176 84 LNQRWEELRELAEERRQRLE----EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLK-KHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1143463340 2299 KSALEHVNSLANELIADGG-ANVEELMKKMDRLNRKWHSLESGLDENAGRVEEA 2351
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3002-3103 |
9.52e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3002 KVEDAYRALLNWLEETEEMMENrKKPSADAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEasSDEEKKALGNK 3081
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEIEER 78
|
90 100
....*....|....*....|..
gi 1143463340 3082 NAQIEDRYKDLLNSAVDRQRKL 3103
Cdd:smart00150 79 LEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1115-1329 |
1.03e-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: 49.75 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1115 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQLPNPTPTQRVNH--- 1191
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIqer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1192 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINMVLKQQQ 1267
Cdd:cd00176 81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 1268 TVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1329
Cdd:cd00176 160 PRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3066-3789 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3066 VAEASSDEEKKALGNKNAQIEDRYKDLLNSAVDRQRKLLDAVDLAERLQEvtipLDSWLQSADKRLQALAKVPITVEKAE 3145
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3146 EMIGEQEA-LQDELEHKSDDLKDVLEIAPMLASLVSV--EDANSISGQVNQLEARARALDAGITNMRPLLESFLQQIQDF 3222
Cdd:TIGR02168 340 AELEEKLEeLKEELESLEAELEELEAELEELESRLEEleEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3223 TLDAEDMTQFVGETEVKL--GELDELPIEPDDLVEQTNILAEIAVSIADRDEMmanifevgKQLAIQGEPEEALIAQKKL 3300
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEELREELEE--------AEQALDAAERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3301 DDLKFRYADLMTSADEKIALLAKAI-------PLSEGFH--EGFDTVMQ----------VLEDMDRDLQTIDEEDPETQA 3361
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISvdEGYEAAIEaalggrlqavVVENLNAAKKAIAFLKQNELG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3362 ELIFLLEEDISQKmRPSVDELTALSNQLQVLCSADkadELQTNTIAMNKLVNS------VADRVARRAE-RIEMASKQSR 3434
Cdd:TIGR02168 572 RVTFLPLDSIKGT-EIQGNDREILKNIEGFLGVAK---DLVKFDPKLRKALSYllggvlVVDDLDNALElAKKLRPGYRI 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3435 AVLDDLQYLIEWFSAARERILEGAPPSLDLEVLKSQLKHQRITNEEASANKvqfrnvagEAKKVARQLgmegNEANEKIS 3514
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK--------ALAELRKEL----EELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3515 DTVDEGKELVEEVMALCADrtetLERALALMEQLTSQFDELNKWLDQMDAELQASpsvttatpAAELREMHDHNEELARM 3594
Cdd:TIGR02168 716 QLRKELEELSRQISALRKD----LARLEAEVEQLEERIAQLSKELTELEAEIEEL--------EERLEEAEEELAEAEAE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3595 VAAYRPIIEGFKSDVGSLHEVLAEDQAPL--LESVAGELVQGYEEVREAVRARGHAIDNMMGATIGFGERLETLVANLQG 3672
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELtlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3673 AADRLRENE----GISADPSVLESRLAENRSIVESLRDKQNAYDalkQTASELLASAPEGDAAAGDVENKLNRLE-KLWK 3747
Cdd:TIGR02168 864 LEELIEELEseleALLNERASLEEALALLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGLEvRIDN 940
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1143463340 3748 EIEREAVDRGVLLEDVLDKAKHFWSELDSCQKAVDDLRNRLE 3789
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3218-3429 |
2.77e-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: 48.60 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3218 QIQDFTLDAEDMTQFVGETEVKLGElDELPIEPDDLVEQTNILAEIAVSIADRDEMMANIFEVGKQLAIQGEPEEALIaQ 3297
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3298 KKLDDLKFRYADLMTSADEKIALLAKAIPLSEGFHEgFDTVMQVLEDMDRDLQTIDEEDPETQAELIF----LLEEDISQ 3373
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLkkhkELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1143463340 3374 KmRPSVDELTALSNQLQVLCSADKADELQTNTIAMNKLVNSVADRVARRAERIEMA 3429
Cdd:cd00176 158 H-EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2248-2349 |
3.43e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.70 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2248 EQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVAKANRAQiQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKM 2327
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1143463340 2328 DRLNRKWHSLESGLDENAGRVE 2349
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3416-3819 |
8.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3416 ADRVARRAERIEMASKQSRAVLDDLQY---LIEWFSAARERiLEGAPPSLDLEVLKSQLKHQRITN--EEASANKVQFRN 3490
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLddaDAEAVEARREE-LEDRDEELRDRLEECRVAAQAHNEeaESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3491 VAGEAKKVARQLGMEGNEANEKISD---TVDEGKELVEEVMALCADRTETLERALALMEQLTSQFDELNkwldQMDAELQ 3567
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR----EREAELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3568 aspsvttatpaAELREMHDHNEELARMVAAYR-PiiEGFKSDVGSLHEVLAEDQAPLLESVAGELvqgyEEVREAVRARG 3646
Cdd:PRK02224 433 -----------ATLRTARERVEEAEALLEAGKcP--ECGQPVEGSPHVETIEEDRERVEELEAEL----EDLEEEVEEVE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3647 HAIdnmmgatigfgERLETLVAnLQGAADRLRENEgisadpSVLESRLAENRSIVESLRDKQnayDALKQTASELLASAP 3726
Cdd:PRK02224 496 ERL-----------ERAEDLVE-AEDRIERLEERR------EDLEELIAERRETIEEKRERA---EELRERAAELEAEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3727 EGDAAAGDVENKLNRLEKLWKEIEREavdRGVLLE--DVLDKAKHFWSELDSCQKAVDDLRNRLE-LVEPATGHPEQLAD 3803
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSK---LAELKEriESLERIRTLLAAIADAEDEIERLREKREaLAELNDERRERLAE 631
|
410
....*....|....*.
gi 1143463340 3804 QQEIMAQVASEMERAR 3819
Cdd:PRK02224 632 KRERKRELEAEFDEAR 647
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3437-3539 |
1.10e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3437 LDDLQYLIEWFSAArERILEGAPPSLDLEVLKSQLKHQRITNEEASANKVQFRNVageaKKVARQLGMEGNEANEKISDT 3516
Cdd:smart00150 4 LRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL----NELGEQLIEEGHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1143463340 3517 VDEGKELVEEVMALCADRTETLE 3539
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4346-4658 |
1.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4346 LEKLKAKLEEVkEAQRDVTAKQtlfdvtrkrgiglAERATRseYKQISmtnEKMSKKWAEmLKKLRDRLREAEQAVLEgg 4425
Cdd:COG1196 188 LERLEDILGEL-ERQLEPLERQ-------------AEKAER--YRELK---EELKELEAE-LLLLKLRELEAELEELE-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4426 afeESMNDLESWVDDELERYQKAEhepvfADIDGVRALVDEESRRSAERKTKENGVKTVVKKADALMASGVDEKDSIAQA 4505
Cdd:COG1196 246 ---AELEELEAELEELEAELAELE-----AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4506 KERLVEKWNQVEEAARHRGNSIKEAEQAAEEFDAKTHALLDWLAVEEQKLKASgLDEVEGVKQEMDEAKGRYQECLKKGE 4585
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143463340 4586 EILSKCQPAAEPILRNwmrvvEARWKEVSEKVDEREFTLLEQEQKAKEQNEQIEKLAKFAAQKREELNRMIEQ 4658
Cdd:COG1196 397 ELAAQLEELEEAEEAL-----LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3674-3761 |
2.27e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3674 ADRLRENEGISADPSVLESRLAENRSIVESLRDKQNAYDALKQTASELLASAPEgdaAAGDVENKLNRLEKLWKEIEREA 3753
Cdd:smart00150 17 KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP---DAEEIEERLEELNERWEELKELA 93
|
....*...
gi 1143463340 3754 VDRGVLLE 3761
Cdd:smart00150 94 EERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3008-3105 |
3.10e-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 characteriztic 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: 40.38 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3008 RALLNWLEETEEMMENRKKPSaDAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEASSDEEkkALGNKNAQIED 3087
Cdd:pfam00435 11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE--EIQERLEELNE 87
|
90
....*....|....*...
gi 1143463340 3088 RYKDLLNSAVDRQRKLLD 3105
Cdd:pfam00435 88 RWEQLLELAAERKQKLEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4276-4586 |
3.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4276 EKKDAIPIKNRLVSLKHRVEKISGRTAERAKQLAVTRDEVATWQDGLHDLEHFISDVLVKIAPEPNTTSSLEKLKA--KL 4353
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKA 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4354 EEVKEAQRDVTAKQTLFDVTRKRGIglAERATRSEYKQISMTNEKMSKKWAEMLKKLRDRLREAEQAVLEggafEESMND 4433
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKK 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4434 LESWVDDELERYQKAEHEPVFADIDGVRAL----VDEESRRSAE--RKTKENGVKTV----------------------- 4484
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakKAEEDKKKAEeaKKAEEDEKKAAealkkeaeeakkaeelkkkeaee 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4485 VKKADALMASGVDEKDSIAQAKERLVEKWNQVEEAARHRGNSIKEAEQAAEEFDAKTHALLDWLAVEEQKLKASGLDEVE 4564
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
330 340
....*....|....*....|..
gi 1143463340 4565 GVKQEMDEAKGRYQECLKKGEE 4586
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKE 1816
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1288-1402 |
4.09e-03 |
|
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: 42.05 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1288 RINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESALQIQMVYRSEYETEmSWLDTVEETINRLRKPEELrpEQY 1367
Cdd:cd00176 65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDL--ESV 141
|
90 100 110
....*....|....*....|....*....|....*
gi 1143463340 1368 QQQLDMLIAEYTNLQEHTQAIEHVNKEGGRFIHEA 1402
Cdd:cd00176 142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEG 176
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
948-993 |
9.81e-03 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 9.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1143463340 948 KVTALCDY---SDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPS 993
Cdd:cd11768 1 IVVALYDFqpiEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
3518-3826 |
9.86e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3518 DEGKELVEEV--------MALCADRTETLERALAL-------MEQLTSQFDELNKWLDQMDAELQASPSVTTATPAAElr 3582
Cdd:COG3096 256 DLFKHLITEAtnyvaadyMRHANERRELSERALELrrelfgaRRQLAEEQYRLVEMARELEELSARESDLEQDYQAAS-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3583 emhDHneeLARMVAAYR--PIIEGFKSDVGSLHEVLAEDQAPLLEsvAGELVQGYEE----------------------- 3637
Cdd:COG3096 334 ---DH---LNLVQTALRqqEKIERYQEDLEELTERLEEQEEVVEE--AAEQLAEAEArleaaeeevdslksqladyqqal 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3638 ---------VREAVRARGHA----------IDNmmgatigFGERLETLVANLQGAADRLRENEGISADPSVLESRLAENR 3698
Cdd:COG3096 406 dvqqtraiqYQQAVQALEKAralcglpdltPEN-------AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3699 SIVESLRDKQNAYDALkQTASELLASAPEGDAAAGDVEN---KLNRLEKLwkEIEREAVDRgvLLEDVldkAKHFWSELD 3775
Cdd:COG3096 479 ELVCKIAGEVERSQAW-QTARELLRRYRSQQALAQRLQQlraQLAELEQR--LRQQQNAER--LLEEF---CQRIGQQLD 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 3776 ScQKAVDDLRNRLElvEPATGHPEQLADQQEIMAQVASEMERARPRIEALS 3826
Cdd:COG3096 551 A-AEELEELLAELE--AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
307-413 |
2.36e-59 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 200.31 E-value: 2.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 386
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQ--SNRENLENAFNVAEKEFGVTRLL 78
|
90 100
....*....|....*....|....*..
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21189 79 DPEDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
307-409 |
1.57e-43 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 155.25 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 386
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKS--NALYNLQNAFNVAEQKLGLTKLL 79
|
90 100
....*....|....*....|...
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLY 409
Cdd:cd21248 80 DPEDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
307-410 |
3.21e-43 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 154.49 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIS-SDSVSNterLNNAFAAADREFGVERL 385
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDpNDHLGN---LNNAFDVAEQELGIAKL 78
|
90 100
....*....|....*....|....*
gi 1143463340 386 LDAEDVDTNNPDEKSIITYVSSLYN 410
Cdd:cd21194 79 LDAEDVDVARPDEKSIMTYVASYYH 103
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
4836-4908 |
4.12e-43 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 152.60 E-value: 4.12e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143463340 4836 EKITHEIELQKKTCSCCTPYQIEKISENHYRFGDTHIKRMVRILRSTVMVRVGGGWESLDEFLHKHDPCRAKG 4908
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
303-410 |
2.22e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.91 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 303 SDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSdsvSN-TERLNNAFAAADREFG 381
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKK---SNaRHNLEHAFNVAERQLG 77
|
90 100
....*....|....*....|....*....
gi 1143463340 382 VERLLDAEDVDTNNPDEKSIITYVSSLYN 410
Cdd:cd21319 78 ITKLLDPEDVFTENPDEKSIITYVVAFYH 106
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
312-413 |
3.68e-38 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. 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. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. 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. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 139.87 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 312 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLLDAEDV 391
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKD--SPESRLEHAFTVAHEHLGIEKLLDPEDV 82
|
90 100
....*....|....*....|..
gi 1143463340 392 DTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21187 83 NVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
304-411 |
3.20e-35 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 131.72 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 304 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVE 383
Cdd:cd21216 7 EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKD--DPRENLNLAFDVAEKHLDIP 84
|
90 100
....*....|....*....|....*....
gi 1143463340 384 RLLDAED-VDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21216 85 KMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
307-413 |
4.84e-35 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 130.88 E-value: 4.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADReFGVERLL 386
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQ--SNLANLEHAFYVAEK-LGVTRLL 77
|
90 100
....*....|....*....|....*..
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21239 78 DPEDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
303-410 |
1.30e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 130.18 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 303 SDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTerLNNAFAAADREFGV 382
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYN--LQNAFNVAEKELGL 78
|
90 100
....*....|....*....|....*...
gi 1143463340 383 ERLLDAEDVDTNNPDEKSIITYVSSLYN 410
Cdd:cd21321 79 TKLLDPEDVNVDQPDEKSIITYVATYYH 106
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
307-410 |
2.20e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 129.21 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKI-SSDSVSNterLNNAFAAADREFGVERL 385
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLrPDRPLYN---LANAFLVAEQELGISQL 80
|
90 100
....*....|....*....|....*
gi 1143463340 386 LDAEDVDTNNPDEKSIITYVSSLYN 410
Cdd:cd21249 81 LDPEDVAVPHPDERSIMTYVSLYYH 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
307-413 |
2.45e-34 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 128.99 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADREFGVERLL 386
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQT--NLENLDQAFSVAERDLGVTRLL 79
|
90 100
....*....|....*....|....*..
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21238 80 DPEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
312-415 |
3.34e-34 |
|
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: 128.89 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 312 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvSNTERLNNAFAAADREFGVERLLDAEDV 391
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQ-SATERLDHAFNIARQHLGIEKLLDPEDV 83
|
90 100
....*....|....*....|....
gi 1143463340 392 DTNNPDEKSIITYVSSLYNALPHE 415
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQVLPQQ 107
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
307-413 |
9.33e-34 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 127.47 E-value: 9.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADReFGVERLL 386
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ--SNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
4838-4906 |
2.41e-33 |
|
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.
Pssm-ID: 460480 Cd Length: 69 Bit Score: 124.63 E-value: 2.41e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463340 4838 ITHEIELQKKTCSCCTPYQIEKISENHYRFGDTHIKRMVRILRSTVMVRVGGGWESLDEFLHKHDPCRA 4906
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
306-413 |
8.63e-33 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 124.74 E-value: 8.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 306 TSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADREFGVERL 385
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRS--NRENLETAFTVAEKELGIPRL 81
|
90 100
....*....|....*....|....*...
gi 1143463340 386 LDAEDVDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21243 82 LDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
304-410 |
1.06e-32 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 125.17 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 304 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVsnTERLNNAFAAADREFGVE 383
Cdd:cd21322 14 ETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNA--TYNLQQAFNTAEQHLGLT 91
|
90 100
....*....|....*....|....*..
gi 1143463340 384 RLLDAEDVDTNNPDEKSIITYVSSLYN 410
Cdd:cd21322 92 KLLDPEDVNMEAPDEKSIITYVVSFYH 118
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
311-412 |
7.04e-32 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 122.07 E-value: 7.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 311 ALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLDAED 390
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKL--AFTVAEKELGIPALLDAED 82
|
90 100
....*....|....*....|...
gi 1143463340 391 -VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21253 83 mVALKVPDKLSILTYVSQYYNYF 105
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
312-413 |
1.46e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. 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. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 121.22 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 312 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISsdSVSNTERLNNAFAAADREFGVERLLDAEDV 391
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVV--KMSPVERLEHAFSKAKNHLGIEKLLDPEDV 82
|
90 100
....*....|....*....|..
gi 1143463340 392 DTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21234 83 AVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
307-410 |
4.43e-30 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 117.12 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTerLNNAFAAADREFGVERLL 386
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYN--LQNAFNLAEQHLGLTKLL 79
|
90 100
....*....|....*....|....
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYN 410
Cdd:cd21320 80 DPEDISVDHPDEKSIITYVVTYYH 103
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
308-410 |
3.43e-29 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 114.17 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 308 ARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLD 387
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRL--AFRVAETSLGIPALLD 78
|
90 100
....*....|....*....|....
gi 1143463340 388 AED-VDTNNPDEKSIITYVSSLYN 410
Cdd:cd21197 79 AEDmVTMHVPDRLSIITYVSQYYN 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
304-412 |
5.89e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 108.63 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 304 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 382
Cdd:cd21290 10 EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDpVTN---LNNAFEVAEKYLDI 86
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 383 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21290 87 PKMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
307-406 |
6.27e-27 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 108.00 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSvsNTERLNNAFAAADREFGVERLL 386
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRS--NRENLEEAFRIAEQELKIPRLL 82
|
90 100
....*....|....*....|
gi 1143463340 387 DAEDVDTNNPDEKSIITYVS 406
Cdd:cd21244 83 EPEDVDVVNPDEKSIMTYVA 102
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
308-410 |
8.16e-27 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 107.65 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 308 ARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLD 387
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRL--AFEVAERELGIPALLD 78
|
90 100
....*....|....*....|....
gi 1143463340 388 AED-VDTNNPDEKSIITYVSSLYN 410
Cdd:cd21252 79 PEDmVSMKVPDCLSIMTYVSQYYN 102
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
307-412 |
9.32e-27 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 107.43 E-value: 9.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNkissdSVSNTERLNN---AFAAADREFGVE 383
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYS-----SLDPKNRRKNfelAFSTAEELADIA 75
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 384 RLLDAED--VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21200 76 PLLEVEDmvRMGNRPDWKCVFTYVQSLYRHL 106
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
310-412 |
1.96e-26 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 106.22 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 310 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLDAE 389
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQL--AFDVAEQELGIPPVMTGQ 80
|
90 100
....*....|....*....|....
gi 1143463340 390 D-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd22198 81 EmASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
310-411 |
2.45e-26 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 106.01 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 310 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSsaiDWNKISSDSVSNTE-RLNNAFAAADREFGVERLLDA 388
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDP---ELFKQAAIEQMDAEaRLNLAFDFAEKKLGIPKLLEA 79
|
90 100
....*....|....*....|...
gi 1143463340 389 EDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21226 80 EDVMTGNPDERSIVLYTSLFYHA 102
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
935-999 |
3.98e-26 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 103.88 E-value: 3.98e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 935 PLWQRGERIPHPIKVTALCDYSDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPSVVFRIP 999
Cdd:pfam17902 1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
307-411 |
4.95e-26 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 105.69 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIS-SDSVSNTERlnnAFAAADREFGVERL 385
Cdd:cd21291 10 TAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDkKDHRGNMQL---AFDIASKEIGIPQL 86
|
90 100
....*....|....*....|....*..
gi 1143463340 386 LDAEDV-DTNNPDEKSIITYVSSLYNA 411
Cdd:cd21291 87 LDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
306-406 |
7.18e-26 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 104.81 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 306 TSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERL 385
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNR--SPRDNLELAFRIAEQHLNIPRL 79
|
90 100
....*....|....*....|.
gi 1143463340 386 LDAEDVDTNNPDEKSIITYVS 406
Cdd:cd21192 80 LEVEDVLVDKPDERSIMTYVS 100
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
304-412 |
5.31e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 103.24 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 304 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 382
Cdd:cd21287 7 EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDpLTN---LNTAFDVAEKYLDI 83
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 383 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21287 84 PKMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
307-413 |
7.76e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.98 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGY-PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLNNAFAAADREFGVER- 384
Cdd:pfam00307 2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGVPKv 81
|
90 100
....*....|....*....|....*....
gi 1143463340 385 LLDAEDVdtNNPDEKSIITYVSSLYNALP 413
Cdd:pfam00307 82 LIEPEDL--VEGDNKSVLTYLASLFRRFQ 108
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
312-410 |
8.03e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 99.04 E-value: 8.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 312 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLLDAED- 390
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKL--AFDAAA-KLGIPRLLDPADm 82
|
90 100
....*....|....*....|
gi 1143463340 391 VDTNNPDEKSIITYVSSLYN 410
Cdd:cd21198 83 VLLSVPDKLSVMTYLHQIRA 102
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
304-412 |
8.70e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 99.80 E-value: 8.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 304 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDS-VSNterLNNAFAAADREFGV 382
Cdd:cd21289 7 EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDpIGN---LNTAFEVAEKYLDI 83
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 383 ERLLDAED-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21289 84 PKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
307-409 |
3.82e-23 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 97.43 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLL 386
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTL--AFKAAE-SVGIPTTL 84
|
90 100
....*....|....*....|....
gi 1143463340 387 DAED-VDTNNPDEKSIITYVSSLY 409
Cdd:cd21199 85 TIDEmVSMERPDWQSVMSYVTAIY 108
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
304-412 |
7.59e-22 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 93.98 E-value: 7.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 304 DATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTerLNNAFAAADREFGVE 383
Cdd:cd21288 7 EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGN--INLAMEIAEKHLDIP 84
|
90 100 110
....*....|....*....|....*....|
gi 1143463340 384 RLLDAED-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21288 85 KMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
307-408 |
2.51e-21 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 91.77 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS-DSVSNTERLNNAFAAadreFGVERL 385
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPlDIKENNKKAFEAFAS----LGVPRL 76
|
90 100
....*....|....*....|....
gi 1143463340 386 LDAED-VDTNNPDEKSIITYVSSL 408
Cdd:cd21255 77 LEPADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
311-413 |
1.78e-20 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 89.46 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 311 ALLQWARRVTAGYPrVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKisSDSVSNTERLNNAFAAADREFGVERLLDAED 390
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQ--ALEKSPRENLEDAFRIAQESLGIPPLLEPED 83
|
90 100
....*....|....*....|...
gi 1143463340 391 VDTNNPDEKSIITYVSSLYNALP 413
Cdd:cd21245 84 VMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
310-408 |
4.02e-20 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 88.14 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 310 DALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISS--DSVSNTERLNNAFAAADREFGVERLLD 387
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1143463340 388 AEDVDTNNPDEKSIITYVSSL 408
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
307-412 |
5.81e-20 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 88.10 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWnkissDSVSNTERLNN---AFAAADREFGVE 383
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDY-----DSLSPSNRKHNfelAFSMAEKLANCD 75
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 384 RLLDAED--VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21261 76 RLIEVEDmmVMGRKPDPMCVFTYVQSLYNHL 106
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
307-409 |
9.79e-20 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 87.78 E-value: 9.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADrEFGVERLL 386
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQ--DKKRNLLLAFQAAE-SVGIKPSL 84
|
90 100
....*....|....*....|....
gi 1143463340 387 DAED-VDTNNPDEKSIITYVSSLY 409
Cdd:cd21257 85 ELSEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3879-4084 |
3.30e-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: 89.43 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLLKMspvEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAADAPPHlAATVRQP 3958
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST---DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3959 VADLNTRWSRLNAALAEREHKLENLMLQMGKLAStIAQLTAWMDKTRATLKDIAPPKnavNLRDIEIAQCKLVVLSNDIH 4038
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1143463340 4039 AHQDSVNAVNRAAQKYIQTSG-ALDAETSDSLKSMNLKWEDIQKVLE 4084
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAE 203
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
309-412 |
4.17e-19 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 85.91 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 309 RDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIssDSVSNTERLNNAFAAADREFGVERLLDA 388
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL--DPANRRHNFTLAFSTAEKHADCAPLLEV 80
|
90 100
....*....|....*....|....*
gi 1143463340 389 ED-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21260 81 EDmVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
307-412 |
6.69e-19 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 85.04 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 386
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQ--NRRHNFEVAFSSAEKHADCPQLL 78
|
90 100
....*....|....*....|....*..
gi 1143463340 387 DAED-VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21259 79 DVEDmVRMREPDWKCVYTYIQEFYRCL 105
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
303-409 |
9.90e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 84.71 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 303 SDATSARdaLLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGV 382
Cdd:cd21195 2 GDIRPSK--LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQL--AFDVAEREFGI 77
|
90 100
....*....|....*....|....*...
gi 1143463340 383 ERLLDAEDV-DTNNPDEKSIITYVSSLY 409
Cdd:cd21195 78 PPVTTGKEMaSAQEPDKLSMVMYLSKFY 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
307-409 |
9.97e-19 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 85.13 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLL 386
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTL--AFQAAE-SVGIKSTL 90
|
90 100
....*....|....*....|....
gi 1143463340 387 DAED-VDTNNPDEKSIITYVSSLY 409
Cdd:cd21256 91 DINEmVRTERPDWQSVMTYVTAIY 114
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
307-412 |
1.24e-18 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 84.33 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDsvSNTERLNNAFAAADREFGVERLL 386
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQ--NRRQNFEVAFSAAEMLADCVPLV 78
|
90 100
....*....|....*....|....*...
gi 1143463340 387 DAED--VDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21258 79 EVEDmmIMGKKPDSKCVFTYVQSLYNHL 106
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4103-4308 |
2.89e-18 |
|
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: 86.73 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4103 EVEKWQRWLEETESALLSTKPtGGLPETAEFQLDEFKALKLDVEHNASPLEAhLHATEQHLKEEPQDADTWLSKTHGAMK 4182
Cdd:cd00176 8 DADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEA-LNELGEQLIEEGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4183 TKWNKVKELLVDREKKLQVAYEQAVALESALnDMEDWIIAAERKLTDQPSISRLPDViEKQLAEHESWMEEVAGRKMAMT 4262
Cdd:cd00176 86 QRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELEAHEPRLK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1143463340 4263 KHQASGVHMQYYCEKKDAIPIKNRLVSLKHRVEKISGRTAERAKQL 4308
Cdd:cd00176 164 SLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
307-408 |
3.80e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.98 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADrEFGVERLL 386
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKK--AYDGFA-SLGISRLL 77
|
90 100
....*....|....*....|...
gi 1143463340 387 DAED-VDTNNPDEKSIITYVSSL 408
Cdd:cd21254 78 EPSDmVLLAVPDKLTVMTYLYQI 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4427-4626 |
4.31e-18 |
|
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: 86.35 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4427 FEESMNDLESWVDDELERYQKAEHEpvfADIDGVRALVDEESRRSAERKTKENGVKTVVKKADALMASGVDEKDSIAQAK 4506
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYG---DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4507 ERLVEKWNQVEEAARHRGNSIKEAEQAAEEFDaKTHALLDWLAVEEQKLKASG-----------LDEVEGVKQEMDEAKG 4575
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDlgkdlesveelLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 4576 RYQECLKKGEEILSKCQPAAEPILRNWMRVVEARWKEVSEKVDEREFTLLE 4626
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
303-409 |
1.36e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 81.53 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 303 SDATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGV 382
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQL--AFDIAEKEFGI 78
|
90 100
....*....|....*....|....*...
gi 1143463340 383 ERLLDAEDVDT-NNPDEKSIITYVSSLY 409
Cdd:cd21251 79 SPIMTGKEMASvGEPDKLSMVMYLTQFY 106
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
312-409 |
9.76e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 78.77 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 312 LLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSNTERLnnAFAAADREFGVERLLDAEDV 391
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQL--AFDVAEREFGIPPVTTGKEM 86
|
90
....*....|....*....
gi 1143463340 392 D-TNNPDEKSIITYVSSLY 409
Cdd:cd21250 87 AsAEEPDKLSMVMYLSKFY 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2999-3216 |
1.94e-16 |
|
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: 81.34 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2999 QQGKVEDAYRALLNWLEETEEMMeNRKKPSADAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEASSDEEKkaL 3078
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3079 GNKNAQIEDRYKDLLNSAVDRQRKLLDAVDLAERLQEVTIpLDSWLQSADKRLQALAKVPiTVEKAEEMIGEQEALQDEL 3158
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1143463340 3159 EHKSDDLKDVLEIAPMLASLVSVEDANSISGQVNQLEARARALDAGITNMRPLLESFL 3216
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
307-427 |
2.08e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 86.53 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWARRVTAGY-PRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKIssDSVSNTERLNN--AFAAADREFGVE 383
Cdd:COG5069 125 TKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVL--DLQKKNKALNNfqAFENANKVIGIA 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1143463340 384 RLLDAEDV-DTNNPDEKSIITYVSSLYNAL----PHEPEMSRLQKVQEE 427
Cdd:COG5069 203 RLIGVEDIvNVSIPDERSIMTYVSWYIIRFglleKIDIALHRVYRLLEA 251
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
760-933 |
5.93e-16 |
|
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: 80.18 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 760 LIAFVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVY 839
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 840 LRQMQSQWDWLLALSKCLEEHLRDALNLKSFMEEASDAEAWIQEQSVRLENNYNRTDfsLEEGERFLRELDEIKEILNKY 919
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD--LESVEELLKKHKELEEELEAH 158
|
170
....*....|....
gi 1143463340 920 HQVLMALTERCASI 933
Cdd:cd00176 159 EPRLKSLNELAEEL 172
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
307-411 |
8.89e-16 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 75.74 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDwNKISSDSVSNTERLNNAFAAADREFGVERLL 386
Cdd:cd21184 1 SGKSLLLEW---VNSKIPEYKVKNFTTDWNDGKALAALVDALKPGLIP-DNESLDKENPLENATKAMDIAEEELGIPKII 76
|
90 100
....*....|....*....|....*
gi 1143463340 387 DAEDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21184 77 TPEDMVSPNVDELSVMTYLSYFRNA 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2320-3042 |
2.11e-15 |
|
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: 84.34 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2320 VEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLKS 2399
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2400 RFGGVDKALEKLKgilEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNS 2479
Cdd:TIGR02168 328 LESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2480 AENELElaaPIAAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEELKKKPDAELKKKLELLYQKWPKALGAARDRK 2559
Cdd:TIGR02168 405 LEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2560 DLVSKAGDLVkqfgDQVQALEQRLQGDQAELDELLASDK---AHDPEVCDALKL-------VELTMARRLAD--VDALNA 2627
Cdd:TIGR02168 482 RELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsGILGVLSELISVdegyeaaIEAALGGRLQAvvVENLNA 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2628 VMNRIESSAPgpdaNRLRRRADTLSDDAKGMAKKARTAADLAQRkqglaKKFERLCDEVSQFTENQKAEIQD-----AIE 2702
Cdd:TIGR02168 558 AKKAIAFLKQ----NELGRVTFLPLDSIKGTEIQGNDREILKNI-----EGFLGVAKDLVKFDPKLRKALSYllggvLVV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2703 KDLLNAERVQSKLNKI-------DDFWS-----------------SNSRELKNVGDEI-----KIDATPEDAQAVDTKLA 2753
Cdd:TIGR02168 629 DDLDNALELAKKLRPGyrivtldGDLVRpggvitggsaktnssilERRREIEELEEKIeeleeKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2754 ELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKINSLVAEIADLDPIGRS-RDELQKQKKEVVELAGDLGSAQ 2832
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2833 TKMLELGAEWEaALGAGIVAQpvfemnRAATDELNKLAARAGKRLAQREKKITETEDEIDKLHADADQIVGALEAIAKD- 2911
Cdd:TIGR02168 789 AQIEQLKEELK-ALREALDEL------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEi 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2912 EALQGAPSQLLDP-KQVSEKVRQLKESLKPVGEKMDAFNTDckllIKTAgpESDTKELDSLLKKVGDAYSDVVGKVSDKE 2990
Cdd:TIGR02168 862 EELEELIEELESElEALLNERASLEEALALLRSELEELSEE----LREL--ESKRSELRRELEELREKLAQLELRLEGLE 935
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 2991 MSVDaavQQQGKVEDAYRALLnwleetEEMMENRKKPSADAKVAKAQLHDYE 3042
Cdd:TIGR02168 936 VRID---NLQERLSEEYSLTL------EEAEALENKIEDDEEEARRRLKRLE 978
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1633-2483 |
1.77e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1633 RIDEARFEAKSLMDEV-------IREESRLKtigaSVLKIEQEISAMRDDVRASgstddvgiSVDEVYETRRRVEDDYMQ 1705
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAkktetgkAEEARKAE----EAKKKAEDARKAEEARKAE--------DARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1706 LLRQCQDLISFQNRLHAMNDEHSEQARRADEWLQMLQ-NDVEDVDQDPRFQRDEDrIQRIEELNRMA-AGGSSQLDDAEQ 1783
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAEDARKAEAARKAEE-ERKAEEARKAEdAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1784 ASRRLLTALEGTNVANDVRARHEELANLRRGKHQKVIDRlsqnmmeaASRKAEAEGVKQAVENLRQWSEQTAQRTRQPVQ 1863
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--------AEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1864 LpltELDLHEARKDEQvLHGEIENRLALIEELEKKAADVGDHASLAELQECKMKLKRSNSDLKGLRDnifdainglQTVN 1943
Cdd:PTZ00121 1307 A---KKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1944 SEGETLSRAVDSAGAKIRSARlpEAQSEVEALQDQADNLERITNNLCNIPNVTRTEPVIQKSKDLRKRVDSCAQELDARm 2023
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK- 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2024 gKLAElESLDAEfdGAKNKLSSFIGAFDDELKGLEKVSIDK-EKLAEQRRQTQDLVDKHSEGNAILDDVEAIAQKVTAED 2102
Cdd:PTZ00121 1451 -KKAE-EAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2103 PSKTGSAQKSVGELGARLQRQASELKaRGDKINKLDSKATSFAESEAAVLGYIEKQKDQLSTgfpvPATKEGVKSQLLDL 2182
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK----KAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2183 ERMNKTGKEEQRRVDDARHSARELAREASVEKEVQDMNQREKKlldewedladqfdavrsRANKAEQVLNEcaqmEKYIG 2262
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-----------------EKKKAEELKKA----EEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2263 AKKnmlegigapSTEPGVAKANRAQIQSMKAETEGEKSALEHVNSLANEliadgGANVEELMKKMDRLNRKWHSLESGLD 2342
Cdd:PTZ00121 1661 IKA---------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEKKKAEELKKAEE 1726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2343 ENAGRVEEAAKLGQELKDIQKELRKELGElesnvekasamssndiGDQLATLDSLKsrfggvDKALEKLKGILEATEELE 2422
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEE----------------KKKIAHLKKEE------EKKAEEIRKEKEAVIEEE 1784
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 2423 VDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENE 2483
Cdd:PTZ00121 1785 LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3434-3653 |
3.79e-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: 74.79 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3434 RAVLDDLQYLIEWFSAArERILEGAPPSLDLEVLKSQLKHQRITNEEASANKVQFRNVAGEAKKVARqlgmEGNEANEKI 3513
Cdd:cd00176 3 QQFLRDADELEAWLSEK-EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE----EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3514 SDTVDEGKELVEEVMALCADRTETLERALALMEQLtSQFDELNKWLDQMDAELQASPSVTTATpaaELREMHDHNEELAR 3593
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLE---SVEELLKKHKELEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3594 MVAAYRPIIEGFKSDVGSLHEVLAEDQAPLLESVAGELVQGYEEVREAVRARGHAIDNMM 3653
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2320-2894 |
4.96e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2320 VEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASA---MSSNDIGDQLATLDS 2396
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2397 LKSRFGGVDKALEKLKG-ILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIG 2475
Cdd:COG1196 307 LEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2476 TVNSAENE-LELAAPIAAESLKLADELKRAEELFQKLIENEGDvsLIRAKVAEELKKKPDAELKKKLELLYQKwpkALGA 2554
Cdd:COG1196 387 ELLEALRAaAELAAQLEELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEEEALEEAAEEEAELEEE---EEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2555 ARDRKDLVSKAgdlvKQFGDQVQALEQRLQGDQAELDELLASDKAHDPEVCDALKLVELTMARRLA-DVDALNAVMNRIE 2633
Cdd:COG1196 462 LELLAELLEEA----ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2634 SSAPGPDANRLRRRADTLSDDAkgmakkARTAADLAQRKQGLAKKFERLCDEVSQFTENQKAEIQDAIEKDLLNAERVQS 2713
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVA------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2714 KLNKIDDFWSSNSRELKNVGDEIKIDATPEDAQAVDTKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGK 2793
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2794 INSLVAEIADLDpigRSRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEAALgagivaqpvfEMNRAATDELNKLAARA 2873
Cdd:COG1196 692 ELELEEALLAEE---EEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL----------LEEEELLEEEALEELPE 758
|
570 580
....*....|....*....|.
gi 1143463340 2874 GKRLAQREKKITETEDEIDKL 2894
Cdd:COG1196 759 PPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2171-3051 |
1.50e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2171 TKEGVKSQLLDLERMNKTGKE------EQRRVDDARHSARELAREASVEKEVQDMNQREKKLLDEWEDLADQFDAVR--S 2242
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDfdfdakEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARkaE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2243 RANKAEQVLNecAQMEKYIGAKKNMLEG----IGAPSTEPGVAKANRAQIQSMKAEtegEKSALEHVNSLANELIADGGA 2318
Cdd:PTZ00121 1138 DARKAEEARK--AEDAKRVEIARKAEDArkaeEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAARKAEEER 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2319 NVEELMKKMDRlnRKWHSLESGldENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLK 2398
Cdd:PTZ00121 1213 KAEEARKAEDA--KKAEAVKKA--EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2399 SRFGGVDKALEKLKGILEATEELEvDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVN 2478
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2479 SAENELELAAPIAAESLKLADELKRAEELFQKLIENEgdvsliraKVAEELKKKpdAELKKKLEllyqkwpkalgAARDR 2558
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK--------KKADELKKA--AAAKKKAD-----------EAKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2559 KDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDELLASdKAHDPEVCDALKlveltmarrladvdalnavmnriESSAPG 2638
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK-KAEEAKKADEAK-----------------------KKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2639 PDANRLRRRAdtlsDDAKGMAKKARTAADlAQRKQGLAKKFE--RLCDEVSQFTENQKA-EIQDAIEKDLLNAERVQSKL 2715
Cdd:PTZ00121 1483 KKADEAKKKA----EEAKKKADEAKKAAE-AKKKADEAKKAEeaKKADEAKKAEEAKKAdEAKKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2716 NKIDDfwsSNSRELKNVGDEikiDATPEDAQAVDTKLAELQAGIDGLLATLQEQNVHLEE-KREQANRVQSESQKAAGKI 2794
Cdd:PTZ00121 1558 KKAEE---KKKAEEAKKAEE---DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEE 1631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2795 NSLVAEIadldpigRSRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEaalgagivAQPVFEMNRAATDElnKLAARAG 2874
Cdd:PTZ00121 1632 KKKVEQL-------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--------KKKAEEAKKAEEDE--KKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2875 KRLAQREKKITE----TEDEIDKLH----ADADQIVGALEAIAKDEALQGAPSQLLDPKQVSEKVRQLKeslKPVGEKMD 2946
Cdd:PTZ00121 1695 KKEAEEAKKAEElkkkEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK---KEEEKKAE 1771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2947 AFNTDCKLLIKTAGPESDTKELDSLLKKVGDAYSDVvgkvsdkemsvdAAVQQQGKVEDAYrallnwLEETEEMMENRKK 3026
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF------------ANIIEGGKEGNLV------INDSKEMEDSAIK 1833
|
890 900
....*....|....*....|....*
gi 1143463340 3027 PSADAKvaKAQLHDYEVLMKHVEDK 3051
Cdd:PTZ00121 1834 EVADSK--NMQLEEADAFEKHKFNK 1856
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2008-2837 |
1.78e-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: 77.79 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2008 LRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGAFDDELKGL-EKVSIDKEKLAEQRRQTQDLVDKHSEGNA 2086
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaNEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2087 ILDDVEA---IAQKVTAEDPSKTGSAQKSVGELGARLQRQASELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQLS 2163
Cdd:TIGR02168 324 QLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2164 TgfpvpatkegVKSQLLDLERMNKTGKEEQRRVDDARHSARELAREASVEKEvqdmNQREKKLLDEWEDLADQFDAVRSR 2243
Cdd:TIGR02168 404 R----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL----EEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2244 ANKAEQVLNECAQMEKYIGAKKNMLE------------------------GIGAP-----STEPG----VAKANRAQIQS 2290
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsGILGVlseliSVDEGyeaaIEAALGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2291 mkAETEGEKSALEHVNSLANEliADGGANVEELMKKMDRLnrkwhsLESGLDENAGRVEEAAKLGQELKDIQKELRKELG 2370
Cdd:TIGR02168 550 --VVVENLNAAKKAIAFLKQN--ELGRVTFLPLDSIKGTE------IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2371 ELESNV----EKASAM---SSNDIGDQLATLDSLKSRFGGV--DKALEKLKGILEATEELEVDATNRAEIQEQLETTQKK 2441
Cdd:TIGR02168 620 YLLGGVlvvdDLDNALelaKKLRPGYRIVTLDGDLVRPGGVitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2442 ADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELE-LAAPIAAESLKLADELKRAEELFQKLIENEgdvsl 2520
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqLEERIAQLSKELTELEAEIEELEERLEEAE----- 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2521 irakvaEELKkkpdaELKKKLELLYQKwpkalgaardrkdlvskagdlVKQFGDQVQALEQRLQGDQAELDELlasdkah 2600
Cdd:TIGR02168 775 ------EELA-----EAEAEIEELEAQ---------------------IEQLKEELKALREALDELRAELTLL------- 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2601 dpevcdalklveltmarrladvdalnavmnRIESSAPGPDANRLRRRadtlsddakgMAKKARTAADLAQRKQGLAKKFE 2680
Cdd:TIGR02168 816 ------------------------------NEEAANLRERLESLERR----------IAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2681 RLCDEVSQFTEnQKAEIQDAIEKDLLNAERVQSKLNKIDDFWSSNSRELKNVGDEI-----KIDATPEDAQAVDTKLAEL 2755
Cdd:TIGR02168 856 SLAAEIEELEE-LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRselrrELEELREKLAQLELRLEGL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2756 QAGIDGLLATLQEQ-NVHLEEKREQANRVQSESQKAAGKINSLVAEIADLDPIG-RSRDELQKQKKEVVELAG---DLGS 2830
Cdd:TIGR02168 935 EVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEEYEELKERYDFLTAqkeDLTE 1014
|
....*..
gi 1143463340 2831 AQTKMLE 2837
Cdd:TIGR02168 1015 AKETLEE 1021
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
309-410 |
2.22e-13 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 68.90 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 309 RDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSDSVSN-TERLNNAFAAADREF-GVERLL 386
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKkRENINLFLNACKKLGlPELDLF 80
|
90 100
....*....|....*....|....
gi 1143463340 387 DAEDVdTNNPDEKSIITYVSSLYN 410
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3989-4203 |
3.31e-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: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3989 KLASTIAQLTAWMDKTRATLKDIAPPKNavnLRDIEIAQCKLVVLSNDIHAHQDSVNAVNRAAQKYIQTSGALDAETSDS 4068
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDD---LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4069 LKSMNLKWEDIQKVLESLAFDMEVAKKEAENVGgEVEKWQRWLEETESALLSTKPtGGLPETAEFQLDEFKALKLDVEHN 4148
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 4149 ASPLEAHLHATEQHLKEEPQDADTWLSKTHGAMKTKWNKVKELLVDREKKLQVAY 4203
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1816-2484 |
1.69e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1816 HQKVIDRLSQNMMEAASRKAEAEGVKQAVENLRQWSEQTAQRTRQPVQLPLTELDLHEARKD------------------ 1877
Cdd:pfam15921 101 HEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEdmledsntqieqlrkmml 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1878 --EQVLHgeiENRLALIEELEKKAADVGDHASLAELQECKMK------LKRSNSDLKGLRDNIFDAINGLQTVNSEGETL 1949
Cdd:pfam15921 181 shEGVLQ---EIRSILVDFEEASGKKIYEHDSMSTMHFRSLGsaiskiLRELDTEISYLKGRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1950 -----------------SRAVDSAG--AKIRSAR--LPEAQSEVEALQDQADNLERITnnLCNIPNVTRTepVIQKSKDL 2008
Cdd:pfam15921 258 ielllqqhqdrieqlisEHEVEITGltEKASSARsqANSIQSQLEIIQEQARNQNSMY--MRQLSDLEST--VSQLRSEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2009 R--KRV-DSCAQELDARMgKLAELESLDAEFDgaKNKLSSFIGAFDDELKGLEKVSIDKEK-LAEQRRQTQDLVDKHSeG 2084
Cdd:pfam15921 334 ReaKRMyEDKIEELEKQL-VLANSELTEARTE--RDQFSQESGNLDDQLQKLLADLHKREKeLSLEKEQNKRLWDRDT-G 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2085 NAI--------LDDVEAIAQKVTAedpskTGSAQKSvgELGARLQRQASELKARGDKINKLdSKATSFAESeaavlgyie 2156
Cdd:pfam15921 410 NSItidhlrreLDDRNMEVQRLEA-----LLKAMKS--ECQGQMERQMAAIQGKNESLEKV-SSLTAQLES--------- 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2157 kqkdqlstgfpvpaTKEGVKSQLLDLERMNKTGKEEQRRVDDARHSARELARE-ASVEKEVQDMNQREKKLLDEWEDLAD 2235
Cdd:pfam15921 473 --------------TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAiEATNAEITKLRSRVDLKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2236 QFDAVRSRANKAEQVLNECAQMEKYIGAKK----NMLEGIGAPSTEPGVAKANRAQIQSmkaETEGEKSALEHVNSLANE 2311
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRqqieNMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEFKILKDK 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2312 liadGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQL 2391
Cdd:pfam15921 616 ----KDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2392 ATLDSLKSRFGGVDKALEKLKGILEATEELEVDATNRA-EIQEQLETTQKKADELERKIENVKKAALNAQNEG--LELEK 2468
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKhfLKEEK 771
|
730
....*....|....*..
gi 1143463340 2469 -KLDELIGTVNSAENEL 2484
Cdd:pfam15921 772 nKLSQELSTVATEKNKM 788
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3659-3873 |
1.87e-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: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3659 FGERLETLVANLQGAADRLRENEGISaDPSVLESRLAENRSIVESLRDKQNAYDALKQTASELLASAPEgdaAAGDVENK 3738
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP---DAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3739 LNRLEKLWKEIEREAVDRGVLLEDVLDKAKHFWsELDSCQKAVDDLRNRLElVEPATGHPEQLADQQEIMAQVASEMERA 3818
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 3819 RPRIEALSIAGKQLADYVPDDEKAVIENQVANVRGGFSTITGLFAEKKRDLIAAM 3873
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2246-2459 |
5.02e-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: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2246 KAEQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVaKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMK 2325
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2326 KMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQkELRKELGELEsnvekaSAMSSNDIGDQLATLDSLKSRFGGVD 2405
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKE------AALASEDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2406 KALEKLKGILEATEEL------EVDATNRAEIQEQLETTQKKADELERKIENVKKAALNA 2459
Cdd:cd00176 153 EELEAHEPRLKSLNELaeelleEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3879-3981 |
5.90e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.04 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLLKMspvEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAADAPPHlAATVRQP 3958
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASE---DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEER 78
|
90 100
....*....|....*....|...
gi 1143463340 3959 VADLNTRWSRLNAALAEREHKLE 3981
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3796-3984 |
6.60e-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: 68.24 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3796 GHPEQLADQQEIMAQVASEMERARPRIEALSIAGKQLADYVPDDeKAVIENQVANVRGGFSTITGLFAEKKRDLIAAMEe 3875
Cdd:cd00176 30 DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERLEELNQRWEELRELAEERRQRLEEALD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3876 AMTFHGDLQELLKWLDMAEQKLLKMspvEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAADAPPHLAATV 3955
Cdd:cd00176 108 LQQFFRDADDLEQWLEEKEAALASE---DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEI 184
|
170 180
....*....|....*....|....*....
gi 1143463340 3956 RQPVADLNTRWSRLNAALAEREHKLENLM 3984
Cdd:cd00176 185 EEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
305-412 |
1.96e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.53 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 305 ATSARDALLQWARRVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISsdSVSNTERLNNAFAAADREFGVER 384
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQ--GLGALEATAWALKVAENELGITP 78
|
90 100
....*....|....*....|....*...
gi 1143463340 385 LLDAEDVDTNNpDEKSIITYVSSLYNAL 412
Cdd:cd21196 79 VVSAQAVVAGS-DPLGLIAYLSHFHSAF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2358-3159 |
2.09e-11 |
|
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: 70.86 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2358 LKDIQKELRKELGELESNVEKASAMSsnDIGDQL--ATLDSLKSRFGGVDKALEKLKGILEATEELEVDATNR-AEIQEQ 2434
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYK--ELKAELreLELALLVLRLEELREELEELQEELKEAEEELEELTAElQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2435 LETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAAPIAAESLKLADELK-RAEELFQKLIE 2513
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2514 NEGDVSLIRAKVAEELKKKPdaELKKKLELLYQKWpkaLGAARDRKDLVSKAGDLVKQF---GDQVQALEQRLQGDQAEL 2590
Cdd:TIGR02168 349 LKEELESLEAELEELEAELE--ELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIerlEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2591 DELLASDKAHDPEVCDA-----------LKLVELTMARRLADVDALNAVMNRIESSAPGpDANRLRRRADTLSDDAKGMA 2659
Cdd:TIGR02168 424 EELLKKLEEAELKELQAeleeleeeleeLQEELERLEEALEELREELEEAEQALDAAER-ELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2660 KKARTAADLAQRKQGLAKKFERLCDEVSqFTENQKAEIQDAIEKDLLNAerVQSKLNKIDDFWSSNSRelKNVGDEIKID 2739
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLSGILGVLSELIS-VDEGYEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQ--NELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2740 ATPEDAQAVDTKLAELQAGIDGLLATLQEqnvhLEEKREQAnrvqsesQKAAGKINSLVAEIADLDpigrSRDELQKQKK 2819
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKD----LVKFDPKL-------RKALSYLLGGVLVVDDLD----NALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2820 E---VVELAGDLgsaqtkmleLGAEWEAALGAGIVAQPVFEmNRAATDELNKLAARAGKRLAQREKKITETEDEIDKLHA 2896
Cdd:TIGR02168 643 PgyrIVTLDGDL---------VRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2897 DADQIVGALEAIAKDEALQGAPSQLLDPK--QVSEKVRQLKESLKPVGEKMDAFNTDC-KLLIKTAGPESDTKELDSLLK 2973
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEveQLEERIAQLSKELTELEAEIEELEERLeEAEEELAEAEAEIEELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2974 KVGDAYSDVVGKVSDKEMSV----DAAVQQQGKVEDAYRALLNWLEETEEMMENRKKPSADAKVAKAQLHDYEVLMKHVE 3049
Cdd:TIGR02168 793 QLKEELKALREALDELRAELtllnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3050 DKKPSVDGFKAMIEKIVAEASSDEEKkaLGNKNAQIEDRYKDLLNSAvDRQRKLLdaVDLAERLQEVTIPLDSWLQSADK 3129
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEE--LSEELRELESKRSELRREL-EELREKL--AQLELRLEGLEVRIDNLQERLSE 947
|
810 820 830
....*....|....*....|....*....|
gi 1143463340 3130 RLQALAKVPITVEKAEEMigEQEALQDELE 3159
Cdd:TIGR02168 948 EYSLTLEEAEALENKIED--DEEEARRRLK 975
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
310-412 |
3.72e-11 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 63.86 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 310 DALLQWARRVTAGYpRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKI---------------------SSDSVSNTER 368
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIrqpttqtvdraqdeaedfwvaEFSPSTGDSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1143463340 369 LNNAFAAADRE-F-----------GVERLLDAEDVDTNNPDEKSIITYVSSLYNAL 412
Cdd:cd21224 82 LSSELLANEKRnFklvqqavaelgGVPALLRASDMSNTIPDEKVVILFLSYLCARL 137
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2322-2939 |
5.51e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2322 ELMKKMDRLnRKWHSLESGLDENAGRVEEaaKLGQELKDIqKELRKELGELESNVEKASAmssndigdQLATLDSLKSRF 2401
Cdd:PRK03918 173 EIKRRIERL-EKFIKRTENIEELIKEKEK--ELEEVLREI-NEISSELPELREELEKLEK--------EVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2402 GGVDKALEKLKGILEATEELEVdatnraEIQEQLETTQKKADELERKIENVKKAALNAQnEGLELEKKLDELIGTVNSAE 2481
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIR------ELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2482 NELElaapiaaeslKLADELKRAEELFQKLIENEGDVslirakvaEELKKKpDAELKKKLELLyQKWPKALgaardrkdl 2561
Cdd:PRK03918 314 KRLS----------RLEEEINGIEERIKELEEKEERL--------EELKKK-LKELEKRLEEL-EERHELY--------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2562 vskagDLVKQFGDQVQALEQRLQGDQAE-LDELLASDKAHDPEVCDALKLVELTMARRLADVDALNAVMNRIESsAPG-- 2638
Cdd:PRK03918 365 -----EEAKAKKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-AKGkc 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2639 PDANRLrrradtLSDDAKG--MAKKARTAADLAQRKQGLAKKFERLcdevsqftENQKAEIQDAIEKdllnaERVQSKLN 2716
Cdd:PRK03918 439 PVCGRE------LTEEHRKelLEEYTAELKRIEKELKEIEEKERKL--------RKELRELEKVLKK-----ESELIKLK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2717 KIDDFWSSNSRELKNVGDEiKIDATPEDAQAVDTKLAELQAGIDGL-------------LATLQEQNVHLEEKREQANRV 2783
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLkkelekleelkkkLAELEKKLDELEEELAELLKE 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2784 QSEsqKAAGKINSLVAEIADLDPIGRSRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEAALGA------------GIV 2851
Cdd:PRK03918 579 LEE--LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRleelrkeleeleKKY 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2852 AQPVFEMNRAATDELNKLAARAGKRLAQREKKITETEDEIDKLHADADQIVGALEAIAKDEalqgapSQLLDPKQVSEKV 2931
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE------KALERVEELREKV 730
|
....*...
gi 1143463340 2932 RQLKESLK 2939
Cdd:PRK03918 731 KKYKALLK 738
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2204-2807 |
8.45e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2204 RELAREASVEKEVQDMNQREKKL-----LDEWEDLADQFDAVRSRANKAEQVLNEcaqmekyigakknmlegigapstep 2278
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELeaellLLKLRELEAELEELEAELEELEAELEE------------------------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2279 gvakaNRAQIQSMKAETEGEKSALEHVNSLANELIAD---GGANVEELMKKMDRLNRKWHSLESGLDENAGRVEE----A 2351
Cdd:COG1196 258 -----LEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELEEELAEleeeL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2352 AKLGQELKDIQKELRKELGELES------NVEKASAMSSNDIGDQLATLDSLKSR-FGGVDKALEKLKGILEATEELEVD 2424
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEaeaelaEAEEALLEAEAELAEAEEELEELAEElLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2425 ATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAAPIAAESLKLADELKRA 2504
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2505 EELFQKLIENEGDvsliRAKVAEELKKKPDAELKKKLELLYQKWPKALGAARDRKDLVSKAGDLVKQFGD---QVQALEQ 2581
Cdd:COG1196 493 LLLLLEAEADYEG----FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVaaaAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2582 RLQGDQAELDELLASDKAHDPEVCDALKLVELTMARRLADVDALNAVMNRIESSAPGPDANRLRRRADTLSDDAKGMAKK 2661
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2662 ARTAADLAQRKQGLAKKFERLCDEVSQFTENQKAEIQDAIEKDLLNAERVQSKLNKIDDfwSSNSRELKNVGDEIKIDAT 2741
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER--ELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143463340 2742 PEDAQAVDTKLAELQAGIDGLLATLQEQNVHLEEKREQANRvqsesqkaagKINSLVAEIADLDPI 2807
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER----------ELERLEREIEALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1847-2593 |
1.01e-10 |
|
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: 68.93 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1847 LRQWSEQTAQRTRQPVQLPLTELDLHEARKDEQVLHGEIENRLALIEELEKKAADVGD--HASLAELQECKMKLKRSNSD 1924
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1925 LKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAKIRsarlpEAQSEVEALQDQADNLERITNNLcnipnVTRTEPVIQK 2004
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLE-----ELKEELESLEAELEELEAELEEL-----ESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2005 SKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGAFDDELKGLEKVSIdKEKLAEQRRQTQDLVDKHSEG 2084
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL-QAELEELEEELEELQEELERL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2085 NAILDDV-EAIAQKVTAEDPsktgsaqksvgelgarLQRQASELKARGDKINKLDSKATSFAESEAAVLgyieKQKDQLS 2163
Cdd:TIGR02168 460 EEALEELrEELEEAEQALDA----------------AERELAQLQARLDSLERLQENLEGFSEGVKALL----KNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2164 TGFpvpatkeGVKSQLLdlermnKTGKEEQRRVDDARHSARELA---REASVEKEVQDMNQREKK-----LLDEWEDLAD 2235
Cdd:TIGR02168 520 GIL-------GVLSELI------SVDEGYEAAIEAALGGRLQAVvveNLNAAKKAIAFLKQNELGrvtflPLDSIKGTEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2236 QFDAVRSRANKaEQVLNECAQMEKYIGAKKNMLEGIGApstepGVAKANR-AQIQSMKAETEGEKSALehvnSLANELIA 2314
Cdd:TIGR02168 587 QGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYLLG-----GVLVVDDlDNALELAKKLRPGYRIV----TLDGDLVR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2315 DGGA-NVEELMKKMDRLNRKwhsleSGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAM---SSNDIGDQ 2390
Cdd:TIGR02168 657 PGGViTGGSAKTNSSILERR-----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleeLSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2391 LATLDSLKSRFGGVDKALEKLKG-ILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKK 2469
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKeLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2470 LDELIGTVNSAENELElaapiaAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEElkKKPDAELKKKLELLYQKWP 2549
Cdd:TIGR02168 812 LTLLNEEAANLRERLE------SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL--EELIEELESELEALLNERA 883
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1143463340 2550 KALGAARDRKDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDEL 2593
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
312-406 |
1.28e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 61.25 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 312 LLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNKIS-SDSVSNTERlnnAFAAADREFGVERLLDAE 389
Cdd:cd21229 8 MLAW---LQAVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDpSNSLENCRR---AMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1143463340 390 DVDTNNPDEKSIITYVS 406
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4075-4658 |
2.12e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4075 KWEDIQKVlESLAFDMEVAKKEAENVGGEVEKWQRWLEETESALLSTKPTGGLPETAE--FQLDEF-KALKLDVEHNASP 4151
Cdd:PTZ00121 1219 KAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEeaRKADELkKAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4152 LEAHLHATEQHLKEEPQDADTWLSKTHGAMKTKWNKVKELLVDREKKLQVAYEQAVALESALNDMEDWIIAAERKLTDQp 4231
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA- 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4232 siSRLPDVIEKQlAEHESWMEEvAGRKMAMTKHQASGVHmQYYCEKKDAIPIKNRLVSLKHRVE-KISGRTAERAKQLAV 4310
Cdd:PTZ00121 1377 --KKKADAAKKK-AEEKKKADE-AKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4311 TRDEVATWQDGLHDLEHF-ISDVLVKIAPEPNTTsslEKLKAKLEEVK----EAQRDVTAKQTLFDVTRKRGIGLAERAT 4385
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKA---DEAKKKAEEAKkkadEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4386 RSEYKQISMTNEKMS-KKWAEMLKKLRDRLREAEQAVLEGGAFEESMNDLESWVDDELERYQKAEHEPVFADIDGVRALV 4464
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4465 DEESRRSAERKTKENGVKtvvkKADalmasgvDEKDSIAQAKERLVEKWNQVEEAAR-HRGNSIKEAEQAAEEFDAKTHA 4543
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELK----KAE-------EEKKKVEQLKKKEAEEKKKAEELKKaEEENKIKAAEEAKKAEEDKKKA 1677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4544 LLDWLAVEEQKLKASGLDEVEGVKQEMDEAKGRYQECLKKGEEIlskcQPAAEpilRNWMRVVEARWKEVSEKVDEREFT 4623
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL----KKAEE---ENKIKAEEAKKEAEEDKKKAEEAK 1750
|
570 580 590
....*....|....*....|....*....|....*
gi 1143463340 4624 LLEQEQKAKEQNEQIEKlaKFAAQKREELNRMIEQ 4658
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEE--KKAEEIRKEKEAVIEE 1783
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1686-2473 |
2.49e-10 |
|
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: 67.39 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1686 GISVDEVYETRRRVEDDYMQLLRQCQDLISFQNRLHA----MNDEHSEQARRADEW---LQMLQNDVEDVDQDPRFQRde 1758
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEkleeLRLEVSELEEEIEELqkeLYALANEISRLEQQKQILR-- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1759 driQRIEELNRMAAGGSSQLDDAEQASRRLLtalegtnvandvrarhEELANLrrgkhQKVIDRLSQNMMEAASRKAEAE 1838
Cdd:TIGR02168 309 ---ERLANLERQLEELEAQLEELESKLDELA----------------EELAEL-----EEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1839 GVKQAVENLRQWSEQTAQRTRQpvqlpltelDLHEARKDEQVLHGEIENRLALIEELEKKAADVGDHASLAELQECKMKL 1918
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRS---------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1919 KRSNSDLKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAKIRSAR--LPEAQSEVEALQDQADNLERITNNLCNIPNVT 1996
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEreLAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1997 RTEP-------------------------------VIQKSKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSS 2045
Cdd:TIGR02168 516 SGLSgilgvlselisvdegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2046 FIGAFDDELKGLEKVSIDKEKLAEQRRQTQDLVDKHSEGNAILDDVEAIAQKVTAEDPSKTGS---AQKSVGELGARLQR 2122
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGgviTGGSAKTNSSILER 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2123 QaSELKARGDKINKLDSKAtsfAESEAAVLGYiEKQKDQLSTGFPVPATKEGVKSQLLDLERMN--KTGKEEQRRVDDAR 2200
Cdd:TIGR02168 676 R-REIEELEEKIEELEEKI---AELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDlaRLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2201 HSAREL----AREASVEKEVQDMNQREKKLLDEWEDL-------ADQFDAVRSRANKAEQVLNE-----------CAQME 2258
Cdd:TIGR02168 751 QLSKELteleAEIEELEERLEEAEEELAEAEAEIEELeaqieqlKEELKALREALDELRAELTLlneeaanlrerLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2259 KYIGAKKNMLEGIgapstepgvakanRAQIQSMKAETEGEKSALEHVNSLANELIADgganVEELMKKMDRLNRKWHSLE 2338
Cdd:TIGR02168 831 RRIAATERRLEDL-------------EEQIEELSEDIESLAAEIEELEELIEELESE----LEALLNERASLEEALALLR 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2339 SGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKAsamssndigdqLATLDSLKSRFGGvdkaleklkgilEAT 2418
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL-----------EVRIDNLQERLSE------------EYS 950
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 2419 EELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDEL 2473
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFL 1005
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2285-2817 |
4.45e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2285 RAQIQSMKAETEG--EKSALEHVNSLANELiADGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQ 2362
Cdd:PRK02224 186 RGSLDQLKAQIEEkeEKDLHERLNGLESEL-AELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2363 -----------------KELRKELGELESNVEKA---SAMSSNDIGDQLATLDSLKSRFGGVDKALEKLK-GILEATEEL 2421
Cdd:PRK02224 265 etiaeterereelaeevRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDRDEELRDRLEECRvAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2422 EVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELElaapiAAESLkLADEL 2501
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-----NAEDF-LEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2502 KRAEELFQKLIENEGDVSLIRAKVAE---------------ELKKKPDAElkkklellyqkwpkalgAARDRKDLVSKAG 2566
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEaealleagkcpecgqPVEGSPHVE-----------------TIEEDRERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2567 DLVKQFGDQVQALEQRLqgDQAEldellasdkahdpevcdalKLVELtmARRLADV-DALNAVMNRIESSAPGPDANR-- 2643
Cdd:PRK02224 482 AELEDLEEEVEEVEERL--ERAE-------------------DLVEA--EDRIERLeERREDLEELIAERRETIEEKRer 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2644 ---LRRRADTLSDDAKGMAKKARTAADLAQRKQGLAKKFERlcdevsqftenQKAEIQDAIEkdllNAERVQSKLNKIDD 2720
Cdd:PRK02224 539 aeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS-----------KLAELKERIE----SLERIRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2721 fwssNSRELKNVGDEIKIDATPEDAQAvdTKLAELQAGIDGLLATLQEQNVhlEEKREQANRVQSESQKAAGKINSLVAE 2800
Cdd:PRK02224 604 ----AEDEIERLREKREALAELNDERR--ERLAEKRERKRELEAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREE 675
|
570
....*....|....*..
gi 1143463340 2801 iadldpigrsRDELQKQ 2817
Cdd:PRK02224 676 ----------RDDLQAE 682
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
307-411 |
8.69e-10 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 58.93 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI----DWNKisSDSVSNTERlnnAFAAADREFGV 382
Cdd:cd21230 1 TPKQRLLGW---IQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDP--NDALENATE---AMQLAEDWLGV 72
|
90 100
....*....|....*....|....*....
gi 1143463340 383 ERLLDAEDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21230 73 PQLITPEEIINPNVDEMSVMTYLSQFPKA 101
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1711-2373 |
9.26e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.52 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1711 QDLISFQNRLHAMNDEHSEQA--RRADEWLQ-----MLQNDVEDVDQDPRFQRD--EDRIQRIEELNRMAAGGS------ 1775
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDAMAdiRRRESQSQedlrnQLQNTVHELEAAKCLKEDmlEDSNTQIEQLRKMMLSHEgvlqei 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1776 -SQLDDAEQASRRLLTALE----------GTNVANDVRARHEELANLRrGKHQKVIDRLSqnmmeaaSRKAEAEgvkQAV 1844
Cdd:pfam15921 190 rSILVDFEEASGKKIYEHDsmstmhfrslGSAISKILRELDTEISYLK-GRIFPVEDQLE-------ALKSESQ---NKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1845 ENLRQWSEQTAQRTRQPVQLPLTELDLHEARKDEQVlhGEIENRLALIEELEKKAadvgDHASLAELQECKMKLKRSNSD 1924
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA--NSIQSQLEIIQEQARNQ----NSMYMRQLSDLESTVSQLRSE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1925 LKGLRDNIFDAINGLQT----VNSEgetlsravdsagakirsarLPEAQSEVEALQDQADNLERITNNLcnIPNVTRTEP 2000
Cdd:pfam15921 333 LREAKRMYEDKIEELEKqlvlANSE-------------------LTEARTERDQFSQESGNLDDQLQKL--LADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2001 VIQKSKDLRKR-----------VDSCAQELDARMGKLAELESL-DAEFDGAKNKLSSFIGAFDDELKGLEKVSidkeKLA 2068
Cdd:pfam15921 392 ELSLEKEQNKRlwdrdtgnsitIDHLRRELDDRNMEVQRLEALlKAMKSECQGQMERQMAAIQGKNESLEKVS----SLT 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2069 EQRRQTQDLVDKHSEgnailddvEAIAQKVTAEdpsktgSAQKSVGELGARLQRQASELKARGDKINKLDSKAtsfaESE 2148
Cdd:pfam15921 468 AQLESTKEMLRKVVE--------ELTAKKMTLE------SSERTVSDLTASLQEKERAIEATNAEITKLRSRV----DLK 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2149 AAVLGYIEKQKDQLSTgfpVPATKEGVKSQLLDLERMNKTGKEE-----QRRVDDARHSARELAREASVEKEVQD--MNQ 2221
Cdd:pfam15921 530 LQELQHLKNEGDHLRN---VQTECEALKLQMAEKDKVIEILRQQienmtQLVGQHGRTAGAMQVEKAQLEKEINDrrLEL 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2222 REKKLLDEWEDL-----------------------ADQFDAVRSRANKAEQVLNECAQ--------MEKYIGAKKNMLEg 2270
Cdd:pfam15921 607 QEFKILKDKKDAkirelearvsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKTsrnelnslSEDYEVLKRNFRN- 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2271 igapSTEPGVAKANRAQIQSMKAETEGEKSAlehvNSLANELIADGGA-NVEELMKK--------MDRLNRKWHSLESGL 2341
Cdd:pfam15921 686 ----KSEEMETTTNKLKMQLKSAQSELEQTR----NTLKSMEGSDGHAmKVAMGMQKqitakrgqIDALQSKIQFLEEAM 757
|
730 740 750
....*....|....*....|....*....|....*..
gi 1143463340 2342 dENAGR-----VEEAAKLGQELKDIQKELRKELGELE 2373
Cdd:pfam15921 758 -TNANKekhflKEEKNKLSQELSTVATEKNKMAGELE 793
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
310-408 |
1.36e-09 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 58.08 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 310 DALLQWARRVTagyPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDWNKISSD-SVSNTERlnnAFAAAdREFGVERLLDA 388
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEeSENNIQR---GLEAG-KSLGVEPVLTA 76
|
90 100
....*....|....*....|
gi 1143463340 389 EDVDTNNPDEKSIITYVSSL 408
Cdd:cd21185 77 EEMADPEVEHLGIMAYAAQL 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2420-3161 |
2.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2420 ELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAAPIA---AESLK 2496
Cdd:PTZ00121 1049 DEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDAR 1128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2497 LADELKRAEElfqklienegdvslirAKVAEELKKKPDAelkkklellyQKWPKALGAARDRKDLVSKAGDLVKQFGDQV 2576
Cdd:PTZ00121 1129 KAEEARKAED----------------ARKAEEARKAEDA----------KRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2577 QALEQRLQGDQAELDELLASDKAHDPEvcDALKLVEltmARRLADVDALNAVMNRIESSAPGPDAnrlrRRADTLSDDAK 2656
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAE--EERKAEE---ARKAEDAKKAEAVKKAEEAKKDAEEA----KKAEEERNNEE 1253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2657 GMAKKARTAADLAQRKQGLAKKFERLCDEVSQFTENQKA-EIQDAIEKDLLNAERVQSKLNKIDDFWSSNSRELKNVGDE 2735
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2736 IKIDATpEDAQAVDTKLAELQAGIDGLLATlqeqnvhlEEKREQANRVQSESQKAAGKINSLVAEIADLDPIGRSRDELQ 2815
Cdd:PTZ00121 1334 AKKKAE-EAKKAAEAAKAEAEAAADEAEAA--------EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2816 KQKKEVVELAgdlgSAQTKMLELGAEWEAALGAGIVAQPVFEMNRAatDELNKLAARAGKrlAQREKKITETEDEIDKLH 2895
Cdd:PTZ00121 1405 KKADELKKAA----AAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKK--AEEAKKKAEEAKKADEAK 1476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2896 ADADQIVGALEAIAKDEALQGAPSQLLDPKQVSEKVRQLK--------ESLKPVGEKMDAfntdcklliKTAGPESDTKE 2967
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkaeeakkaDEAKKAEEAKKA---------DEAKKAEEKKK 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2968 LDSLLKKVGDAYSDVVGKVSDKEMSVDAAVQQQGKVEDAYRALLNWLEETEEMMENRKKPSAD-------AKVAKAQLHD 3040
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakkaeeAKIKAEELKK 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3041 YEVLMKHVEDKKPSVDGFKAMIEKIVAEASSDEEKKALGNKNAQIEDRYKDLLNSAVDRQRKLLDAV----DLAERLQEV 3116
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeaEEAKKAEEL 1707
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3117 TIPLDSWLQSADKRLQALAKVPITVEKA-----EEMIGEQEALQDELEHK 3161
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAkkeaeEDKKKAEEAKKDEEEKK 1757
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2248-2821 |
2.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2248 EQVLNECAQMEKYIGAKKNMLEgigapstepgVAKANRAQIQSMKAETEGEKSAlehvnslaNELIADGGANVEELMKKM 2327
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNLGE----------VIKEIKRRIERLEKFIKRTENI--------EELIKEKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2328 DRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKasamssndigdqlatLDSLKSRFGGVDKA 2407
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK---------------IRELEERIEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2408 LEKLKGILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELiGTVNSAENELELA 2487
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2488 APIAAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEELKKKPDAELKKKLELLYQKWPKALGAARDRKDLVSK--- 2564
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkk 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2565 ----------------AGDLVKQFGDQVQALEQRLQGDQAELDELLASDKAHDPEVCDALKLVEL-TMARRLADVDALNA 2627
Cdd:PRK03918 434 akgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2628 VMNRIESSAPGPDANRLRRRADTLSDDAKGMAKKARTAADLAQRKQGLAKKFERLcdevsqftENQKAEIQDAI-EKDLL 2706
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL--------EEELAELLKELeELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2707 NAERVQSKLNKIDDFWsSNSRELKNVGDEI-----KIDATPEDAQAVDTKLAELQAGIDGLLATLQEQNVHL--EEKREQ 2779
Cdd:PRK03918 586 SVEELEERLKELEPFY-NEYLELKDAEKELereekELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseEEYEEL 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1143463340 2780 ANRVQSESQKAAGK------INSLVAEIA-DLDPIGRSRDELQKQKKEV 2821
Cdd:PRK03918 665 REEYLELSRELAGLraeleeLEKRREEIKkTLEKLKEELEEREKAKKEL 713
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4205-4420 |
3.37e-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: 60.15 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4205 QAVALESALNDMEDWIIAAERKLTDQPSISRLPDViEKQLAEHESWMEEVAGRKMAMTKHQASGVHM--QYYCEKKDaip 4282
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLieEGHPDAEE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4283 IKNRLVSLKHRVEKISGRTAERAKQLAVTRDEVATWQDgLHDLEHFISDVLVKIAPEPnTTSSLEKLKAKLEEVKEAQRD 4362
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1143463340 4363 VTAKQTLFDVTRKRGIGLAERATRSEYKQISMTNEKMSKKWAEMLKKLRDRLREAEQA 4420
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1655-2387 |
3.94e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1655 LKTIGASVLKI----EQEISAMRDDVrasgstddvgISVDEVYETRRRVEDDYMQLLRQcqdliSFQNRLHAMNDEH--- 1727
Cdd:pfam15921 215 FRSLGSAISKIlrelDTEISYLKGRI----------FPVEDQLEALKSESQNKIELLLQ-----QHQDRIEQLISEHeve 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1728 ----SEQARRADEWLQMLQNDVEDVDQDPRFQ----------------------RDEDRI--QRIEELNRMAAGGSSQLD 1779
Cdd:pfam15921 280 itglTEKASSARSQANSIQSQLEIIQEQARNQnsmymrqlsdlestvsqlrselREAKRMyeDKIEELEKQLVLANSELT 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1780 DAE-------QASRRLLTALEgtNVANDVRARHEELAnLRRGKHQKVIDRLSQNMM-------EAASRKAEAEGVKQAVE 1845
Cdd:pfam15921 360 EARterdqfsQESGNLDDQLQ--KLLADLHKREKELS-LEKEQNKRLWDRDTGNSItidhlrrELDDRNMEVQRLEALLK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1846 NLRqwSEQTAQRTRQPVQLPLTELDLHEARKDEQVLHGEIENRLALIEELEKKAADVGDHASL-----AELQECKMKLKR 1920
Cdd:pfam15921 437 AMK--SECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltASLQEKERAIEA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1921 SNSDLKGLRDNIFDAINGLQTVNSEGETLsRAVDSAGAKIRsARLPEAQSEVEALQDQADNLERItnnlcnIPNVTRTEP 2000
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEGDHL-RNVQTECEALK-LQMAEKDKVIEILRQQIENMTQL------VGQHGRTAG 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2001 VIQKSK-DLRKRVDSCAQEL-------DARMGKLAELESLDAEFDGAKNKLssfIGAFDDELKGLEKVSIDKEKLAEQRR 2072
Cdd:pfam15921 587 AMQVEKaQLEKEINDRRLELqefkilkDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKDIKQERDQLLNEVK 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2073 QTQdlvdkhSEGNAILDDVEAIAQKVTaedpSKTGSAQKSVGELGARLQRQASELKARGDKINKL---DSKATSFAESEA 2149
Cdd:pfam15921 664 TSR------NELNSLSEDYEVLKRNFR----NKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegsDGHAMKVAMGMQ 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2150 AVLGYIEKQKDQLSTgfpvpatkegvKSQLLDlERMNKTGKEEQRRVDDARHSARELAREAS----VEKEVQDMNQREKK 2225
Cdd:pfam15921 734 KQITAKRGQIDALQS-----------KIQFLE-EAMTNANKEKHFLKEEKNKLSQELSTVATeknkMAGELEVLRSQERR 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2226 LLDEWEDLADQFDAVRSRANKAEQVLNECAQMEKYIGAKKNM----LEGIG---APSTEPGVAK-ANRAQIQSMKAETEG 2297
Cdd:pfam15921 802 LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLdvkeLQGPGytsNSSMKPRLLQpASFTRTHSNVPSSQS 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2298 EKSALEHVNSLANELIADGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKD--IQKELRKELGELESN 2375
Cdd:pfam15921 882 TASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDciIESSLRSDICHSSSN 961
|
810
....*....|..
gi 1143463340 2376 VEKASAMSSNDI 2387
Cdd:pfam15921 962 SLQTEGSKSSET 973
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3879-3982 |
8.56e-09 |
|
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 characteriztic 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: 56.17 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLlkmSPVEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQLAaDAPPHLAATVRQP 3958
Cdd:pfam00435 6 FFRDADDLESWIEEKEALL---SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQER 81
|
90 100
....*....|....*....|....
gi 1143463340 3959 VADLNTRWSRLNAALAEREHKLEN 3982
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4352-4771 |
2.00e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4352 KLEEVKEAQ--RDVTAKQTLFDVTRKRGIGLAERATRSE-------YKQISMTNEKMSKKWAEMLKKLRDRLREAEQAV- 4421
Cdd:PTZ00121 1165 KAEEARKAEdaKKAEAARKAEEVRKAEELRKAEDARKAEaarkaeeERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKk 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4422 LEGGAFEESMNDLESWVDDELERYQKAEHEPVFADIDGVRALvdEESRRSAERKTKENGVKTVVKKADALMASGVDE-KD 4500
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEaKK 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4501 SIAQAKERLVEKWNQVEEAARHRGNSIKEAEQAAEEFD-AKTHALLDWLAVEEQKLKASGLDEVEGVKQEMDEAKGRYQE 4579
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4580 CLKKGEEIlsKCQPAAEPILRNWMRVVEARWKEVSEKVDEREFTLLEQEQKAKEQNEQIEKLAKFAAQKR--EELNRMIE 4657
Cdd:PTZ00121 1403 DKKKADEL--KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkaDEAKKKAE 1480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4658 QppAQDLDTMEQNICDFANLDSELREQQPEVDAACKSAKKGARNPAAEMLSTEWKKlwlDAMGLQSSLDNQKAllEEMKR 4737
Cdd:PTZ00121 1481 E--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KADEAKKAEEKKKA--DELKK 1553
|
410 420 430
....*....|....*....|....*....|....
gi 1143463340 4738 LEGWKWEDWKeRYVEWNDHAKARVNDLFRRIDRL 4771
Cdd:PTZ00121 1554 AEELKKAEEK-KKAEEAKKAEEDKNMALRKAEEA 1586
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2199-2571 |
2.66e-08 |
|
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: 60.85 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2199 ARHSARELAREASVEKEVQDMNQREKKLLDEWEDLADQFDAVRSRANKAEQVLNECAQMEKYIGAKKNMLEGigAPSTEP 2278
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2279 GVAKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKMDRLNRKwhslesgldenagRVEEAAKLGQEL 2358
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS-------------RIPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2359 KDIQKELRKELGELEsnvekasamssndigdqlATLDSLKSRFGGVDKALEKLKGILEATEElevdatNRAEIQEQLETT 2438
Cdd:TIGR02169 804 EEEVSRIEARLREIE------------------QKLNRLTLEKEYLEKEIQELQEQRIDLKE------QIKSIEKEIENL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2439 QKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENEL-ELAAPIAAESLKLADELKRAEELFQKLIENEGD 2517
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIeELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 2518 VSLIRAKVAEELK-KKPDAELKKKLELLYQKWPKALGAARDRKDLVSKAGDLVKQ 2571
Cdd:TIGR02169 940 KGEDEEIPEEELSlEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2348-3352 |
4.19e-08 |
|
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: 60.08 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2348 VEEAAKLGQELKDIQKELRkELGELESNVEKASAMSSnDIGDQLATLDSLKsrfggvDKALE--KLKGILEATEELEVdA 2425
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALE-ELEEVEENIERLDLIID-EKRQQLERLRRER------EKAERyqALLKEKREYEGYEL-L 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2426 TNRAEIQEQLETTQKKADELERKIEnvkkaalnaqneglELEKKLDELIGTVNSAENEL-ELAAPIAAESLKLADELKRa 2504
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELE--------------KLTEEISELEKRLEEIEQLLeELNKKIKDLGEEEQLRVKE- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2505 eelfqKLIENEGDVSLIRAKVAEELKKKPDAELK-KKLELLYQKwpKALGAARDRKDLVSKAGDlVKQFGDQVQALEQRL 2583
Cdd:TIGR02169 295 -----KIGELEAEIASLERSIAEKERELEDAEERlAKLEAEIDK--LLAEIEELEREIEEERKR-RDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2584 QGDQAELDELlasDKAHDpevcdalKLVELTMARRladvDALNAVMNRIESsapgpdanrLRRRADTLSDDAKGM-AKKA 2662
Cdd:TIGR02169 367 EDLRAELEEV---DKEFA-------ETRDELKDYR----EKLEKLKREINE---------LKRELDRLQEELQRLsEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2663 RTAADLAQRKQGLAKKFERLCD---EVSQFTEN--QKAEIQDAIEKDLlnaERVQSKLNKIDDFWSSNSRELKNVGDEIK 2737
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDkalEIKKQEWKleQLAADLSKYEQEL---YDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2738 I--DATPEDAQAVDtklaELQAGIDGLLATLQEqnvhLEEKREqanRVQSESQKAAGkiNSLVAEIADLDPIGRSRDELQ 2815
Cdd:TIGR02169 501 AseERVRGGRAVEE----VLKASIQGVHGTVAQ----LGSVGE---RYATAIEVAAG--NRLNNVVVEDDAVAKEAIELL 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2816 KQKKevvelagdLGSAQ----TKMLELGAEWEAALGAGIVA------------QPVFEMNRAATDELNKLAAraGKRLAQ 2879
Cdd:TIGR02169 568 KRRK--------AGRATflplNKMRDERRDLSILSEDGVIGfavdlvefdpkyEPAFKYVFGDTLVVEDIEA--ARRLMG 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2880 REKKITETEDEIDKLHAdadqIVGALEAiakdealqgAPSQLLDPKQVSEKVRQLKESLkpvgEKMDafntdckllikta 2959
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGA----MTGGSRA---------PRGGILFSRSEPAELQRLRERL----EGLK------------- 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2960 gpesdtKELDSLLKKVgdaysdvvgkvSDKEMSVDAAVQqqgKVEDAYRallnwleETEEMMENRKKPSADAKVAKAQLH 3039
Cdd:TIGR02169 688 ------RELSSLQSEL-----------RRIENRLDELSQ---ELSDASR-------KIGEIEKEIEQLEQEEEKLKERLE 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3040 DYEVLMKHVEDKKPSVdgfKAMIEKIVAEASSDEEKkaLGNKNAQIEDRYKDLLNSAVDRQRKLLDAVDlaerlqEVTIP 3119
Cdd:TIGR02169 741 ELEEDLSSLEQEIENV---KSELKELEARIEELEED--LHKLEEALNDLEARLSHSRIPEIQAELSKLE------EEVSR 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3120 LDSWLQSADKRLQALAkvpITVEKAEEMIGEQEALQDELEHKSDDLKDVLE-IAPMLASLVSVEDanSISGQVNQLEARA 3198
Cdd:TIGR02169 810 IEARLREIEQKLNRLT---LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnLNGKKEELEEELE--ELEAALRDLESRL 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3199 RALDAGITNMRPLLESFLQQIQDFTLDAEDMTQFVGETEVKLG----ELDELPIEPDDLVEQTNILAEIAVSIADRDEMM 3274
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3275 ANI--FEVGKQLAIQgEPEEAliaQKKLDDLKFRYADLMTSADEKIALLAKaipLSEGFHEGFdtvMQVLEDMDRDLQTI 3352
Cdd:TIGR02169 965 EEIraLEPVNMLAIQ-EYEEV---LKRLDELKEKRAKLEEERKAILERIEE---YEKKKREVF---MEAFEAINENFNEI 1034
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1519-2489 |
7.30e-08 |
|
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: 59.31 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1519 ESIDAATKNVQNVKQSLDSWRDRIKERLDEIDRLcteEGDSLTPEQYSALREMRRQ-----LADEYDTVLRTVEGIHTRL 1593
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERL---RREREKAERYQALLKEKREyegyeLLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1594 nilsalliefssvtSSMQSWMTDRTRLAGDIRHKSGDpmRIDEARFEAKSLMDEVIREESRLKTigaSVLKIEQEISAMR 1673
Cdd:TIGR02169 247 --------------ASLEEELEKLTEEISELEKRLEE--IEQLLEELNKKIKDLGEEEQLRVKE---KIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1674 DDVRASGStddvgiSVDEVYETRRRVEDDYMQLLRQCQDLISFQNRLHAMNDEHSEQARRADEWLQMLQNDVEDVDQDPR 1753
Cdd:TIGR02169 308 RSIAEKER------ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1754 FQRDE--DRIQRIEELNRmaaggssQLDDAEQASRRLLTALegtnvandvRARHEELANLR------RGKHQKVIDRLSQ 1825
Cdd:TIGR02169 382 ETRDElkDYREKLEKLKR-------EINELKRELDRLQEEL---------QRLSEELADLNaaiagiEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1826 NMMEAASRKAEAEGVKQAVENLRQWSEQTAQRTRQpVQLPLTELDLHEARKDEQVLHGEIENRLALIEELEKKAADVGDH 1905
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR-VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1906 ASLAELQECKMKLKRSNSDLKGLR-DNIF--------DAINGLQTVNsegetLSRAVDSAGAKIRSARLPEAQSEVEALQ 1976
Cdd:TIGR02169 525 GTVAQLGSVGERYATAIEVAAGNRlNNVVveddavakEAIELLKRRK-----AGRATFLPLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1977 DQADNLERITNNLCNIPNVTRTEPVIQKSKDLRKRVdscaqeldarMGKlAELESLDAE-FDgaknKLSSFIGAFDDELK 2055
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRL----------MGK-YRMVTLEGElFE----KSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2056 GLEKVSIDKEKLAEQRRQTQDLVDkhsEGNAILDDVEAIAQKVTA------EDPSKTGSAQKSVGELGARLQRQASELKA 2129
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKR---ELSSLQSELRRIENRLDElsqelsDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2130 RGDKINKLDSKATSFAESEAAVLGYIEKQKDQLSTgfpvpatkegVKSQLLDLERMnktgkEEQRRVDDARHSARELARE 2209
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHK----------LEEALNDLEAR-----LSHSRIPEIQAELSKLEEE 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2210 -ASVEKEVQDMNQREKKLLDEWEDLADqfdavrSRANKAEQVLnecaqmekYIGAKKNMlegigapstepgvakaNRAQI 2288
Cdd:TIGR02169 807 vSRIEARLREIEQKLNRLTLEKEYLEK------EIQELQEQRI--------DLKEQIKS----------------IEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2289 QSMKAETEGEKSALEHVNSLANELIADgganVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKE 2368
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESR----LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2369 LGELESNVEKASAMSSNDigdqlATLDSLKSRFGGVDKALEKLKGI-LEATEELEVDATNRAEIQEQLETTQKKADELER 2447
Cdd:TIGR02169 933 LSEIEDPKGEDEEIPEEE-----LSLEDVQAELQRVEEEIRALEPVnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 1143463340 2448 KIENVKKAALNAQNEGLE-LEKKLDELIGTVNSAENELELAAP 2489
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEAFEaINENFNEIFAELSGGTGELILENP 1050
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2341-2877 |
8.03e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2341 LDENA--GRVEEAAKLGQELKDIQKELRKE------LGELESNVEKASAMSsndigDQLATLDSLKSRFggvdKALEKLK 2412
Cdd:COG4913 218 LEEPDtfEAADALVEHFDDLERAHEALEDAreqielLEPIRELAERYAAAR-----ERLAELEYLRAAL----RLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2413 GILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLE-LEKKLDELIGTVNSAENELE------ 2485
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRArleall 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2486 --LAAPIAAESLKLADELKRAEELFQKLIENEGDVS--LIRAKVAEELKKKPDAELKKKLELLYQK---WPKALGAARDR 2558
Cdd:COG4913 369 aaLGLPLPASAEEFAALRAEAAALLEALEEELEALEeaLAEAEAALRDLRRELRELEAEIASLERRksnIPARLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2559 --KDLVSKAGDLvKQFGD--QVQALEQRLQ-------GDQAeLDeLLASDKAHDpevcDALKLVELTMARRLADVDALNA 2627
Cdd:COG4913 449 laEALGLDEAEL-PFVGEliEVRPEEERWRgaiervlGGFA-LT-LLVPPEHYA----AALRWVNRLHLRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2628 VMNRIESSAPGPDA-----------------NRLRRRAD--------TLSDDAK-----GMAKKARTAADLAQRKQGL-- 2675
Cdd:COG4913 522 GLPDPERPRLDPDSlagkldfkphpfrawleAELGRRFDyvcvdspeELRRHPRaitraGQVKGNGTRHEKDDRRRIRsr 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2676 -------AKKFERLCDEVSQFTE--NQKAEIQDAIEKDLLNAERVQSKLNKIDDFWSsnsrelknvgDEIKIDATPEDAQ 2746
Cdd:COG4913 602 yvlgfdnRAKLAALEAELAELEEelAEAEERLEALEAELDALQERREALQRLAEYSW----------DEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2747 AVDTKLAELQAGiDGLLATLQEQnvhLEEKREQANRVQSESQKAAGKINSLVAEIADLdpigrsrDELQKQKKEVVELAG 2826
Cdd:COG4913 672 ELEAELERLDAS-SDDLAALEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQA-------EEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 2827 DLGSAQTKmLELGAEWEAALGAGIVAQpVFEMNRAATDELNKLAARAGKRL 2877
Cdd:COG4913 741 DLARLELR-ALLEERFAAALGDAVERE-LRENLEERIDALRARLNRAEEEL 789
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1745-2258 |
1.09e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1745 VEDV--DQDPRFQRDEDRIQRIEE------LNRMAAGGSSQLDDAEQASRRLLTALEGTNVANDVRARHEElanlrrgkH 1816
Cdd:PRK02224 178 VERVlsDQRGSLDQLKAQIEEKEEkdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE--------R 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1817 QKVIDRLSQNMMEAASRKAEAEGVKQAVenlrqwSEQTAQRTRQPVQLpltELDLHEARKDEQVLHGEIENRLALIEELE 1896
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREEL------AEEVRDLRERLEEL---EEERDDLLAEAGLDDADAEAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1897 KKAADVGDhaslaELQECKMKLKRSNSDLKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAKI--RSARLPEAQSEVEA 1974
Cdd:PRK02224 321 DRDEELRD-----RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVedRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1975 LQDQ------------------ADNLERITNNLCNIPNVTRT-EPVIQKSKDLRK--RVDSCAQE---------LDARMG 2024
Cdd:PRK02224 396 LRERfgdapvdlgnaedfleelREERDELREREAELEATLRTaRERVEEAEALLEagKCPECGQPvegsphvetIEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2025 KLAELESLDAEFDGAKNKLSSFIgafdDELKGLEKVSIDKEKLAEQRRQTQDLVDKHSEG-----------NAILDDVEA 2093
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERL----ERAEDLVEAEDRIERLEERREDLEELIAERRETieekreraeelRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2094 IAQKVTAEDPSKTGSAQKSVGELGArLQRQASELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQlstgfpvpATKE 2173
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAE-LNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAL--------AELN 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2174 GVKSQLLDLERMNKT---GKEEQRRVDDARhSARELARE--ASVEKEVQDMNQREKKL----------LDEWEDLADQFD 2238
Cdd:PRK02224 623 DERRERLAEKRERKReleAEFDEARIEEAR-EDKERAEEylEQVEEKLDELREERDDLqaeigaveneLEELEELRERRE 701
|
570 580
....*....|....*....|
gi 1143463340 2239 AVRSRANKAEQVLNECAQME 2258
Cdd:PRK02224 702 ALENRVEALEALYDEAEELE 721
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4103-4200 |
1.16e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 52.72 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4103 EVEKWQRWLEETEsALLSTKPTGGLPETAEFQLDEFKALKLDVEHNASPLEAHLHATEQHLKEEPQDADTwLSKTHGAMK 4182
Cdd:smart00150 6 DADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLEELN 83
|
90
....*....|....*...
gi 1143463340 4183 TKWNKVKELLVDREKKLQ 4200
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
664-865 |
1.27e-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: 55.53 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 664 FSRVEECIEWVRVRMEKLTTMEFLEDLETLEHVFEQHKFDNRDIQDFRQNVDECIARQAEVSAEDTYEYCEL---LRVLE 740
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIqerLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 741 SEYQQLRDLSAGRMLDLDSLIA---FVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYND 817
Cdd:cd00176 86 QRWEELRELAEERRQRLEEALDlqqFFRDADDLEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEAHEPRLKS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1143463340 818 VHNQGAALLNQGHP-AIRVIEVYLRQMQSQWDWLLALSKCLEEHLRDAL 865
Cdd:cd00176 165 LNELAEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1997-2511 |
1.50e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1997 RTEPVIQKSKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGafddELKGLEkvsidkEKLAEQRRQTQD 2076
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEG----SKRKLE------EKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2077 LVDKHSEGNAILDDVEAIAQKVTA-----EDPSKTGSAQKSVGELGARLQRQASELKARGDKINKLDSKATSFAESEAAV 2151
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2152 ---LGYIEKQKDQLSTGFPVPATKEGVKSQL--LDLERMNKTGKEEQRRVDDARHSAREL-AREASVEKEVQDMNQREKK 2225
Cdd:PRK03918 351 ekrLEELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKItARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2226 L-------------LDEwEDLADQFDAVRSRANKAEQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVAKANRAQIQSMK 2292
Cdd:PRK03918 431 LkkakgkcpvcgreLTE-EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2293 AETEG--------EKSALEHVNSLANEL------IADGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEaakLGQEL 2358
Cdd:PRK03918 510 EKLKKynleelekKAEEYEKLKEKLIKLkgeiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE---LGFES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2359 KDiqkELRKELGELESNVEKASAMSS--NDIGDQLATLDSLKSRfggVDKALEKLKGILEATEEL--EVDATNRAEIQEQ 2434
Cdd:PRK03918 587 VE---ELEERLKELEPFYNEYLELKDaeKELEREEKELKKLEEE---LDKAFEELAETEKRLEELrkELEELEKKYSEEE 660
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1143463340 2435 LETTQKKADELERKIenvkkAALNAQNEglELEKKLDELIGTVNSAENELELAAPIAAESLKLADELKRAEELFQKL 2511
Cdd:PRK03918 661 YEELREEYLELSREL-----AGLRAELE--ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4534-4735 |
1.91e-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: 55.14 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4534 AEEFDAKTHALLDWLAVEEQKLKASG-----------LDEVEGVKQEMDEAKGRYQECLKKGEEILSKCQPAAEPIlRNW 4602
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDygddlesvealLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-QER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4603 MRVVEARWKEVSEKVDEREfTLLEQEQKAKEQNEQIEKLAKFAAQKREELNRmieQPPAQDLDTMEQNICDFANLDSELR 4682
Cdd:cd00176 81 LEELNQRWEELRELAEERR-QRLEEALDLQQFFRDADDLEQWLEEKEAALAS---EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463340 4683 EQQPEVDAACKSAKK------GARNPAAEMLSTEWKKLWLDamgLQSSLDNQKALLEEM 4735
Cdd:cd00176 157 AHEPRLKSLNELAEElleeghPDADEEIEEKLEELNERWEE---LLELAEERQKKLEEA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1873-2454 |
2.24e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1873 EARKDEQVLHGEIENRlalIEELEKKAADVgdhasLAELQECKMKLKRSNSDLKGLR------DNIFDAINGLQTVNSEG 1946
Cdd:PRK03918 179 ERLEKFIKRTENIEEL---IKEKEKELEEV-----LREINEISSELPELREELEKLEkevkelEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1947 ETLSRAVDSAGAKIRSaRLPEAQSEVEALQDQADNLERITnnlcniPNVTRTEPVI-------QKSKDLRKRVDSCAQEL 2019
Cdd:PRK03918 251 EGSKRKLEEKIRELEE-RIEELKKEIEELEEKVKELKELK------EKAEEYIKLSefyeeylDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2020 DARMGKLAELESLDAEFDGAKNKLSSFigafDDELKGLEKvsidKEKLAEQRRQTQDLVDKHSEGNAILDdVEAIAQKVT 2099
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKEL----EKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLT-PEKLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2100 AEDPSKTgSAQKSVGELGARLQRQASELKARGDKINKLDSkatsfAESEAAVLGYIEKQKDQlstgfpvpatKEGVKSQL 2179
Cdd:PRK03918 395 ELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKK-----AKGKCPVCGRELTEEHR----------KELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2180 LDLERMNKTGKEEQRRVDDARHSARELAREASVEKEVQdmnqREKKLLDEWEDLADQF-----DAVRSRANKAEQVLNEC 2254
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI----KLKELAEQLKELEEKLkkynlEELEKKAEEYEKLKEKL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2255 AQMEKYIGAKKNMLEGIGApstepgvAKANRAQIQSMKAETEGEKSALEHvnslanELIADGGANVEELMKKMDRLN--- 2331
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEE-------LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEpfy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2332 RKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLD----SLKSRFGGVDKA 2407
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELReeylELSRELAGLRAE 681
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 2408 LEKLKGILEAT----EELEVDATNRAEIQEQLETTQKKADELERKIENVKK 2454
Cdd:PRK03918 682 LEELEKRREEIkktlEKLKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2337-3030 |
2.82e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2337 LESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLKSRFGGVDKALEKLKGILE 2416
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2417 ATEEL------EVDATNRAEIQEQLETTQKKADELERKIENVKK---------AALNAQNEG---LELEKKLDELIGTVN 2478
Cdd:pfam15921 195 DFEEAsgkkiyEHDSMSTMHFRSLGSAISKILRELDTEISYLKGrifpvedqlEALKSESQNkieLLLQQHQDRIEQLIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2479 SAENELELAAPIAAESLKLADELKRAEELFQKLIEN------------EGDVSLIRAKVAEELKKKPDA--ELKKKLELL 2544
Cdd:pfam15921 275 EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqnsmymrqlsdlESTVSQLRSELREAKRMYEDKieELEKQLVLA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2545 YQKwpkaLGAARDRKDLVSK-AGDLvkqfGDQVQALEQRLQGDQAELDellasdkahdpevcdalklVELTMARRLADVD 2623
Cdd:pfam15921 355 NSE----LTEARTERDQFSQeSGNL----DDQLQKLLADLHKREKELS-------------------LEKEQNKRLWDRD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2624 ALNAVMN---RIESSAPGPDANRLRRRADTLSDDAKGMAKKARTAAdlaqrkQGLAKKFERLCDEVSQFtENQKAEIQDA 2700
Cdd:pfam15921 408 TGNSITIdhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAI------QGKNESLEKVSSLTAQL-ESTKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2701 IEKDLLNAERVQSKLNKIDDFWSSNSRElknvgdEIKIDATpedaqavDTKLAELQAGIDGLLATLQeqnvHLEEKREQA 2780
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEK------ERAIEAT-------NAEITKLRSRVDLKLQELQ----HLKNEGDHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2781 NRVQSESQkaagkinSLVAEIADLDPIgrsRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEAalgagivaqpvfEMN- 2859
Cdd:pfam15921 544 RNVQTECE-------ALKLQMAEKDKV---IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK------------EINd 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2860 -RAATDELNKLAARAGKRLAQREKKITETEDEIDKLHADADQIVGALEAIA--KDEALQGAPSQLLDPKQVSEKVRQLKE 2936
Cdd:pfam15921 602 rRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKqeRDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2937 SLKPVGEKMDAFNTDCKLLIKTAGPESDTKE--LDSLLKKVGDAYSDVVG---KVSDKEMSVDAAvqqQGKVEDAYRALL 3011
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSELEQTRntLKSMEGSDGHAMKVAMGmqkQITAKRGQIDAL---QSKIQFLEEAMT 758
|
730
....*....|....*....
gi 1143463340 3012 NWLEETEEMMENRKKPSAD 3030
Cdd:pfam15921 759 NANKEKHFLKEEKNKLSQE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2336-3103 |
2.88e-07 |
|
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: 57.39 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2336 SLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIgdqlatlDSLKSRFGGVDKALEKLKGIL 2415
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-------LRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2416 EATE-ELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELigtvnsaENELElaaPIAAES 2494
Cdd:TIGR02169 311 AEKErELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL-------RAELE---EVDKEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2495 LKLADELKRAEELFQKLIENEGDVSLIRAKVAEELKKKPD--AELKKKLELLYQKWPKALGAARDRKDLVSKAGDLVKQF 2572
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2573 GDQVQALEQRLQGDQAELDellasdkahdpEVCDALKLVELTMARRLADVDAlnavmnrIESSAPGPDANRlrrraDTLS 2652
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYD-----------RVEKELSKLQRELAEAEAQARA-------SEERVRGGRAVE-----EVLK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2653 DDAKGMAKkarTAADLAQRKQGLAKKFE-----RLCDEVSQFTENQKAEIQDAIEKDLLNAERVqsKLNKIDDFWSSNSR 2727
Cdd:TIGR02169 518 ASIQGVHG---TVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFL--PLNKMRDERRDLSI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2728 ELKN--VGDEIK-IDATPEDAQAV-----DTKLAE-LQAGIDGL----LATLQEQNV---------HLEEKREQANRVQ- 2784
Cdd:TIGR02169 593 LSEDgvIGFAVDlVEFDPKYEPAFkyvfgDTLVVEdIEAARRLMgkyrMVTLEGELFeksgamtggSRAPRGGILFSRSe 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2785 -SESQKAAGKINSLVAEIADLdpigrsRDELQKQKKEVVELAGDLGSAQTKMLELGAEWEAALG-----AGIVAQ---PV 2855
Cdd:TIGR02169 673 pAELQRLRERLEGLKRELSSL------QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeklKERLEEleeDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2856 FEMNRAATDELNKLAARAgKRLAQREKKITETEDEIDKLHAD-----ADQIVGALEAIakDEALQGAPSQLLDPKQVSEK 2930
Cdd:TIGR02169 747 SSLEQEIENVKSELKELE-ARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKL--EEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2931 VRQLKESLKPVGEKMDAFNTDCKLLIKTAGPESDT-----KELDSLLKKVGDAYSDVVGKVSDKEMSVDAAVQQQGKVED 3005
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3006 AYRALLNWLEETEEMMENRKKPSADAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIvaeassDEEKKALGNKNAQI 3085
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRV------EEEIRALEPVNMLA 977
|
810
....*....|....*...
gi 1143463340 3086 EDRYKDLLNSAVDRQRKL 3103
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKR 995
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
763-861 |
4.47e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.18 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 763 FVRAAQLELIWVSERESIEVTRNWSDIKQlDLPMLTNYYKQLLHEMELREKQYNDVHNQGAALLNQGHPAIRVIEVYLRQ 842
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEE 81
|
90
....*....|....*....
gi 1143463340 843 MQSQWDWLLALSKCLEEHL 861
Cdd:smart00150 82 LNERWEELKELAEERRQKL 100
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4427-4528 |
5.44e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4427 FEESMNDLESWVDdelERYQKAEHEPVFADIDGVRALVDEESRRSAERKTKENGVKTVVKKADALMASGVDEKDSIAQAK 4506
Cdd:smart00150 3 FLRDADELEAWLE---EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1143463340 4507 ERLVEKWNQVEEAARHRGNSIK 4528
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2109-2527 |
7.30e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2109 AQKSVGELGARLQRQASELKARGDKINKLDSK---ATSFAESEAAVLGYIEKQKDQLSTgfpVPATKEGVKSQLLDLERM 2185
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQreqARETRDEADEVLEEHEERREELET---LEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2186 NKTGKEEQRRVDDARHSARELAREASVEKEVQDMNQrekklldewEDLADQFDAVRSRANKAEQVLNECAQMekyIGAKK 2265
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDLLAEAGLDDADA---------EAVEARREELEDRDEELRDRLEECRVA---AQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2266 NMLEGigapstepgvAKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKMDRLNRKWHSLESGLDENA 2345
Cdd:PRK02224 342 EEAES----------LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2346 GRVEEAAKLGQELKDIQKELRKELGELESNVEKASAM------------------------SSNDIGDQLATLDSLKSRF 2401
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2402 GGVDKALEKLKGILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGtvnSAE 2481
Cdd:PRK02224 492 EEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE---EAE 568
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1143463340 2482 NELELAAPIAAESLKLADE---LKRAEELFQKLIENEGDVSLIRAKVAE 2527
Cdd:PRK02224 569 EAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKREA 617
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2043-2510 |
1.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2043 LSSFIGAFDDELKGLEKVS-----IDKEKLAEQRRQTQDLVDKHSEGNAILDDVEAIAQKVtaedpsktgsaqksvgelg 2117
Cdd:COG4717 44 RAMLLERLEKEADELFKPQgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2118 ARLQRQASELKARGDKINKLDSKATSFAESEAAvlgyiekqKDQLStgfPVPATKEGVKSQLLDLERMNKTGKEEQRRVD 2197
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQELEAL--------EAELA---ELPERLEELEERLEELRELEEELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2198 DARHSARELAREASVEKEvqdmnQREKKLLDEWEDLADQFDAVRSRANKAEQVLNEC-------------AQMEKYIGAK 2264
Cdd:COG4717 174 ELQEELEELLEQLSLATE-----EELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqleneleaAALEERLKEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2265 KNMLEGIGA--------------PSTEPGVAKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKMDRL 2330
Cdd:COG4717 249 RLLLLIAAAllallglggsllslILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2331 NRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKE--LGELESNVEKASAMSSND---IGDQLATLDSLKSRFGGVD 2405
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAGVEDEEElraALEQAEEYQELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2406 KALEKLKGILEAteelEVDATNRAEIQEQLETTQKKADELERKIENV--KKAALNAQNEGLELEKKLDELIGTVNSAENE 2483
Cdd:COG4717 409 EQLEELLGELEE----LLEALDEEELEEELEELEEELEELEEELEELreELAELEAELEQLEEDGELAELLQELEELKAE 484
|
490 500
....*....|....*....|....*...
gi 1143463340 2484 LELAApIAAESLKLADE-LKRAEELFQK 2510
Cdd:COG4717 485 LRELA-EEWAALKLALElLEEAREEYRE 511
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2144-2351 |
2.91e-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: 51.68 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2144 FAESEAAVLGYIEKQKDQLSTGFPvPATKEGVKSQLLDLERMNKTGKEEQRRVDDARHSARELARE-----ASVEKEVQD 2218
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdaEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2219 MNQREKKLLDEWEDLADQFDavrsRANKAEQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVAKANRaQIQSMKAETEGE 2298
Cdd:cd00176 84 LNQRWEELRELAEERRQRLE----EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLK-KHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1143463340 2299 KSALEHVNSLANELIADGG-ANVEELMKKMDRLNRKWHSLESGLDENAGRVEEA 2351
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHpDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2389-2939 |
6.10e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2389 DQLATLDSLKSRfggVDKALEK---LKGILEATEELEvDATNRAEIQEQLETT------QKKADELERKIENVKKAALNA 2459
Cdd:COG4913 232 EHFDDLERAHEA---LEDAREQielLEPIRELAERYA-AARERLAELEYLRAAlrlwfaQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2460 QNEGLELEKKLDELIGTVNSAENELELAAPIAAESLK-----LADELKRAEELFQKLIENEGDVSLIRAKVAEELkkkpd 2534
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEERERRRARLEALLAALGLPLPASAEEF----- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2535 AELKKKLELLYQKWPKALGAARDRKDlvskagdlvkQFGDQVQALEQRLQGDQAELDELLASDKAHDPEV-------CDA 2607
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALA----------EAEAALRDLRRELRELEAEIASLERRKSNIPARLlalrdalAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2608 LK-----------LVEL----------------TMARRL----ADVDALNAVMNRIessapgPDANRLR--------RRA 2648
Cdd:COG4913 453 LGldeaelpfvgeLIEVrpeeerwrgaiervlgGFALTLlvppEHYAAALRWVNRL------HLRGRLVyervrtglPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2649 DTLSDDAKGMAKKARTAADLAQR--KQGLAKKFERLC-DEVSQFTENQKAeiqdaIEKDLLnaervqsklnkiddfwSSN 2725
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCvDSPEELRRHPRA-----ITRAGQ----------------VKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2726 SRELKNVGDEIKIDATP---EDAQAvdtKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQsESQKAAGKINSLVAEIA 2802
Cdd:COG4913 586 NGTRHEKDDRRRIRSRYvlgFDNRA---KLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2803 DLDPIGRSRDELQKQKKEVVELAGDLGsaqtkmlELGAEWEAAlgagivaqpvfemnRAATDELNKLAARAGKRLAQREK 2882
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLA-------ALEEQLEEL--------------EAELEELEEELDELKGEIGRLEK 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1143463340 2883 KITETEDEIDKLHADADQIvGALEAIAKDEALQGAPSQLLDPKQVSEKVRQLKESLK 2939
Cdd:COG4913 721 ELEQAEEELDELQDRLEAA-EDLARLELRALLEERFAAALGDAVERELRENLEERID 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4293-4710 |
7.51e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4293 RVEKISgRTAERAKQLAVTRDEVATWQDGLHDLEHFISDVLVKIAPEPNTTSSLEKL--KAKLEEVKEAQRDVTAkqtlf 4370
Cdd:PTZ00121 1231 KAEEAK-KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeeKKKADEAKKAEEKKKA----- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4371 DVTRKRgiglAERATRSEykQISMTNEKMSKKWAEMLKKLRDRLREAEQAVLEGgafEESMNDLESWVDDELERYQKAEH 4450
Cdd:PTZ00121 1305 DEAKKK----AEEAKKAD--EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA---EAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4451 EPVFADIDGVRAlvdEESRRSAERKTKENGVKtvvKKADALMASGvDEKDSIAQAKERLVEKWNQVE-----EAARHRGN 4525
Cdd:PTZ00121 1376 AKKKADAAKKKA---EEKKKADEAKKKAEEDK---KKADELKKAA-AAKKKADEAKKKAEEKKKADEakkkaEEAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4526 SIKEAEQAAEEFDAKTHAlldwlaveEQKLKASGLDEVEGVKQEMDEAKGRYQECLKKGEEILSKCQPAAepilrnwmRV 4605
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKA--------EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK--------KA 1512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4606 VEARWKEVSEKVDEREFTllEQEQKAKEQNEQIEKLAKFAAQKREELNRMIEQPPAQDLDTMEQNICDFANLDSELREQQ 4685
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKA--EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
410 420
....*....|....*....|....*
gi 1143463340 4686 PEVDAACKSAKKGARNPAAEMLSTE 4710
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3002-3103 |
9.52e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3002 KVEDAYRALLNWLEETEEMMENrKKPSADAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEasSDEEKKALGNK 3081
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEIEER 78
|
90 100
....*....|....*....|..
gi 1143463340 3082 NAQIEDRYKDLLNSAVDRQRKL 3103
Cdd:smart00150 79 LEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1115-1329 |
1.03e-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: 49.75 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1115 QYDQKMAELLKKLEEAWRELNDAVgkpISRSPEDLERVIHAHKRFEDALQALDSDVANVKELFRQLPNPTPTQRVNH--- 1191
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIqer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1192 -DRLNGLWDDLWDLSRMYVERIKVLESVLNGMVEVADI---VRQHEITLNSfDDLPAALDKLRGHHSQLLEINMVLKQQQ 1267
Cdd:cd00176 81 lEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLeqwLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 1268 TVIDQLNRNVALLrqhvsrtrINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESAL 1329
Cdd:cd00176 160 PRLKSLNELAEEL--------LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1633-1900 |
1.28e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1633 RIDEARFEAKSLMDEVIREESRLKTIGASVLKIEQEISAMRDDVRASGStddvgiSVDEVYETRRRVEDDYMQLLRQCQD 1712
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA------ELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1713 LISFQNRLHAMNDEHSEQARRADEWLQMLQNDVEDVDQdprfQRDEDRIQRIEELNRMAAGGSSQLDDAEQASRRLLTAL 1792
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1793 EGTNVANDVRARHEELANLRRGKHQKVIDRLSQNMMEAASRKAEAEGVKQAVENLRQWSEQTAQRTRQPVQLPLTELDLH 1872
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260
....*....|....*....|....*...
gi 1143463340 1873 EARKDEQVLHGEIENRLALIEELEKKAA 1900
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1999-2755 |
1.39e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1999 EPVIQKSKDLRKRVDSCAQELDARMGKLA----ELESLDAEfdgaknklssfIGAFDDElkGLEKVSIDKEKLAEQRRQT 2074
Cdd:pfam12128 290 QLLRTLDDQWKEKRDELNGELSAADAAVAkdrsELEALEDQ-----------HGAFLDA--DIETAAADQEQLPSWQSEL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2075 QDLvdkhsegNAILDDVEAIAQKVTAEdpsktgsAQKSVGELGARLQRQASELKARGDKINklDSKATSFAESEAAVLGY 2154
Cdd:pfam12128 357 ENL-------EERLKALTGKHQDVTAK-------YNRRRSKIKEQNNRDIAGIKDKLAKIR--EARDRQLAVAEDDLQAL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2155 IEKQKDQLSTGF-PVPATKEGVKSQLldlermnktgKEEQRRVDDARHSARELAREASVEKEVQDMNQREKKLLDEWEDL 2233
Cdd:pfam12128 421 ESELREQLEAGKlEFNEEEYRLKSRL----------GELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2234 ADQFDAVRSRANKAEQVLNECAQMEKYIGAKKNMLEGIGAP---------STEPGVAKANRAQIQSmkaetegekSALEH 2304
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhflRKEAPDWEQSIGKVIS---------PELLH 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2305 VNSLANELIADGGANVEELMKKMDRLNR----KWHSLESGLDENAGRVEEAAklgQELKDIQKELRKELGELESNVEKAS 2380
Cdd:pfam12128 562 RTDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEELRERLDKAEEAL---QSAREKQAAAEEQLVQANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2381 AMSSndigDQLATLDSLKSRFG--GVDKALEKLKgILEATEElevdatNRAEIQEQLETTQKKADELERKIenvkKAALN 2458
Cdd:pfam12128 639 REET----FARTALKNARLDLRrlFDEKQSEKDK-KNKALAE------RKDSANERLNSLEAQLKQLDKKH----QAWLE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2459 AQNEGL-----ELEKKLDELIGTVNSAENELElaAPIAAESLKLADELK-----RAEELFQKLIENEGDVSLIRaKVAEE 2528
Cdd:pfam12128 704 EQKEQKreartEKQAYWQVVEGALDAQLALLK--AAIAARRSGAKAELKaletwYKRDLASLGVDPDVIAKLKR-EIRTL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2529 LKKKPDAELKKKLELLYQKWPKALGAARD--RKDLVSKAGDLVKQFGDQVQALEQRLQGDQAELD-ELLASDKAHDpEVC 2605
Cdd:pfam12128 781 ERKIERIAVRRQEVLRYFDWYQETWLQRRprLATQLSNIERAISELQQQLARLIADTKLRRAKLEmERKASEKQQV-RLS 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2606 DALKLVELTMaRRLADVdALNAVMNRIESSAPGPDA--NRLRRRADTLSDDAK--------GMAKKARTA---------- 2665
Cdd:pfam12128 860 ENLRGLRCEM-SKLATL-KEDANSEQAQGSIGERLAqlEDLKLKRDYLSESVKkyvehfknVIADHSGSGlaetweslre 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2666 ADLAQRKQGLAKKFERLCDEVSQFTENQKAEIQDAIEKDL--LNAERVQSKLNKIDDF---WSSNSREL-KNVGDEIKID 2739
Cdd:pfam12128 938 EDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQvsILGVDLTEFYDVLADFdrrIASFSRELqREVGEEAFFE 1017
|
810
....*....|....*.
gi 1143463340 2740 ATPEDAQAVDTKLAEL 2755
Cdd:pfam12128 1018 GVSESAVRIRSKVSEL 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1834-2452 |
1.68e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1834 KAEAEgVKQAVENLRQWSEQTAQRTRQPVQLPLTELDLHEARKDEQVLHGEIENRLALIEELEKKAADVGD--HASLAEL 1911
Cdd:COG1196 219 KEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1912 QECKMKLKRSNSDLKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAKIRSARlPEAQSEVEALQDQADNLERITNNLcn 1991
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-EELEEAEAELAEAEEALLEAEAEL-- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1992 ipnvtrtepvIQKSKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGAFDDELKGLEKVSIDKEKLAEQR 2071
Cdd:COG1196 375 ----------AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2072 RQTQDLVDKHSEGNAILDDVEAIAQKVTAEDPSKTGSAQKSVGELGARLQRQASELKARGDKINKLDSKATSFAESEAAV 2151
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2152 LGYIEKQKDQLSTGFPVPATKEGVKSQLLDLERMNKTGKEEQRRVDDARHSARELAREASVE-KEVQDMNQREKKLLDEW 2230
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAaLAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2231 EDLADQFDAVRSRANKAEQVLN-ECAQMEKYIGAKKNMLEGIGAPSTEPGVAKANRAQIQSMKAETEGEKSALEHVNSLA 2309
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2310 NELIADGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGD 2389
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143463340 2390 QLATLDSLKsrfggvdKALEKLKGI-LEATEELEVDATNRAEIQEQLETTQKKADELERKIENV 2452
Cdd:COG1196 765 LERELERLE-------REIEALGPVnLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEI 821
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3066-3789 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3066 VAEASSDEEKKALGNKNAQIEDRYKDLLNSAVDRQRKLLDAVDLAERLQEvtipLDSWLQSADKRLQALAKVPITVEKAE 3145
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3146 EMIGEQEA-LQDELEHKSDDLKDVLEIAPMLASLVSV--EDANSISGQVNQLEARARALDAGITNMRPLLESFLQQIQDF 3222
Cdd:TIGR02168 340 AELEEKLEeLKEELESLEAELEELEAELEELESRLEEleEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3223 TLDAEDMTQFVGETEVKL--GELDELPIEPDDLVEQTNILAEIAVSIADRDEMmanifevgKQLAIQGEPEEALIAQKKL 3300
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKElqAELEELEEELEELQEELERLEEALEELREELEE--------AEQALDAAERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3301 DDLKFRYADLMTSADEKIALLAKAI-------PLSEGFH--EGFDTVMQ----------VLEDMDRDLQTIDEEDPETQA 3361
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISvdEGYEAAIEaalggrlqavVVENLNAAKKAIAFLKQNELG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3362 ELIFLLEEDISQKmRPSVDELTALSNQLQVLCSADkadELQTNTIAMNKLVNS------VADRVARRAE-RIEMASKQSR 3434
Cdd:TIGR02168 572 RVTFLPLDSIKGT-EIQGNDREILKNIEGFLGVAK---DLVKFDPKLRKALSYllggvlVVDDLDNALElAKKLRPGYRI 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3435 AVLDDLQYLIEWFSAARERILEGAPPSLDLEVLKSQLKHQRITNEEASANKvqfrnvagEAKKVARQLgmegNEANEKIS 3514
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK--------ALAELRKEL----EELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3515 DTVDEGKELVEEVMALCADrtetLERALALMEQLTSQFDELNKWLDQMDAELQASpsvttatpAAELREMHDHNEELARM 3594
Cdd:TIGR02168 716 QLRKELEELSRQISALRKD----LARLEAEVEQLEERIAQLSKELTELEAEIEEL--------EERLEEAEEELAEAEAE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3595 VAAYRPIIEGFKSDVGSLHEVLAEDQAPL--LESVAGELVQGYEEVREAVRARGHAIDNMMGATIGFGERLETLVANLQG 3672
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELtlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3673 AADRLRENE----GISADPSVLESRLAENRSIVESLRDKQNAYDalkQTASELLASAPEGDAAAGDVENKLNRLE-KLWK 3747
Cdd:TIGR02168 864 LEELIEELEseleALLNERASLEEALALLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGLEvRIDN 940
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1143463340 3748 EIEREAVDRGVLLEDVLDKAKHFWSELDSCQKAVDDLRNRLE 3789
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
302-411 |
2.74e-05 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 46.60 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 302 GSDATSARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNkiSSDSVSNTERLNNAFAAADREF 380
Cdd:cd21314 6 DARKQTPKQRLLGW---IQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCpDWE--SWDPNQPVQNAREAMQQADDWL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 381 GVERLLDAEDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21314 81 GVPQVIAPEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3218-3429 |
2.77e-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: 48.60 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3218 QIQDFTLDAEDMTQFVGETEVKLGElDELPIEPDDLVEQTNILAEIAVSIADRDEMMANIFEVGKQLAIQGEPEEALIaQ 3297
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3298 KKLDDLKFRYADLMTSADEKIALLAKAIPLSEGFHEgFDTVMQVLEDMDRDLQTIDEEDPETQAELIF----LLEEDISQ 3373
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLkkhkELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1143463340 3374 KmRPSVDELTALSNQLQVLCSADKADELQTNTIAMNKLVNSVADRVARRAERIEMA 3429
Cdd:cd00176 158 H-EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2281-2541 |
7.61e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2281 AKANRAQIQSMKAETEGEKSALEHVNSLANELIADgganVEELMKKMDRLNRKWHSLESGLDENAGRVeeaaklgQELKD 2360
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAEL-------AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2361 IQKELRKELGELESNVEK-ASAMSSNDIGDQLATLDSLKSrFGGVDKALEKLKGILEAteelevdatnRAEIQEQLETTQ 2439
Cdd:COG4942 91 EIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPED-FLDAVRRLQYLKYLAPA----------RREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2440 KKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAAPIAAESLKladELKRAEELFQKLIEnegDVS 2519
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA---ELQQEAEELEALIA---RLE 233
|
250 260
....*....|....*....|..
gi 1143463340 2520 LIRAKVAEELKKKPDAELKKKL 2541
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2425-2666 |
1.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2425 ATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELElaapiaaeslKLADELKRA 2504
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------ALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2505 EElfqklienegdvsliRAKVAEELKKKPDAELKKKLELLY----QKWPKALGAARDRKDLVsKAGDLVKQFGDQVQALE 2580
Cdd:COG4942 89 EK---------------EIAELRAELEAQKEELAELLRALYrlgrQPPLALLLSPEDFLDAV-RRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2581 QRLQGDQAELDELLASDKAHDPEVCDALKLVELTMARRLADVDALNAVMNRIESSAPG--PDANRLRRRADTLSDDAKGM 2658
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAElaAELAELQQEAEELEALIARL 232
|
....*...
gi 1143463340 2659 AKKARTAA 2666
Cdd:COG4942 233 EAEAAAAA 240
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2321-3121 |
1.25e-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: 48.81 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2321 EELMKK---MDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNV-EKASAMSSNDIGDQLATLDS 2396
Cdd:pfam02463 176 KKLIEEtenLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2397 LKSRF-GGVDKALEKLKGILEATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIG 2475
Cdd:pfam02463 256 SKQEIeKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2476 TVNSAENELELAApIAAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEELKKKPDAELKKKLELLYQKWPKALGAA 2555
Cdd:pfam02463 336 EIEELEKELKELE-IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2556 RDRKDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDELLASDKAHDPEVCDALK----------LVELTMARRLADVDAL 2625
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKksedllketqLVKLQEQLELLLSRQK 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2626 NAVMNRIESSAPGPDANRLRRRADTLSDDAKGMA---KKARTAADLAQRKQGLAKKFE--RLCDEVSQFTENQKAEIQDA 2700
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEvsATADEVEERQKLVRALTELP 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2701 IEKDLLNAERVQSKLNKIDD-FWSSNSRELKNVGDEIKIDATPEDAQAV---------------------------DTKL 2752
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIaVLEIDPILNLAQLDKATLEADEDDKRAKvvegilkdteltklkesakakesglrkGVSL 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2753 AELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKINSLVAEIADLDPIGRSR---DELQKQKKEVVELAGDLG 2829
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDKI 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2830 SAQTKMLELGAEWEAALGAGIVAQPVFEMNRAAtDELNKLAARAGKRLAQREKKITETEDEIDKLhadADQIVGALEAIA 2909
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS-ELSLKEKELAEEREKTEKLKVEEEKEEKLKA---QEEELRALEEEL 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2910 KDEALQGAPSQLLDPKQVSEKVRQLKESLKPVGEKMDAFNtdcKLLIKTAGPESDTKELDSLLKKVGDAYSDVVGKVSDK 2989
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK---LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2990 EMSVDAAVQQQGKVEDAYRALLNWLEETEEMMENRKKPSADAKVakaQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEa 3069
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL---KYEEEPEELLLEEADEKEKEENNKEEEEERNK- 963
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 3070 SSDEEKKALGNKNAQIEDRYKDLLNSAVDRQRKLLDAVDLAERLQEVTIPLD 3121
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3461-4229 |
1.70e-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: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3461 SLDLEVLKSQLKHQRitnEEASANKVQFRNVAGEAKKVARQLgmegNEANEKISDTVDEGKELVEEVmalcADRTETLER 3540
Cdd:TIGR02168 224 ELELALLVLRLEELR---EELEELQEELKEAEEELEELTAEL----QELEEKLEELRLEVSELEEEI----EELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3541 ALALMEQLTSQFDELNKWLDQMDAELQASpsvttatpAAELREMHDHNEELARMVAAYRPIIEGFKSDVGSLHEVLAEdq 3620
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEEL--------EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3621 aplLESVAGELVQGYEEVREAVRARGHAIDNMmgatigfGERLETLVANLQGAADRLrenegisadpSVLESRLAENRSI 3700
Cdd:TIGR02168 363 ---LEAELEELESRLEELEEQLETLRSKVAQL-------ELQIASLNNEIERLEARL----------ERLEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3701 VESLRDKQNAYDaLKQTASELLASAPEGDAAAGDVENKLNRLEKLWKEIEReavdrgvlLEDVLDKAKHFWSELDSCQKA 3780
Cdd:TIGR02168 423 IEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEE--------AEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3781 VDDLRNRLElvEPATGHPEQLADQQEI--MAQVASEMERARPRIE-ALSIA-GKQLADYVPDDEKAVIENQ--VANVRGG 3854
Cdd:TIGR02168 494 LERLQENLE--GFSEGVKALLKNQSGLsgILGVLSELISVDEGYEaAIEAAlGGRLQAVVVENLNAAKKAIafLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3855 FSTITGLFAEKKRDLIAAMEEAMTFHGDLQELLKWLDMAEQKLlkmSPVehakhmteIEQLLKELHTFKDevhergvake 3934
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL---RKA--------LSYLLGGVLVVDD---------- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3935 qvVATALQLAADAPPHLAATVRQPVAdLNTRWS------RLNAALAEREHKLENLMLQMGKLASTIAQLTAWMDKTRATL 4008
Cdd:TIGR02168 631 --LDNALELAKKLRPGYRIVTLDGDL-VRPGGVitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4009 KDIAppknavnlRDIEIAQCKLVVLSNDIHAHQDSVNAVNRAAQKYIQTSGALDAETSDSLKSMNLKWEDIQKVLESLAf 4088
Cdd:TIGR02168 708 EELE--------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA- 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4089 dmeVAKKEAENVGGEVEKWQRWLEETESALLSTKptGGLPETAEFQLDEFKALKlDVEHNASPLEAHLHATEQHLKEEPQ 4168
Cdd:TIGR02168 779 ---EAEAEIEELEAQIEQLKEELKALREALDELR--AELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 4169 DAdTWLSKTHGAMKTKWNKVKELLVDREKKLQVAYEQAVALESALNDMEDWIIAAERKLTD 4229
Cdd:TIGR02168 853 DI-ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2204-2981 |
1.71e-04 |
|
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: 48.14 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2204 RELAREASVEKEVqdmNQREKKLLDEWEDlADQFDAVRSRANKAEQ--VLNECAQMEKYIGAKKNMLEGIgapstepgva 2281
Cdd:TIGR02169 184 ENIERLDLIIDEK---RQQLERLRREREK-AERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL---------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2282 KANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANveelmkKMDRLNRKWHSLESGLdENAGRVEEAAKlgQELKDI 2361
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEI-ASLERSIAEKE--RELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2362 QKELRK---ELGELESNVEKasamSSNDIGDQLATLDSLKSRFGGVDKALEKLKGILEateelEVDATNRA------EIQ 2432
Cdd:TIGR02169 321 EERLAKleaEIDKLLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRAELE-----EVDKEFAEtrdelkDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2433 EQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAApiaaesLKLADELKRAEELFQKLI 2512
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA------LEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2513 ENEGDVSLIRAKVAEELKKKPDAELK-KKLELLYQKWPKALGAARDRKDLVSKAGD----LVKQFG----DQVQALE--- 2580
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRElAEAEAQARASEERVRGGRAVEEVLKASIQgvhgTVAQLGsvgeRYATAIEvaa 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2581 -QRLQ-------GDQAELDELLASDKA---------------------HDPEVCD-ALKLVELTMARRLADVDAL--NAV 2628
Cdd:TIGR02169 546 gNRLNnvvveddAVAKEAIELLKRRKAgratflplnkmrderrdlsilSEDGVIGfAVDLVEFDPKYEPAFKYVFgdTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2629 MNRIESSAPGPDANRLRRRADTLSDDAKGMAKKARTAADLAQRKQGLAKKFERLCDEVsqftenqkaeiqDAIEKDLlna 2708
Cdd:TIGR02169 626 VEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERL------------EGLKREL--- 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2709 ERVQSKLNKIDDFWSSNSRELKnvgdeikidatpeDAQAvdtKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQ 2788
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELS-------------DASR---KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2789 KAAGKINSLVAEIADLD--------------------PIGRSRDELQKQKKEVVELAGDLGSAQTKM--LELGAEWEAAL 2846
Cdd:TIGR02169 755 NVKSELKELEARIEELEedlhkleealndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLnrLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2847 GAGIVAQPVF-----EMNRAATDELNKLAARAGKRLAQREKKITETEDEIDKLHADADqivgalEAIAKDEALQGAPSQL 2921
Cdd:TIGR02169 835 IQELQEQRIDlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD------ELEAQLRELERKIEEL 908
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 2922 -LDPKQVSEKVRQLKESLKPVGEKMDAFNTDCKLLIKTAGPESDTKELDSLLKKVGDAYSD 2981
Cdd:TIGR02169 909 eAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2286-2905 |
1.86e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2286 AQIQSMKAETEGEKSALEHV-NSLANELIadggaNVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKE 2364
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEyNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEER 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2365 LRkelgELESNVEKASAMSSNDIGDQLATLDSLKSRFGGVDKALEKLKGILEATEELEVDATNRAEIQEQLETTQKKADE 2444
Cdd:PRK01156 282 HM----KIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2445 LE----------RKIENVKKaalNAQNEGLELEKKLDELIGTVNSAEnelelaapIAAESLKladelKRAEELFQKLIEN 2514
Cdd:PRK01156 358 LEgyemdynsylKSIESLKK---KIEEYSKNIERMSAFISEILKIQE--------IDPDAIK-----KELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2515 EGDVSLIRAKVAEELKKKpdAELKKKLELL--YQKWP---KALGAardrkdlvSKAGDLVKQFGDQVQALEQrlqgdqaE 2589
Cdd:PRK01156 422 SSKVSSLNQRIRALRENL--DELSRNMEMLngQSVCPvcgTTLGE--------EKSNHIINHYNEKKSRLEE-------K 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2590 LDELLASDKAHDPEVCDALKLVELTMARrlaDVDALNAVMNRIESsapgpdanrLRRRADTLSDDAKGMAKKARTAADLA 2669
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIES---------ARADLEDIKIKINELKDKHDKYEEIK 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2670 QRKQGLakkfeRLCDEVSQFTENQKAEIQdaieKDLLNAERVQSKLNKIddfwSSNSRELKNVGDEIKIDaTPEDAQAVD 2749
Cdd:PRK01156 553 NRYKSL-----KLEDLDSKRTSWLNALAV----ISLIDIETNRSRSNEI----KKQLNDLESRLQEIEIG-FPDDKSYID 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2750 TKLAElqagIDGLLATLQEQNVHLEEKREQANRVQsesqkaaGKINSLVAEIADLDPIGRSRDELQKQKKEVVELAGDLG 2829
Cdd:PRK01156 619 KSIRE----IENEANNLNNKYNEIQENKILIEKLR-------GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1143463340 2830 SAQTKMLELGAEWEAALgagivaqpvfEMNRAATDELNklaaragKRLAQREKKItETEDEIDKLHADADQIVGAL 2905
Cdd:PRK01156 688 KALDDAKANRARLESTI----------EILRTRINELS-------DRINDINETL-ESMKKIKKAIGDLKRLREAF 745
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2866-3651 |
1.97e-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: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2866 LNKLAaRAGKRLAQREKKITETEDEIDKLHADADQIVGALEAIAKDEALQGApSQLLDPKQVSEKVRQLKESLKPVGEKM 2945
Cdd:TIGR02168 178 ERKLE-RTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELA-LLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2946 DAFNTDckllIKTAGPESDTK-----ELDSLLKKVGDAYSDVVGKVSDKEMSVDAAVQQQGKVEDAYRALLNWLEETEEM 3020
Cdd:TIGR02168 256 EELTAE----LQELEEKLEELrlevsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3021 MENRKKPSADAKVAKAQLhdyevlmkhvedkKPSVDGFKAMIEKivAEASSDEEKKALGNKNAQIE---DRYKDLLNSAV 3097
Cdd:TIGR02168 332 LDELAEELAELEEKLEEL-------------KEELESLEAELEE--LEAELEELESRLEELEEQLEtlrSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3098 DRQRKLLDAVDLAERLQEVTIPLDSWLQSADKRLQALAKvpitvEKAEEMIGEQEALQDELEHKSDDLKDVLEIAPMlas 3177
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL-----KELQAELEELEEELEELQEELERLEEALEELRE--- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3178 lvSVEDANSISGQVNQLEARARALDAGITNMRPLLESFLQQIQDFTLDAEDMTQFVGE--TEVKLGELDELPIEP----- 3250
Cdd:TIGR02168 469 --ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEAalggr 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3251 -DDLVEQTNILAEIAVSIADRDEMMANIFEVGKQLAIQGEPEEALIAQKKLDDLKFRYADLMTSADE-KIAL-------- 3320
Cdd:TIGR02168 547 lQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALsyllggvl 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3321 ----LAKAIPLSEGFHEGFDTV-----------MQVLEDMDRDLQTIdeedpETQAELiflleEDISQKMRPSVDELTAL 3385
Cdd:TIGR02168 627 vvddLDNALELAKKLRPGYRIVtldgdlvrpggVITGGSAKTNSSIL-----ERRREI-----EELEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3386 SNQLQVLCSA-----DKADELQTNTIAMNKLVNSVADRVARRAERIEMASKQSRAVLDDLQYLIEWFSAARERILEGAPP 3460
Cdd:TIGR02168 697 EKALAELRKEleeleEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3461 SLDLEVLKSQLKHQRitnEEASANKVQFRNVAGEAKKVARQLGMEGNEANEKISD---TVDEGKELVEEVMALCADRTET 3537
Cdd:TIGR02168 777 LAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESlerRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3538 LERALALMEQLTSQFDE----LNKWLDQMDAELQASPSVTTA--TPAAELREMHDHN-------EELARMVAAYRPIIEG 3604
Cdd:TIGR02168 854 IESLAAEIEELEELIEEleseLEALLNERASLEEALALLRSEleELSEELRELESKRselrrelEELREKLAQLELRLEG 933
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1143463340 3605 FKSDVGSLHEVLAEDQAPLLEsVAGELVQGYEEVREAVRARGHAIDN 3651
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLE-EAEALENKIEDDEEEARRRLKRLEN 979
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1720-2450 |
2.26e-04 |
|
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: 47.66 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1720 LHAMNDEHSEQARRADEWLQmLQNDVEDVDQDPRFQRDEDRIQRIEELNRMAAGGSSQLDDAEQASRRLLTALEGTN--- 1796
Cdd:TIGR00618 181 LALMEFAKKKSLHGKAELLT-LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkq 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1797 -VANDVRARHEELANL--RRGKHQKVIDRLSQNMMEAASRKAEAEGVKQAVENLRQWSEQTAQRTR---QPVQLPLTELD 1870
Cdd:TIGR00618 260 qLLKQLRARIEELRAQeaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKllmKRAAHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1871 LHEARKDEQVLHGEiENRLALIEELEKKAADVGDHAsLAELQEckmklkrsnsdLKGLRDNIFDAINGLQTVNSEGETLS 1950
Cdd:TIGR00618 340 IEEQRRLLQTLHSQ-EIHIRDAHEVATSIREISCQQ-HTLTQH-----------IHTLQQQKTTLTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1951 RAVDSAGAKIrSARLPEAQSEVEALQDQADNLERITNNLCNIPNVTRTEpvIQKSKDLRKrvdsCAQELDARMGKLAELE 2030
Cdd:TIGR00618 407 REQATIDTRT-SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE--KLEKIHLQE----SAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2031 SLDAEFDGAKnklsSFIGAFDDELKGLEKVSIDKEKLAEQRRQ-----------TQDLVDKHSEGNAILDDVEAIAQKVT 2099
Cdd:TIGR00618 480 QIHLQETRKK----AVVLARLLELQEEPCPLCGSCIHPNPARQdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2100 aedpsktgsaqKSVGELGARLQRQASELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQlstgfpvpatkegvKSQL 2179
Cdd:TIGR00618 556 -----------KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA--------------EDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2180 LDLERMNKTGKEEQrrVDDARHSARELAREASVEKEVQDMNQREKKLLDEWEDLAdqfdAVRSRANKA---EQVLNECAQ 2256
Cdd:TIGR00618 611 ACEQHALLRKLQPE--QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH----ALSIRVLPKellASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2257 MEKYIGAKKNMLEGIG----APSTEPGVAKANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKMDrLNR 2332
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAqcqtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKART-EAH 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2333 KWHSLESGLDENAGrvEEAAKLGQELKDIQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLKSRFGGVDKALEKLK 2412
Cdd:TIGR00618 764 FNNNEEVTAALQTG--AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKS 841
|
730 740 750
....*....|....*....|....*....|....*....
gi 1143463340 2413 GIL-EATEELEVDATNRAEiQEQLETTQKKADELERKIE 2450
Cdd:TIGR00618 842 ATLgEITHQLLKYEECSKQ-LAQLTQEQAKIIQLSDKLN 879
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2248-2349 |
3.43e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.70 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2248 EQVLNECAQMEKYIGAKKNMLEGIGAPSTEPGVAKANRAQiQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKM 2327
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKH-EAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1143463340 2328 DRLNRKWHSLESGLDENAGRVE 2349
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
296-411 |
3.49e-04 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 43.23 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 296 DDVSLHGSDATSaRDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILhryrsSAI---------DWNkiSSDSVSNT 366
Cdd:cd21315 6 DDGPDDGKGPTP-KQRLLGW---IQSKVPDLPITNFTNDWNDGKAIGALV-----DALapglcpdweDWD--PKDAVKNA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1143463340 367 ERlnnAFAAADREFGVERLLDAEDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21315 75 KE---AMDLAEDWLDVPQLIKPEEMVNPKVDELSMMTYLSQFPNA 116
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2282-2486 |
3.52e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2282 KANRAQIQSMKAETEGEKSALEHVNSLANELIADGGANVEELMKKMDrlnrkwhslesgldenagrveEAAKLGQELKDI 2361
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYD---------------------ELVEEAKTIKAE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2362 QKELRKELGELESNVEKASAmSSNDIGDQLATLDSLKSRFGGVDKALEK-------LKGILEATEELEVDATNRAEIQEQ 2434
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSA-ALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHS 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1143463340 2435 LE-----------------TTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELEL 2486
Cdd:PHA02562 315 LEkldtaideleeimdefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3464-4248 |
3.73e-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: 46.97 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3464 LEVLKSQLKHQRITNEEAsankVQFRNVAGEAKKVARQL-GMEGNEANEKISDTVDEGKELVEEVMALcadrTETLERAL 3542
Cdd:TIGR02168 195 LNELERQLKSLERQAEKA----ERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELEEL----TAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3543 ALMEQLTSQFDELNKWLDQMDAELQAspsVTTATPAAELREMHdHNEELARMV---AAYRPIIEGFKSDVGSLHEVLAEd 3619
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYA---LANEISRLEQQKQI-LRERLANLErqlEELEAQLEELESKLDELAEELAE- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3620 QAPLLESVAGELvqgyEEVREAVRARGHAIDNMMGATIGFGERLETL---VANLQGAADRLReNEGISADPSV--LESRL 3694
Cdd:TIGR02168 342 LEEKLEELKEEL----ESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLN-NEIERLEARLerLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3695 AENRSIVESLRDKQNAYDaLKQTASELLASAPEGDAAAGDVENKLNRLEKLWKEIEReavdrgvlLEDVLDKAKHFWSEL 3774
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEE--------AEQALDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3775 DSCQKAVDDLRNRLElvEPATGHPEQLADQQEI--MAQVASEMERARPRIE-ALSIA-GKQLADYVPDDEKAVIENQ--V 3848
Cdd:TIGR02168 488 QARLDSLERLQENLE--GFSEGVKALLKNQSGLsgILGVLSELISVDEGYEaAIEAAlGGRLQAVVVENLNAAKKAIafL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3849 ANVRGGFSTITGLFAEKKRDLIAAMEEAMTFHGDLQELLKWLDMAEQKLLK--------MSPVEHAKHMTEIEQLLKELH 3920
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggVLVVDDLDNALELAKKLRPGY 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3921 TF----KDEVHERGVAK--------------------EQVVATALQLAADAPPHLAAtVRQPVADLNTRWSRLNAALAER 3976
Cdd:TIGR02168 646 RIvtldGDLVRPGGVITggsaktnssilerrreieelEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3977 EHKLENLMLQMGKLASTIAQLTAWMDKTRATLKDIAPPKnAVNLRDIEIAQCKLVVLSNDIHAHQDSVNAVNRAAQKYIQ 4056
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4057 TSGALDAEtsdsLKSMNLKWEDIQKVLESLAFDMEVAKKEAENVggeVEKWQRWLEETESALLSTKPTGGLPETAEFQLD 4136
Cdd:TIGR02168 804 ALDELRAE----LTLLNEEAANLRERLESLERRIAATERRLEDL---EEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4137 EFKALKLDVEHNASPLEAHLHATEQHLKEepqdadtwLSKTHGAMKTKWNKVKELLVDREKKLQVAYEQAVALESALNdm 4216
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRE--------LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS-- 946
|
810 820 830
....*....|....*....|....*....|..
gi 1143463340 4217 EDWIIAAERKLTDQPSISRLPDVIEKQLAEHE 4248
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2213-2485 |
3.73e-04 |
|
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: 46.94 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2213 EKEVQDMNQREKKLLDEWEDLADQFDAVRSRANKAEQVLNECAQMEKYIGAKKNMLEgigapstepgvakanrAQIQSMK 2292
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE----------------KEIERLK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2293 AETEGEKSA---LEHVNSLANELIADGGANVEELMKKMDRLNRKWHSLESGLDEN----AGRVEEAAKLGQELKDI---Q 2362
Cdd:TIGR04523 433 ETIIKNNSEikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelKSKEKELKKLNEEKKELeekV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2363 KELRKELGELESNVEKASAMSS------NDIGDQLATLDS------LKSRFGGVDKALEKLK----GILEATEELEVDA- 2425
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKekeskiSDLEDELNKDDFelkkenLEKEIDEKNKEIEELKqtqkSLKKKQEEKQELId 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143463340 2426 ---TNRAEIQEQLETTQKKADELERKIENVKKaalnaQNEGLELEKKldeligTVNSAENELE 2485
Cdd:TIGR04523 593 qkeKEKKDLIKEIEEKEKKISSLEKELEKAKK-----ENEKLSSIIK------NIKSKKNKLK 644
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3474-4030 |
3.80e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3474 QRITNEEASANKVQFRNVAGEAKKVARQLGMEGNEANEKISDTVDEGKELVEEVMALCADRTETLEralALMEQLTSQFD 3553
Cdd:pfam12128 278 QEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAA---ADQEQLPSWQS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3554 ELNKWLDQMDAELQASPSVTTATPAAELREMHDHNEELARMVAAYRPIIEGFKSDVGSLHEVLAEDQAPLLESVAGELVQ 3633
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3634 GYEEVREAVRARGHAIDNMMGATIgfGERLETLVANLQGAADRLRENEGiSADPSVleSRLAENRSIVESLRDKQN---- 3709
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATA--TPELLLQLENFDERIERAREEQE-AANAEV--ERLQSELRQARKRRDQASealr 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3710 -AYDALKQTASELLASAPEGDAAAGDVENKLNRLEKLWKEIEREAVDRGVLLEDVLDKAkhFWSELDSCQKAVDDLRNRL 3788
Cdd:pfam12128 510 qASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPE--VWDGSVGGELNLYGVKLDL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3789 ELVEpatgHPEQLADQQEI---MAQVASEMERARPRIEALSIAGKQLADYVpDDEKAVIENQVANVRGGFSTITGLFAEk 3865
Cdd:pfam12128 588 KRID----VPEWAASEEELrerLDKAEEALQSAREKQAAAEEQLVQANGEL-EKASREETFARTALKNARLDLRRLFDE- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3866 KRDLIAAMEEAMTFHGDL-QELLKWLDmAEQKLLKMspvEHAKHMTEIEQLLKELHTFKDE-----VHERGVAKEQVVAT 3939
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSaNERLNSLE-AQLKQLDK---KHQAWLEEQKEQKREARTEKQAywqvvEGALDAQLALLKAA 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3940 ALQLAADAPPHLAATVRQPVADLNTR------WSRLNAALAEREHKLENLmlqmGKLASTIAQLTAWMDKTRATLKdiap 4013
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLgvdpdvIAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRR---- 809
|
570
....*....|....*..
gi 1143463340 4014 PKNAVNLRDIEIAQCKL 4030
Cdd:pfam12128 810 PRLATQLSNIERAISEL 826
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2338-2815 |
5.10e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.59 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2338 ESGLDENaGRVEEAAKLGQELKDIQKELRKELGELesnvekasamssNDIGDQLATLDSLKSrfgGVDKALEKLKGILEA 2417
Cdd:pfam13166 72 EENLSEQ-GEIKPIFTLGEESIEIQEKIAKLKKEI------------KDHEEKLDAAEANLQ---KLDKEKEKLEADFLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2418 TEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNegLELEKKLDELIGTVNsaENELELAAPIAAESLKL 2497
Cdd:pfam13166 136 ECWKKIKRKKNSALSEALNGFKYEANFKSRLLREIEKDNFNAGV--LLSDEDRKAALATVF--SDNKPEIAPLTFNVIDF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2498 aDELKRAEELFQKLIeneGDVSLIrakvaEELKKKPDAelkkklellyQKWPKA-LGAARDRKDL---------VSKAGD 2567
Cdd:pfam13166 212 -DALEKAEILIQKVI---GKSSAI-----EELIKNPDL----------ADWVEQgLELHKAHLDTcpfcgqplpAERKAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2568 LVKQFGDQVQALEQRLQGDQAELDELLASDKAhdpevcdalklveltmarRLADVDALNavmnrIESSAPGPDANRLRRR 2647
Cdd:pfam13166 273 LEAHFDDEFTEFQNRLQKLIEKVESAISSLLA------------------QLPAVSDLA-----SLLSAFELDVEDIESE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2648 ADTLSDDAKGMAKKartaadLAQRKQGLAKKFE--RLCDEVSQFTENQkAEIQDAIEKdllNAERVQ---SKLNK-IDDF 2721
Cdd:pfam13166 330 AEVLNSQLDGLRRA------LEAKRKDPFKSIEldSVDAKIESINDLV-ASINELIAK---HNEITDnfeEEKNKaKKKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2722 WSSNSRELKnvgdeIKIDATPEDAQAVDTKLAELQAGIDGLLATLQEQNvhlEEKREQANRVQSEsQKAAGKINSLVAEi 2801
Cdd:pfam13166 400 RLHLVEEFK-----SEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLR---EEIKELEAQLRDH-KPGADEINKLLKA- 469
|
490
....*....|....
gi 1143463340 2802 adldpIGRSRDELQ 2815
Cdd:pfam13166 470 -----FGFGELELS 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2332-2768 |
5.94e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2332 RKWHSLESGLDENAGRVEEAAKLGQELKDIQKE---LRKELGELESNVEKASAMSSNdiGDQLATLDSLKSRFGGVDKAL 2408
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEleeLEAELEELREELEKLEKLLQL--LPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2409 EKLKGILEATEELEVDatnRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLE-LEKKLDELIGTVNSAENELEla 2487
Cdd:COG4717 149 EELEERLEELRELEEE---LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEeLQQRLAELEEELEEAQEELE-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2488 apIAAESLKLADELKRAEELFQKLIENEGDVSLIRAKVAEELkkkpdaeLKKKLELLYQKWPKAL----GAARDRKDLVS 2563
Cdd:COG4717 224 --ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLflvlGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2564 KAGDLVKQFGDQVQALEQRLQGDQAELDELLAsdKAHDPEVCDALKLVELtmARRLADVDALNAVMNRIESSApgpDANR 2643
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLA--ALGLPPDLSPEELLEL--LDRIEELQELLREAEELEEEL---QLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2644 LRRRADTLSDDAKGMAKKA-RTAADLAQRKQGLAKKFERLCDEVSQFTENQKAEIQDaiekdlLNAERVQSKLNKIDDFW 2722
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA------LDEEELEEELEELEEEL 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1143463340 2723 SSNSRELKNVGDEI-KIDATPEDAQAvDTKLAELQAGIDGLLATLQE 2768
Cdd:COG4717 442 EELEEELEELREELaELEAELEQLEE-DGELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1966-2513 |
6.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1966 PEAQSEVEALQDQADNLERITNNLCNIpnvtrtepviQKSKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLss 2045
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDA----------REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2046 FIGAFDDELKGLEKvsiDKEKLAEQRRQTQDLVDKHsegNAILDDVEAiaqkvtaedpsktgsAQKSVGelGARLQRQAS 2125
Cdd:COG4913 289 RLELLEAELEELRA---ELARLEAELERLEARLDAL---REELDELEA---------------QIRGNG--GDRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2126 ELKARGDKINKLDSKATSFAESEAAVlgyiekqkdqlstGFPVPATKEGVKSQLLDLERMNKTGKEEQRRVDDARHSARE 2205
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAAL-------------GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2206 LAREA-----SVEKEVQDMNQReKKLLDEWedLADQFDAVRSRANKAE----------QVLNECAQ----MEKYIGAKKN 2266
Cdd:COG4913 413 ALRDLrrelrELEAEIASLERR-KSNIPAR--LLALRDALAEALGLDEaelpfvgeliEVRPEEERwrgaIERVLGGFAL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2267 MLegIGAPSTEPGVAKA-----NRAQIQSMKAETEGEKSALE--HVNSLANELIADGGA-------------------NV 2320
Cdd:COG4913 490 TL--LVPPEHYAAALRWvnrlhLRGRLVYERVRTGLPDPERPrlDPDSLAGKLDFKPHPfrawleaelgrrfdyvcvdSP 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2321 EEL---------------------MKKMDRLNRKW----------HSLESGLDENAGRVEEAAKLGQELKDIQKELRK-- 2367
Cdd:COG4913 568 EELrrhpraitragqvkgngtrheKDDRRRIRSRYvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQErr 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2368 -------ELGELESNVEKASAMSSnDIGDQLATLDSLKSRFGGVDKALEKLKGILEATEELevdatnRAEIQEQLETTQK 2440
Cdd:COG4913 648 ealqrlaEYSWDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELEELEEE------LDELKGEIGRLEK 720
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143463340 2441 KADELERKIENVKKAALNAQNEG-LELEKKLDELIGTVNSAENELELAAPIAAESLKLADELKRAEELFQKLIE 2513
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLArLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2746-2907 |
6.74e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2746 QAVDTKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKINSLVAEIADLD----------PIGRSRDELQ 2815
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyeeqlGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2816 KQKKEVVELAGDLGSAQTKMLELGAEWEAALgagivaqpvfEMNRAATDELNKLAARAGKRLAQREKKITETEDEIDKLH 2895
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELE----------EELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1143463340 2896 ADADQIVGALEA 2907
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2289-2550 |
6.98e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.79 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2289 QSMKAETEGEKSALEHVNSLANELIADGGANVEELMK-KMDRLNRKWHslESGLDENAGRVEEAAKLGQELKDIQKELRK 2367
Cdd:pfam05667 258 SAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLtKGSRFTHTEK--LQFTNEAPAATSSPPTKVETEEELQQQREE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2368 ELGELESNvekasamssndigdqlatLDSLKSRfggvdkaleklkgILEATEELEVDATNRAEIQEQLETTQKKADELER 2447
Cdd:pfam05667 336 ELEELQEQ------------------LEDLESS-------------IQELEKEIKKLESSIKQVEEELEELKEQNEELEK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2448 KIENVKKAA---LNAQNEGLELEKKLDEligtvnSAENELELA-------APIAAESLKLADEL-KRAEELFQKLIENEG 2516
Cdd:pfam05667 385 QYKVKKKTLdllPDAEENIAKLQALVDA------SAQRLVELAgqwekhrVPLIEEYRALKEAKsNKEDESQRKLEEIKE 458
|
250 260 270
....*....|....*....|....*....|....
gi 1143463340 2517 DVSLIRaKVAEELKKKpdAELKKKLELLYQKWPK 2550
Cdd:pfam05667 459 LREKIK-EVAEEAKQK--EELYKQLVAEYERLPK 489
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2318-2601 |
7.38e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2318 ANVEELMKKMDRLNRKWHSLESGLDEnagrveeaakLGQELKDIQKELRKELGELESNVEKASAMSS--NDIGDQLATL- 2394
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDE----------LNEELKELAEKRDELNAQVKELREEAQELREkrDELNEKVKELk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2395 DSLKSRFGGVDKALEKLKGILEATEELEVDATNRAEIQ---EQLETTQ--------------KKADELERKIENVKKAaL 2457
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRkeiERLEWRQqtevlspeeekelvEKIKELEKELEKAKKA-L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2458 NAQNEGLELEKKLDELIGTVNSAENEL-ELAAPIAAESLKLADELKRAEELFQKLIENEGDVSLIRAKvAEELKKKPDAE 2536
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIkELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK-ADELHEEIIEL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 2537 LKKKLELLyqkwpKALGAARDRKDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDELLASDKAHD 2601
Cdd:COG1340 236 QKELRELR-----KELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEELKLLQKSGL 295
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3416-3819 |
8.07e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3416 ADRVARRAERIEMASKQSRAVLDDLQY---LIEWFSAARERiLEGAPPSLDLEVLKSQLKHQRITN--EEASANKVQFRN 3490
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLddaDAEAVEARREE-LEDRDEELRDRLEECRVAAQAHNEeaESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3491 VAGEAKKVARQLGMEGNEANEKISD---TVDEGKELVEEVMALCADRTETLERALALMEQLTSQFDELNkwldQMDAELQ 3567
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR----EREAELE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3568 aspsvttatpaAELREMHDHNEELARMVAAYR-PiiEGFKSDVGSLHEVLAEDQAPLLESVAGELvqgyEEVREAVRARG 3646
Cdd:PRK02224 433 -----------ATLRTARERVEEAEALLEAGKcP--ECGQPVEGSPHVETIEEDRERVEELEAEL----EDLEEEVEEVE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3647 HAIdnmmgatigfgERLETLVAnLQGAADRLRENEgisadpSVLESRLAENRSIVESLRDKQnayDALKQTASELLASAP 3726
Cdd:PRK02224 496 ERL-----------ERAEDLVE-AEDRIERLEERR------EDLEELIAERRETIEEKRERA---EELRERAAELEAEAE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3727 EGDAAAGDVENKLNRLEKLWKEIEREavdRGVLLE--DVLDKAKHFWSELDSCQKAVDDLRNRLE-LVEPATGHPEQLAD 3803
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSK---LAELKEriESLERIRTLLAAIADAEDEIERLREKREaLAELNDERRERLAE 631
|
410
....*....|....*.
gi 1143463340 3804 QQEIMAQVASEMERAR 3819
Cdd:PRK02224 632 KRERKRELEAEFDEAR 647
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3799-4536 |
8.22e-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: 46.20 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3799 EQLADQQEIMAQVASEMERARPRIEALSIAGKQLadyvpDDEKAVIENQVANVRGGFSTITGLFAEKKRDLIAAMEEAMT 3878
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEEL-----RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3879 FHGDLQELLKWLDMAEQKLLKMSpvEHAKHMTEIEQLLKELHTFKDEVHERGVAKEQVVATALQlaadapphlaatvrqp 3958
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELA--EELAELEEKLEELKEELESLEAELEELEAELEELESRLE---------------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3959 vaDLNTRWSRLNAALAEREHKLENLMLQMGKLASTIAQLTAWMDKTRATLKDIAPPKNAVNLRDIEIAQCKLVVLSNDIH 4038
Cdd:TIGR02168 376 --ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4039 AHQDSVNAVNRAAQKYIQTSGALDAETSDSLKSMNLKWEDIQKVLESLAFDMEVAK---KEAENVGGEV----------E 4105
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKallKNQSGLSGILgvlselisvdE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4106 KWQRWLEetesALLSTKPTGGLPETAEFQLDEFKALKLDVEHNASPLEAhlhateqhlkeePQDADTWLSKTHGAMKTKW 4185
Cdd:TIGR02168 534 GYEAAIE----AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL------------DSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4186 NKVKELLVDREK---KLQVA-------------YEQAVALESALNDMEDWIIAAERKLTDQPSISRLPDVIEKQLAEHES 4249
Cdd:TIGR02168 598 EGFLGVAKDLVKfdpKLRKAlsyllggvlvvddLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4250 WMEEVAgRKMAMTKHQASGVHMQYYCEKKDAIPIKNRLVSLKHRVEKISGRTAERAKQLAVTRDEVATWQDGLHDLEHFI 4329
Cdd:TIGR02168 678 EIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4330 SDVLVKIAP-EPNTTSSLEKLKAKLEEVKEAQRDVTAKQTLFDVTRKRGIGL--AERATRSEYKQISMTNEKMSKKWAEM 4406
Cdd:TIGR02168 757 TELEAEIEElEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4407 LKKLRDRLREAEQAVLEGGAFEESMNDLESWVDDELERYQKAEHEpVFADIDGVRALVDEESRRSAERKTKENGVKTVVK 4486
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE-RASLEEALALLRSELEELSEELRELESKRSELRR 915
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1143463340 4487 KADALMASGVDEKDSIAQAK-------ERLVEKWNQVEEAARHRGNSIKEAEQAAEE 4536
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEvridnlqERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2301-2519 |
9.18e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2301 ALEHVNSLANELIADGGANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELESNVEKAS 2380
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2381 A----------MSSNDIGDQLATLDS-----LKSRFGGVDKALEKLKGILEATEELEVDATN-RAEIQEQLETTQKKADE 2444
Cdd:COG3883 86 EelgeraralyRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEELKADKAELEAkKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1143463340 2445 LERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAAPIAAESLKLADELKRAEELFQKLIENEGDVS 2519
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
307-411 |
9.51e-04 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 42.00 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNkiSSDSVSNTERLNNAFAAADREFGVERL 385
Cdd:cd21313 8 TPKQRLLGW---IQNKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWE--SWDPQKPVDNAREAMQQADDWLGVPQV 82
|
90 100
....*....|....*....|....*.
gi 1143463340 386 LDAEDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21313 83 ITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2744-2907 |
9.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2744 DAQAVDTKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKINSLVAEIADLdpigrsRDELQKQKKEVVE 2823
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA------EAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2824 LAGDL--GSAQTKMLE--LGAE-WEAALGAGIVAQPVFEMNRAATDELNKLAAragkRLAQREKKITETEDEIDKLHADA 2898
Cdd:COG3883 91 RARALyrSGGSVSYLDvlLGSEsFSDFLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAELEALKAEL 166
|
....*....
gi 1143463340 2899 DQIVGALEA 2907
Cdd:COG3883 167 EAAKAELEA 175
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2318-2538 |
9.83e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2318 ANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRK------ELGELE------SNVEK------- 2378
Cdd:COG0497 151 AGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgEEEELEeerrrlSNAEKlrealqe 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2379 -ASAMSSNDIG--DQLATLDSLKSRFGGVDKALEKLKGILE-ATEELEvDATNR-AEIQEQLETTQKKADELERKIenvk 2453
Cdd:COG0497 231 aLEALSGGEGGalDLLGQALRALERLAEYDPSLAELAERLEsALIELE-EAASElRRYLDSLEFDPERLEEVEERL---- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2454 kAALNAqnegleLEKK----LDELIGTVNSAENELELAAPIAAESLKLADELKRAEELFQKLIEnegDVSLIRAKVAEEL 2529
Cdd:COG0497 306 -ALLRR------LARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAE---KLSAARKKAAKKL 375
|
....*....
gi 1143463340 2530 KKKPDAELK 2538
Cdd:COG0497 376 EKAVTAELA 384
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1777-2379 |
9.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1777 QLDDAEQASRRLLTALEGTNVA----NDVRARHEELANLRRGKHQK---VIDRLSQNMMEAASRKAEAEGVKQAVENLRQ 1849
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRierlEKFIKRTENIEELIKEKEKEleeVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1850 WSEQTAQRTRQpvqlplTELDLHEARKDEQVLhGEIENRLA----LIEELEKKAADVGDHASLAE----LQECKMKLKRS 1921
Cdd:PRK03918 236 LKEEIEELEKE------LESLEGSKRKLEEKI-RELEERIEelkkEIEELEEKVKELKELKEKAEeyikLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1922 NSDLKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAKI-----RSARLPEAQSEVEALQDQADNLERITNNLCNIPnvt 1996
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLT--- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1997 rTEPVIQKSKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGA-------FDDELKglekvsidKEKLAE 2069
Cdd:PRK03918 386 -PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHR--------KELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2070 QRRQTQDLVDKHSEGNAILDDVEAIAQKVtaedpsktgsaqksvgELGARLQRQASELKARGDKINKLDSKATSFAESEa 2149
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELREL----------------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEE- 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2150 avlgyIEKQKDQLstgfpvpatkEGVKSQLLDLERMNKTGKEEQRRVDDARHSARELareasvEKEVQDMNQREKKLLDE 2229
Cdd:PRK03918 520 -----LEKKAEEY----------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL------EKKLDELEEELAELLKE 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2230 WEDLA-DQFDAVRSRANKAEQVLNECAQM---EKYIGAKKNMLEgigapSTEPGVAKAnRAQIQSMKAETEGEKSALEHV 2305
Cdd:PRK03918 579 LEELGfESVEELEERLKELEPFYNEYLELkdaEKELEREEKELK-----KLEEELDKA-FEELAETEKRLEELRKELEEL 652
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1143463340 2306 NSLANEliadggANVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKDIQKELRKELGELEsNVEKA 2379
Cdd:PRK03918 653 EKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKA 719
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
307-410 |
9.98e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.90 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWA----RRvtAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAIDwNKISSDSVSNTERLNNA---FAAAdRE 379
Cdd:cd21218 10 PPEEILLRWVnyhlKK--AGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCD-KELVLEVLSEEDLEKRAekvLQAA-EK 85
|
90 100 110
....*....|....*....|....*....|.
gi 1143463340 380 FGVERLLDAEDVDTNNPDEksIITYVSSLYN 410
Cdd:cd21218 86 LGCKYFLTPEDIVSGNPRL--NLAFVATLFN 114
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3437-3539 |
1.10e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3437 LDDLQYLIEWFSAArERILEGAPPSLDLEVLKSQLKHQRITNEEASANKVQFRNVageaKKVARQLGMEGNEANEKISDT 3516
Cdd:smart00150 4 LRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL----NELGEQLIEEGHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1143463340 3517 VDEGKELVEEVMALCADRTETLE 3539
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1749-2456 |
1.28e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1749 DQDPRFQRDEDRIQRIEELNRMAAGGSSQLDDAEQASRRLLTaLEGTNVANDVR--ARHEELANLRRGKHQKVI---DRL 1823
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSH-LHFGYKSDETLiaSRQEERQETSAELNQLLRtldDQW 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1824 SQNMMEAASRKAEAEGvkqAVENLRQWSEQTAQRTRQPVQLPLTELDLHEARKDEqvLHGEIENRLALIEELEKKAADVg 1903
Cdd:pfam12128 300 KEKRDELNGELSAADA---AVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS--WQSELENLEERLKALTGKHQDV- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1904 DHASLAELQECKMKLKRSNSDLKGLRDNIFDAINGLQTVnseGETLSRAVDSAGAKIRSARLPEAQSEVEALQDQADNLE 1983
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAV---AEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1984 RITNNlcnipnVTRTEPVIQKSKDLRKRVDSCAQELDARMGKLAELESLDAEFDGAKNKLSSFIGafDDELKGLEKVSID 2063
Cdd:pfam12128 451 LRLNQ------ATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR--QASRRLEERQSAL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2064 KEKLAEQRRQTQDLVdkHSEGNAILDDVEAIAQKVTAE-------DPSKTGSAQK---SVGELGARLQR--------QAS 2125
Cdd:pfam12128 523 DELELQLFPQAGTLL--HFLRKEAPDWEQSIGKVISPEllhrtdlDPEVWDGSVGgelNLYGVKLDLKRidvpewaaSEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2126 ELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQLSTGFPVPATkeGVKSQLLDLERMNKTGKEEQRRVDDARHSare 2205
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART--ALKNARLDLRRLFDEKQSEKDKKNKALAE--- 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2206 laREASVEKEVQDMNQREKKLLDEWEDLADQFDAVRSRANKAEQvlnecAQMEKYIGAKKNMLEGIGApstepgvakANR 2285
Cdd:pfam12128 676 --RKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ-----AYWQVVEGALDAQLALLKA---------AIA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2286 AQIQSMKAETEGEKSalEHVNSLAN-----ELIADGGANVEELMKKMDRLNRKWHSL--------ESGLDENAGRVEEAA 2352
Cdd:pfam12128 740 ARRSGAKAELKALET--WYKRDLASlgvdpDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLS 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2353 KLGQElkdiQKELRKELGELESNVEKASAmssnDIGDQLATLDSLKSRfggVDKALEKLKGILEATEELEVDATNrAEIQ 2432
Cdd:pfam12128 818 NIERA----ISELQQQLARLIADTKLRRA----KLEMERKASEKQQVR---LSENLRGLRCEMSKLATLKEDANS-EQAQ 885
|
730 740
....*....|....*....|....
gi 1143463340 2433 EQLETTQKKADELERKIENVKKAA 2456
Cdd:pfam12128 886 GSIGERLAQLEDLKLKRDYLSESV 909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4346-4658 |
1.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4346 LEKLKAKLEEVkEAQRDVTAKQtlfdvtrkrgiglAERATRseYKQISmtnEKMSKKWAEmLKKLRDRLREAEQAVLEgg 4425
Cdd:COG1196 188 LERLEDILGEL-ERQLEPLERQ-------------AEKAER--YRELK---EELKELEAE-LLLLKLRELEAELEELE-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4426 afeESMNDLESWVDDELERYQKAEhepvfADIDGVRALVDEESRRSAERKTKENGVKTVVKKADALMASGVDEKDSIAQA 4505
Cdd:COG1196 246 ---AELEELEAELEELEAELAELE-----AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4506 KERLVEKWNQVEEAARHRGNSIKEAEQAAEEFDAKTHALLDWLAVEEQKLKASgLDEVEGVKQEMDEAKGRYQECLKKGE 4585
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1143463340 4586 EILSKCQPAAEPILRNwmrvvEARWKEVSEKVDEREFTLLEQEQKAKEQNEQIEKLAKFAAQKREELNRMIEQ 4658
Cdd:COG1196 397 ELAAQLEELEEAEEAL-----LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2603-2845 |
2.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2603 EVCDALKLVELTMARRLADVDALNAVMNRIESSAP-----------GPDANRLRRRADTLSD-------DAKgMAKKART 2664
Cdd:COG3206 98 RVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVkgsnvieisytSPDPELAAAVANALAEayleqnlELR-REEARKA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2665 AADLAQRKQGLAKKFERLCDEVSQFTENQKAEIQDAIEKDLLNA--------ERVQSKLNKIDDFWSSNSRELKNVGDEI 2736
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQlselesqlAEARAELAEAEARLAALRAQLGSGPDAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2737 KIDATPEDAQAVDTKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKI-NSLVAEIADLDpigRSRDELQ 2815
Cdd:COG3206 257 PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQ---AREASLQ 333
|
250 260 270
....*....|....*....|....*....|
gi 1143463340 2816 KQKKEVVELAGDLGSAQTKMLELGAEWEAA 2845
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREVEVA 363
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3674-3761 |
2.27e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3674 ADRLRENEGISADPSVLESRLAENRSIVESLRDKQNAYDALKQTASELLASAPEgdaAAGDVENKLNRLEKLWKEIEREA 3753
Cdd:smart00150 17 KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP---DAEEIEERLEELNERWEELKELA 93
|
....*...
gi 1143463340 3754 VDRGVLLE 3761
Cdd:smart00150 94 EERRQKLE 101
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2406-2594 |
2.81e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2406 KALEKLKGILEATEELEVDATNRAEIQEQlettQKKADELERKIENVKKAALNAQNEGLELEKKLDEligtvNSAENELE 2485
Cdd:PRK09510 88 QAEELQQKQAAEQERLKQLEKERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----AEAKRAAA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2486 LAAPIAAESLKLADE--LKRAEELFQKLIENEGdvsliRAKVAEELKKKPDAELKKKLELLYQKWPKALGAARDRKDLVS 2563
Cdd:PRK09510 159 AAKKAAAEAKKKAEAeaAKKAAAEAKKKAEAEA-----AAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE 233
|
170 180 190
....*....|....*....|....*....|.
gi 1143463340 2564 KAGDLVKQFGDQVQALEQRlQGDQAELDELL 2594
Cdd:PRK09510 234 AKAAAEKAAAAKAAEKAAA-AKAAAEVDDLF 263
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3008-3105 |
3.10e-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 characteriztic 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: 40.38 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3008 RALLNWLEETEEMMENRKKPSaDAKVAKAQLHDYEVLMKHVEDKKPSVDGFKAMIEKIVAEASSDEEkkALGNKNAQIED 3087
Cdd:pfam00435 11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE--EIQERLEELNE 87
|
90
....*....|....*...
gi 1143463340 3088 RYKDLLNSAVDRQRKLLD 3105
Cdd:pfam00435 88 RWEQLLELAAERKQKLEE 105
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
307-411 |
3.10e-03 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 40.56 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 307 SARDALLQWarrVTAGYPRVNVNNFSSSWRDGLAFNAILHRYRSSAI-DWNkiSSDSVSNTERLNNAFAAADREFGVERL 385
Cdd:cd21312 12 TPKQRLLGW---IQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWD--SWDASKPVTNAREAMQQADDWLGIPQV 86
|
90 100
....*....|....*....|....*.
gi 1143463340 386 LDAEDVDTNNPDEKSIITYVSSLYNA 411
Cdd:cd21312 87 ITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2281-2547 |
3.33e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2281 AKANRAQIQSMKAETEGEKSALEHVNSLANELIAdggaNVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKD 2360
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKRDELNE----KVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2361 IQKELRKELGELESNVEKASAmsSNDIGDQLATLDslksrfggvdKALEKLKGILEATEELevdatnrAEIQEQLETTQK 2440
Cdd:COG1340 114 LRKEIERLEWRQQTEVLSPEE--EKELVEKIKELE----------KELEKAKKALEKNEKL-------KELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2441 KADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELElaapiaaESLKLADEL-KRAEELFQKLIENEGDVS 2519
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIV-------EAQEKADELhEEIIELQKELRELRKELK 247
|
250 260
....*....|....*....|....*...
gi 1143463340 2520 LIRAKVAEELKKKPDAELKKKLELLYQK 2547
Cdd:COG1340 248 KLRKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4276-4586 |
3.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4276 EKKDAIPIKNRLVSLKHRVEKISGRTAERAKQLAVTRDEVATWQDGLHDLEHFISDVLVKIAPEPNTTSSLEKLKA--KL 4353
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKA 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4354 EEVKEAQRDVTAKQTLFDVTRKRGIglAERATRSEYKQISMTNEKMSKKWAEMLKKLRDRLREAEQAVLEggafEESMND 4433
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKK 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4434 LESWVDDELERYQKAEHEPVFADIDGVRAL----VDEESRRSAE--RKTKENGVKTV----------------------- 4484
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakKAEEDKKKAEeaKKAEEDEKKAAealkkeaeeakkaeelkkkeaee 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4485 VKKADALMASGVDEKDSIAQAKERLVEKWNQVEEAARHRGNSIKEAEQAAEEFDAKTHALLDWLAVEEQKLKASGLDEVE 4564
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
330 340
....*....|....*....|..
gi 1143463340 4565 GVKQEMDEAKGRYQECLKKGEE 4586
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKE 1816
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4535-4624 |
3.55e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4535 EEFDAKTHALLDWLAVEEQKLKASG-----------LDEVEGVKQEMDEAKGRYQECLKKGEEILSKCQPAAEPIlRNWM 4603
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDlgkdlesvealLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI-EERL 79
|
90 100
....*....|....*....|.
gi 1143463340 4604 RVVEARWKEVSEKVDEREFTL 4624
Cdd:smart00150 80 EELNERWEELKELAEERRQKL 100
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2349-2598 |
3.71e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2349 EEAAKLGQELKDIQKELRKELGELESNVEKASAmssndIGDQLATLDslksrfggvdkaleklKGILEATEELEVDATNR 2428
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA-----LLKQLAALE----------------RRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2429 AEIQEQLETTQKKADELERKIEnvkkaalnaqneglELEKKLDELIGTVNSAENELELAAPIAAESlklADELKRAEELF 2508
Cdd:COG4942 79 AALEAELAELEKEIAELRAELE--------------AQKEELAELLRALYRLGRQPPLALLLSPED---FLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2509 QKLIENegdvsliRAKVAEELKKKPD--AELKKKLELLYQKWPKALGAARDRKDLVSKAgdlVKQFGDQVQALEQRLQGD 2586
Cdd:COG4942 142 KYLAPA-------RREQAEELRADLAelAALRAELEAERAELEALLAELEEERAALEAL---KAERQKLLARLEKELAEL 211
|
250
....*....|..
gi 1143463340 2587 QAELDELLASDK 2598
Cdd:COG4942 212 AAELAELQQEAE 223
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
4347-4736 |
3.98e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4347 EKLKAKLEEVKEAQRDVTAKQTLFDVTRKRGIGLaERATRSEYKQISMTNEKMSKKWAEMLKKLRDRLREAEQAVL-EGG 4425
Cdd:COG5185 129 EIVALKDELIKVEKLDEIADIEASYGEVETGIIK-DIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTvNSI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4426 AFEESMNDLeswVDDELERYQKAEHEPVFADidgvRALVDEESRRSaERKTKENGVKTVVKKADALMASGVDEKdsiaqa 4505
Cdd:COG5185 208 KESETGNLG---SESTLLEKAKEIINIEEAL----KGFQDPESELE-DLAQTSDKLEKLVEQNTDLRLEKLGEN------ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4506 kerlVEKWNQVEEAarhRGNSIKEAEQAAEEFDAKTHALLDWLAVE---EQKLKASGLDEVEGVKQEMDEAKGRYQECLK 4582
Cdd:COG5185 274 ----AESSKRLNEN---ANNLIKQFENTKEKIAEYTKSIDIKKATEsleEQLAAAEAEQELEESKRETETGIQNLTAEIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4583 KGEEILSKCQPAAEPILRNwmRVVEARWKEVSEKVDEREFTL-----------LEQEQKAKEQNEQIEKLAKFAAQKREE 4651
Cdd:COG5185 347 QGQESLTENLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIestkesldeipQNQRGYAQEILATLEDTLKAADRQIEE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 4652 LNRMIEQPPAQdldtMEQNICDFANLDSELREQQPEVDAACKSAKKGARNPAAEMLSTEWKKLWLDAMGLQSSLDNQKAL 4731
Cdd:COG5185 425 LQRQIEQATSS----NEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAT 500
|
....*
gi 1143463340 4732 LEEMK 4736
Cdd:COG5185 501 LEKLR 505
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1288-1402 |
4.09e-03 |
|
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: 42.05 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1288 RINEGHHPDVDAIEDEVQKLNVRWENVNSQIASRLLAVESALQIQMVYRSEYETEmSWLDTVEETINRLRKPEELrpEQY 1367
Cdd:cd00176 65 QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDL--ESV 141
|
90 100 110
....*....|....*....|....*....|....*
gi 1143463340 1368 QQQLDMLIAEYTNLQEHTQAIEHVNKEGGRFIHEA 1402
Cdd:cd00176 142 EELLKKHKELEEELEAHEPRLKSLNELAEELLEEG 176
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2680-3163 |
4.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2680 ERLCDEVSQFTENQKAEIQDAIEKDL---LNAERvqSKLNKIDDfwssnsrELKNVGDE-IKIDATPEDAQAV------- 2748
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLherLNGLE--SELAELDE-------EIERYEEQrEQARETRDEADEVleeheer 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2749 DTKLAELQAGIDGLLATLQEQNVHLEEKREQANRVQSESQKAAGKINSLVAEI----ADLDPIGRSRDELQKQKKEVVEl 2824
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddADAEAVEARREELEDRDEELRD- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2825 agDLGSAQTKMLELGAEWEAALGAGIVAQPVFEMNRAATDELNKLAARAGKRLAQREKKITETEDEIDKLhadadqivga 2904
Cdd:PRK02224 329 --RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL---------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2905 leaiakDEALQGAPSQLLDPKQVSEKVRQLKESLKpvgEKMDAFNTDckllIKTAgpESDTKELDSLLK--KVGDAYSDV 2982
Cdd:PRK02224 397 ------RERFGDAPVDLGNAEDFLEELREERDELR---EREAELEAT----LRTA--RERVEEAEALLEagKCPECGQPV 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2983 VGkvsdkEMSVDAAVQQQGKVEDaYRALLNWLEETEEMMENRKKPSADAKVAKAQlhdyevlmkhVEDKKPSVDGFKAMI 3062
Cdd:PRK02224 462 EG-----SPHVETIEEDRERVEE-LEAELEDLEEEVEEVEERLERAEDLVEAEDR----------IERLEERREDLEELI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3063 EKIVAEASSDEEKKALGNKNAQiedrykDLLNSAVDRQRKLLDAVDLAERLQEVTIPLDSWLQSADKRLQALAKVPITVE 3142
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAA------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
|
490 500
....*....|....*....|.
gi 1143463340 3143 KAEEMIGEQEALQDELEHKSD 3163
Cdd:PRK02224 600 AIADAEDEIERLREKREALAE 620
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3989-4084 |
4.48e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.62 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3989 KLASTIAQLTAWMDKTRATLKDIAPPKNavnLRDIEIAQCKLVVLSNDIHAHQDSVNAVNRAAQKYIQTSGALDAETSDS 4068
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKD---LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
|
90
....*....|....*.
gi 1143463340 4069 LKSMNLKWEDIQKVLE 4084
Cdd:smart00150 79 LEELNERWEELKELAE 94
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1884-2472 |
4.57e-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: 43.56 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1884 EIENRLALIEELEKKAADVGDHASlAELQECKMKLKRSNSDLKGLRDNIFDAINGLQTVNSEGETLSRAVDSAGAkirsa 1963
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLT-KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA----- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1964 rlpeAQSEVealqdqadnLERITNNLCNIPNVTRTEPviQKSKDLRKRVDSCAQELDARMGKLAELESLdaefdgAKNKl 2043
Cdd:pfam05483 346 ----AHSFV---------VTEFEATTCSLEELLRTEQ--QRLEKNEDQLKIITMELQKKSSELEEMTKF------KNNK- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2044 ssfigafDDELKGLEKVSIDKEKLAEQRRQtqdlvdkhsegnailddVEAIAQkvtaedpsktgsaqksvgELGARLQRQ 2123
Cdd:pfam05483 404 -------EVELEELKKILAEDEKLLDEKKQ-----------------FEKIAE------------------ELKGKEQEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2124 ASELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQLStgfpvpatKEGVKSQLLDlERMNKTGKEEQRRVDDARHSA 2203
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE--------KEKLKNIELT-AHCDKLLLENKELTQEASDMT 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2204 RELAREasvEKEVQDMNQREKKLLDEWEDLADQFDAVRsraNKAEQVLNECAQMEKYIGAKKNMLEGiGAPSTEPGVAKA 2283
Cdd:pfam05483 513 LELKKH---QEDIINCKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVKCKLDKSEE-NARSIEYEVLKK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2284 NRaQIQSMKAETEGEKSALEHVNSLANELIADGGAnveeLMKKMDRLNRKWHSLESGLDENAGRVEEAA-KLGQELKDIQ 2362
Cdd:pfam05483 586 EK-QMKILENKCNNLKKQIENKNKNIEELHQENKA----LKKKGSAENKQLNAYEIKVNKLELELASAKqKFEEIIDNYQ 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2363 KELR-KELGE--LESNVEKASAMSSNDIGDQLATLDSLKSRFGGVDKALEKLKGILEATEELEVDATNRAEIQEQLETTQ 2439
Cdd:pfam05483 661 KEIEdKKISEekLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA 740
|
570 580 590
....*....|....*....|....*....|...
gi 1143463340 2440 KKAdeLERKIENVKKAALNAQNEgLELEKKLDE 2472
Cdd:pfam05483 741 KAA--LEIELSNIKAELLSLKKQ-LEIEKEEKE 770
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2281-2703 |
4.63e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2281 AKANRAQIQSMKAETEGEKSALEHVNSLANELIAdgganVEELMKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQELKD 2360
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2361 IQKELRKELGELESNVEKASAMSSNDIGDQLATLDSLKSRFGGVDKALEKLKGILEATEElevdatNRAEIQEQLEttqk 2440
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE------ELEQLENELE---- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2441 kADELERKIENvKKAALNAQNEGLELEKKLDELIGTV-NSAENELELAAPIAAESLKLADELKRAEELFQKLIENEGDVS 2519
Cdd:COG4717 238 -AAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLIlTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2520 LIRAKVAEELkkkpdAELKKKLELLYQKWPKALGAARDRKDLVSKAGDLVKQFgdqvqaleqRLQGDQAELDELLASDKA 2599
Cdd:COG4717 316 LEEEELEELL-----AALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL---------QLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2600 HDPE----VCDALKLVELTMARRLADVDALNAVMNRIESSAPGPDANRLRRRADTLSDDAKGMAKKARtaaDLAQRKQGL 2675
Cdd:COG4717 382 EDEEelraALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELE---ELREELAEL 458
|
410 420 430
....*....|....*....|....*....|...
gi 1143463340 2676 AKKFERLC-----DEVSQFTENQKAEIQDAIEK 2703
Cdd:COG4717 459 EAELEQLEedgelAELLQELEELKAELRELAEE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3434-4001 |
4.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3434 RAVLDDLQYLIEWFSAARERILEGAPPSLdLEVLKSQLKHQRITNEEASANKVQFRNVAGEAKKV------ARQ----LG 3503
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEEKDLHER-LNGLESELAELDEEIERYEEQREQARETRDEADEVleeheeRREeletLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3504 MEGNEANEKISDTVDEGKELVEEVmalcADRTETLERalaLMEQLTSQFDELNkwLDQMDAElqaspsvttaTPAAELRE 3583
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEV----RDLRERLEE---LEEERDDLLAEAG--LDDADAE----------AVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3584 MHDHNEELARMVAAYRPIIEGFKSDVGSLHEVLA--EDQAPLLESVAGELVQGYEEVREAVRARGHAIDNM--------- 3652
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADdlEERAEELREEAAELESELEEAREAVEDRREEIEELeeeieelre 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3653 --MGATIGFGErLETLVANLQGAADRLRENEG-ISADPSVLESRLAENR------------------SIVESLRDKqnay 3711
Cdd:PRK02224 399 rfGDAPVDLGN-AEDFLEELREERDELREREAeLEATLRTARERVEEAEalleagkcpecgqpvegsPHVETIEED---- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3712 dalKQTASELLASAPEGDAAAGDVENKLNRLEKLwKEIEREavdrgvlLEDVLDKAKHFWSELDSCQKAVDDLRNRLE-L 3790
Cdd:PRK02224 474 ---RERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDR-------IERLEERREDLEELIAERRETIEEKRERAEeL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3791 VEPATGHPEQLADQQEIMAQVASEMERARPRIEALsiagkqladyvpDDEKAVIENQVANVrggfstitglfaEKKRDLI 3870
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL------------NSKLAELKERIESL------------ERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3871 AAMEEAMTFHGDLQELLK-WLDMAEQKLlkmspvEHAKHMTEIEQLLKElhTFKDEVHERGVAKEQVVATALQLAADAPP 3949
Cdd:PRK02224 599 AAIADAEDEIERLREKREaLAELNDERR------ERLAEKRERKRELEA--EFDEARIEEAREDKERAEEYLEQVEEKLD 670
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 3950 HLAA----------TVRQPVADLNTRWSRLnAALAEREHKLENLMLQMGKLASTIAQLTAWM 4001
Cdd:PRK02224 671 ELREerddlqaeigAVENELEELEELRERR-EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2665-2841 |
5.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2665 AADLAQRKQglaKKFERLCDEVSQFtENQKAEIQDAIEKDLLNAERVQSKLNKIDDFWSSNSRELKNVGDEIK------- 2737
Cdd:PHA02562 211 NGENIARKQ---NKYDELVEEAKTI-KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggv 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2738 -------IDATPEDAQAVDTKLAELQAGIDgllatlqeqnvHLEEKREQANRVQSESQKAAGKINSLVAEIADLD-PIGR 2809
Cdd:PHA02562 287 cptctqqISEGPDRITKIKDKLKELQHSLE-----------KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqSLIT 355
|
170 180 190
....*....|....*....|....*....|..
gi 1143463340 2810 SRDELQKQKKEVVELAGDLGSAQTKMLELGAE 2841
Cdd:PHA02562 356 LVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2118-2402 |
5.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2118 ARLQRQASELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQLSTGfpvpATKEGVKSQLLDLERMNKTGKEEQRRVD 2197
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE----REIAELEAELERLDASSDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2198 DARHSARELareasvEKEVQDMNQREKKLLDEWEDLADQFDAVRSRANKAEQvlNECAQMEKYIGAkknMLEGIGAPSTE 2277
Cdd:COG4913 696 ELEAELEEL------EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED--LARLELRALLEE---RFAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2278 PGVAKANRAQIQSMKAETEGEKSALEhvnslaneliadgganveelmKKMDRLNRKWHSLESGLDENAGRVEEAAKLGQE 2357
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELE---------------------RAMRAFNREWPAETADLDADLESLPEYLALLDR 823
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2358 LKDIQ--------KELRKE-----LGELESNVEKAsamsSNDIGDQLATL-DSLK-SRFG 2402
Cdd:COG4913 824 LEEDGlpeyeerfKELLNEnsiefVADLLSKLRRA----IREIKERIDPLnDSLKrIPFG 879
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2417-2599 |
7.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2417 ATEELEVDATNRAEIQEQLETTQKKADELERKIENVKKAALNAQNEGLELEKKLDELIGTVNSAENELELAAPIAAESLK 2496
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2497 --------------------LADELKRAeELFQKLIENEGDVsLIRAKVAEELKKKPDAELKKKLELLYQKWPKALGAAR 2556
Cdd:COG3883 94 alyrsggsvsyldvllgsesFSDFLDRL-SALSKIADADADL-LEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1143463340 2557 DRKDLVSKAGDLVKQFGDQVQALEQRLQGDQAELDELLASDKA 2599
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1868-2085 |
7.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1868 ELDLHEARKDEQVLHGE---IENRLALIEELEKKAADVGDHAS----LAELQECKMKLKRSNSDLKGLRDNIFDAINGLQ 1940
Cdd:COG4913 623 EEELAEAEERLEALEAEldaLQERREALQRLAEYSWDEIDVASaereIAELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1941 TVNSEGETLSRAVDSAGAKIRsarlpEAQSEVEALQDQADNLERITNNLCN------IPNVTRTEPVIQKSKDLRKRVDS 2014
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAAEDLARLELRalleerFAAALGDAVERELRENLEERIDA 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1143463340 2015 CAQELDARMGKLAEL-ESLDAEFDGAKNKLSSFIGAFDDELKGLEKvsIDKEKLAEQRRQTQDLVDKHSEGN 2085
Cdd:COG4913 778 LRARLNRAEEELERAmRAFNREWPAETADLDADLESLPEYLALLDR--LEEDGLPEYEERFKELLNENSIEF 847
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1717-2226 |
9.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1717 QNRLHAMNDEHSEQARRADEwlQMLQNDVEDVDQD--PRFQRDEDRIQRIEELNRMAAGGSSQLDDAEQASRRLLTALEG 1794
Cdd:COG1196 271 ELRLELEELELELEEAQAEE--YELLAELARLEQDiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1795 -----TNVANDVRARHEELANLRRGKHQKVIDRLSQNMMEAASRKAEAEGVKQAVENLRQWSEQTAQRTRQPVQlpLTEL 1869
Cdd:COG1196 349 aeeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE--LEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1870 DLHEARKDEQVLHGEIENRLALIEELEKKAADVGDHASLAELQECKMKLKRSNSDLKGLRDNIFDAINGLQTVNSEGETL 1949
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 1950 SRAVDSAGAKIRSARLPEAQSEVEALQDQADN-LERITNNLCNIPNVTRTEPVIQKSKDLRKRVDSCAQELDARMGKLAE 2028
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaLEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2029 LESlDAEFDGAKNKLSSFIGAFDDELKGLEKVSIDKEKLAEQRRQTQDLVDKHSEGNAILDDVEAIAQKVTAEDPSKTGS 2108
Cdd:COG1196 587 ALA-AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 2109 AQKSVGELGARLQRQASELKARGDKINKLDSKATSFAESEAAVLGYIEKQKDQLstgfpvpATKEGVKSQLLDLERMNKT 2188
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE-------ELEEEALEEQLEAEREELL 738
|
490 500 510
....*....|....*....|....*....|....*...
gi 1143463340 2189 GKEEQRRVDDARHSARELAREASVEKEVQDMNQREKKL 2226
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
948-993 |
9.81e-03 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 9.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1143463340 948 KVTALCDY---SDENVTIKAGDDVYLLDNSDLIKWTIRDISGAEGQVPS 993
Cdd:cd11768 1 IVVALYDFqpiEPGDLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
3518-3826 |
9.86e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3518 DEGKELVEEV--------MALCADRTETLERALAL-------MEQLTSQFDELNKWLDQMDAELQASPSVTTATPAAElr 3582
Cdd:COG3096 256 DLFKHLITEAtnyvaadyMRHANERRELSERALELrrelfgaRRQLAEEQYRLVEMARELEELSARESDLEQDYQAAS-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3583 emhDHneeLARMVAAYR--PIIEGFKSDVGSLHEVLAEDQAPLLEsvAGELVQGYEE----------------------- 3637
Cdd:COG3096 334 ---DH---LNLVQTALRqqEKIERYQEDLEELTERLEEQEEVVEE--AAEQLAEAEArleaaeeevdslksqladyqqal 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3638 ---------VREAVRARGHA----------IDNmmgatigFGERLETLVANLQGAADRLRENEGISADPSVLESRLAENR 3698
Cdd:COG3096 406 dvqqtraiqYQQAVQALEKAralcglpdltPEN-------AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1143463340 3699 SIVESLRDKQNAYDALkQTASELLASAPEGDAAAGDVEN---KLNRLEKLwkEIEREAVDRgvLLEDVldkAKHFWSELD 3775
Cdd:COG3096 479 ELVCKIAGEVERSQAW-QTARELLRRYRSQQALAQRLQQlraQLAELEQR--LRQQQNAER--LLEEF---CQRIGQQLD 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1143463340 3776 ScQKAVDDLRNRLElvEPATGHPEQLADQQEIMAQVASEMERARPRIEALS 3826
Cdd:COG3096 551 A-AEELEELLAELE--AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| |
