|
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 ... |
178-282 |
1.02e-70 |
|
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: 233.44 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
8408-8475 |
1.19e-38 |
|
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: 140.42 E-value: 1.19e-38
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 8408 IQDEVRRQVCKCTCIKQFRIHKIGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLVKNDPCR 8475
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCR 68
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
8406-8475 |
7.45e-36 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 132.57 E-value: 7.45e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8406 ELIQDEVRRQVCKCTCIKQFRIHKIGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLVKNDPCR 8475
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7699-7909 |
4.02e-32 |
|
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: 127.56 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7699 FHGELNKFISWLTDTEKTLNNLQPVSRLVErVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyFSQKQDVVLIKNLLS 7778
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7779 SIQHRWEKIVSRSAERTRHLERGYKEAKQFNDTWkDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQP 7858
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 7859 VYDGVNKAGRLLKERCPSDDVPTIQAMLTELKSHWNNVCSKSVDRQRKLEE 7909
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7916-8126 |
3.42e-28 |
|
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: 116.01 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7916 QFTEALDALLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 7995
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7996 ELNAAWDRVCKLSVSKQDRLEHAQRLAEEFHkKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEA 8075
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 8076 NLRETLNIGQDIMKRCHPDSVPIMKQWLSVIRARWEELTALGRQRSARLSN 8126
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
178-282 |
1.47e-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: 104.68 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGY-PGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSN--SNKQNLELAFTVAEKEFGVTR- 253
Cdd:pfam00307 2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKv 81
|
90 100
....*....|....*....|....*....
gi 1397727998 254 LLDPEDVDvpNPDEKSILTYVSSLYDVFP 282
Cdd:pfam00307 82 LIEPEDLV--EGDNKSVLTYLASLFRRFQ 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7480-7692 |
2.52e-25 |
|
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: 107.92 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7480 QFDHAHKELKNWMDLVDVTLDEITPVyGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMtSEGIAQAQGLKTKM 7559
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7560 EDMEKTWENIQAKSRAKQDMLEDGLREAQgFTGELQDILAKINDIEGQLIiSKPVGGLPETAKEQLEKFMDVYAELEKLE 7639
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1397727998 7640 PQVQSLNVMGEKLGGKSKGPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDA 7692
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7039-7257 |
4.62e-25 |
|
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: 107.15 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7039 ARHFHEAHTELVVWLDDVEPVLSELDVLSvDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMcGSKGAEQVQS 7118
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7119 MLDDDNRRMDNVRTKVRDRSNSIDQAMQQsAEFTDKLENMLDTLTvTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEM 7198
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727998 7199 RHNALESVKNAAEELLRqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETL 7257
Cdd:cd00176 158 HEPRLKSLNELAEELLE---EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6610-6823 |
2.17e-24 |
|
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: 105.22 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 KFQDAMASLLDWLAETEELVAMQKAPSPEQrVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITgLDPAERKHIESEL 6689
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6690 QQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDpLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHE 6769
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 6770 PAMKQLATAGKKLQDYCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAL 6823
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
174-324 |
1.97e-23 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 110.03 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 174 QEDISAREALLLWSRRTTEGY-PGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFR--QARSNSNKQNLELAFTVAEKEFG 250
Cdd:COG5069 121 EGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNvlDLQKKNKALNNFQAFENANKVIG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 251 VTRLLDPEDV-DVPNPDEKSILTYVSSLYDVFPQVPSVEQSLRDNERQLKVEEYRDLA-----SSLLRWLSDVTVFMQNR 324
Cdd:COG5069 201 IARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGLLEKIDIALHRVYRLLEADETLIQLrlpyeIILLRLLNLIHLKQANW 280
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6063-6277 |
2.75e-22 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 99.06 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6063 QAEKFEADCKELLTWISEAANNLQESEPlSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPttEVRAI 6142
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP--DAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6143 ADKVGELQGEWTRLQQEVTVQDSRLTMAgSHAQQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEM 6222
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 6223 MKKSHDRERLNSEGTSLVE-CVDSGKEAIKQQVAVINERWDAVNKALSERASHLED 6277
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEeGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5736-5947 |
5.92e-21 |
|
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: 95.21 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5736 FMQDMQDILQWLDLKDHETDSAQPlPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQQQL 5815
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5816 QELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEqQLTLWLAQKDRMLDVLGPVAMEPNmLASQMEQVKVLREELSAQE 5895
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5896 PTYDHFLNCAHGILERCGDKSQDGIAvsRRLDTVSKAWNKLQSRLNERSKNL 5947
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIE--EKLEELNERWEELLELAEERQKKL 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6498-6712 |
1.41e-20 |
|
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: 94.05 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6498 QHLTQALNLVWGDIDKASSTLDAMGPaGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQALIKTAVAGSNTtgLE 6577
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEEGHPDAEE--IQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6578 TDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMaSLLDWLAETEELVAMQKAPSPEQRVvRAQLQEQKLVQKMVT 6657
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 6658 DRTPSMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEE 6712
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
181-277 |
5.04e-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: 88.53 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 181 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSN----KQNLELAFTVAEKEFGVTRLLD 256
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSL 277
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7260-7475 |
7.34e-20 |
|
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: 92.12 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7260 AEKFWDELHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMvGTTEQPEVQK 7339
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7340 NVDDAGASLAAISDQYSKRSQELESALAQAVHFQDqLMKLLVWLQEAEDEFSEFEPVASEfETIKKQWDELKNFKTRVEP 7419
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDL-ESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7420 KNVEIESLNQHVTELTKSSTPEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMAL 7475
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
820-884 |
6.16e-19 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 84.24 E-value: 6.16e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 820 PLSLRAQPVRSPLRLRTLCSCHLPEVNLQRGEECFLISNSQLVKWRIKTLKGIETECPSVCLLIP 884
Cdd:pfam17902 1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
646-812 |
4.00e-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: 87.12 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 646 LSEFLQGATAELTWLAEREEVEVTRDWVSKDLNLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVLM 725
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 726 ASLQARWSWLLQLVTCLDAHLKHTIAHNQFFEEARHCEQWMARHTELLQNRFARDNIpmEQAELLIRELQELQEQLREYE 805
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHE 159
|
....*..
gi 1397727998 806 RRIASLT 812
Cdd:cd00176 160 PRLKSLN 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6420-7318 |
6.46e-17 |
|
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: 90.12 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6420 AELGSQLadmkDFLTRLGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQH 6499
Cdd:TIGR02168 196 NELERQL----KSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6500 LTQALNLVWGDIDKASSTLDAmgpaggnvttVKALQEEL---KGFVKSTMEPLQKQFESVSRQGQALIKTAV-AGSNTTG 6575
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYA----------LANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6576 LETDLESLAERWAGLVEKVAEHEKnldsallrtgKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKM 6655
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEA----------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6656 VTDRtpsMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAAN 6735
Cdd:TIGR02168 412 LEDR---RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6736 KRFTALEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQL------------ATAGKKLQDY-CKGEDVIMiqlKIDGVQ 6802
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieAALGGRLQAVvVENLNAAK---KAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6803 KQNGELRSHIedcleqMEEALPLAKHFQEAHAEFLSWASKVepelraleLGVPDEetnIEELANQLTEEMQPLLdiinse 6882
Cdd:TIGR02168 566 KQNELGRVTF------LPLDSIKGTEIQGNDREILKNIEGF--------LGVAKD---LVKFDPKLRKALSYLL------ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6883 gaelaevapgdAGLRVediinrdnkrFDNLRDQIEKRAQKVQLARqrsseVVNELGDLV--DWFVDADSRLQNQQPIA-- 6958
Cdd:TIGR02168 623 -----------GGVLV----------VDDLDNALELAKKLRPGYR-----IVTLDGDLVrpGGVITGGSAKTNSSILErr 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6959 SDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSaIRNKMDELKQWVDTVSgsaNERQSLLEQAVPF 7038
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLE---AEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7039 ARHFHEAHTELVVWLDDVEpvlSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALvamcgSKGAEQVQS 7118
Cdd:TIGR02168 753 SKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-----NEEAANLRE 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7119 MLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAepiSAQPDKLREQIEENKAMEEDLEM 7198
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7199 RHNALESVKNAAEELLrqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGR-QRALEETLAVAEKFWDELHALNSSLKDL 7277
Cdd:TIGR02168 902 ELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1397727998 7278 QEALSS---VDQPALEP-EAIREQQEELEALKEDIEASQADFEEV 7318
Cdd:TIGR02168 978 ENKIKElgpVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5229-5450 |
3.55e-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: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5229 KHRQFNDVAFKLLTWLTDMEGQLSSvkqDAGLSEPQQLQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNSLSGQAAEq 5308
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5309 qqvakLQSTMNDLSVRYSTLTKDINSHVTQLQAAVTHSQDITQAMnELVSWMDSAEQVVTTQLPISLRrPELNAQLQSFS 5388
Cdd:cd00176 77 -----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDL-ESVEELLKKHK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5389 AVDADVTNHQSALDAVKALANELVKTCELDIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEE 5450
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7807-7908 |
4.37e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 74.67 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7807 QFNDTWKDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQAML 7886
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7887 TELKSHWNNVCSKSVDRQRKLE 7908
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5347-5556 |
9.96e-15 |
|
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: 77.10 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5347 QDITQAMNELVSWMDSAEQVVTTQLPISlRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELVKTCELDiARAVEQR 5426
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5427 LTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEkLEQTNLWVHDGILQLDSKELSKL--SSDDMKQQLEKLAREKHNRL 5504
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDleSVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5505 RTIQEIQVAAEQLLQDPRTGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASD 5556
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6825-7036 |
4.17e-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: 72.48 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6825 LAKHFQEAHAEFLSWASKVEPELRALELGvpDEETNIEELANQ---LTEEMQPL---LDIINSEGAELAEVAPGDAGlRV 6898
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKheaLEAELAAHeerVEALNELGEQLIEEGHPDAE-EI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6899 EDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVvNELGDLVDWFVDADSRLQNQQPIaSDLDLLQQQLAEQKVMNEEI 6978
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6979 NNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAV 7036
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5734-5837 |
1.53e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 67.35 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5734 RTFMQDMQDILQWLDLKDhETDSAQPLPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQQ 5813
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEE 77
|
90 100
....*....|....*....|....
gi 1397727998 5814 QLQELDDKWHGLRALSEQQRKGLE 5837
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7916-8016 |
2.42e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 66.58 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7916 QFTEALDALLDWLAKVEPALADDaPVHGDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 7995
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727998 7996 ELNAAWDRVCKLSVSKQDRLE 8016
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6065-6167 |
2.42e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 66.58 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6065 EKFEADCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPttEVRAIAD 6144
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|...
gi 1397727998 6145 KVGELQGEWTRLQQEVTVQDSRL 6167
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5843-6060 |
3.55e-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: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5843 LRDMREHEQqltlWLAQKDRMLDVLGPVAmEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDgiaV 5922
Cdd:cd00176 6 LRDADELEA----WLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5923 SRRLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRgLADWLSDFSDKLDGQGKVSSQPDKQhKQLQELKQLESEL 6002
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVE-ELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6003 IVQQPRLARARDLCRQLCDKAKDASTKtDLRSKLTALEKDMNDTTRKLEICKAAVEEA 6060
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6610-6711 |
3.72e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 63.50 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 KFQDAMASLLDWLAETEELVAmQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITgLDPAERKHIESEL 6689
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 6690 QQLNSRWEALTKRVVDRTAILE 6711
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7181-7767 |
1.03e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7181 KLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrgrqraLEETLAVA 7260
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE--------LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7261 EKFWDELHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEasqaDFEEVQQTGDTLLGMVGTTEQPEVQKN 7340
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELE------ERIEELKKEIEELEEKVK----ELKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7341 VDDAGASlaaisdQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRVEPK 7420
Cdd:PRK03918 311 EIEKRLS------RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7421 nvEIESLNQHVTELTKSSTPeqasvLREPMTQLNIRWNNLLTNIGDRQR---ELQMAL----LTAGQFDHAHKElknwmD 7493
Cdd:PRK03918 385 --TPEKLEKELEELEKAKEE-----IEEEISKITARIGELKKEIKELKKaieELKKAKgkcpVCGRELTEEHRK-----E 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7494 LVDVTLDEItpvygdpKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMTSEGIA-QAQGLKTKM-----EDMEKTWE 7567
Cdd:PRK03918 453 LLEEYTAEL-------KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeQLKELEEKLkkynlEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7568 NIQ------AKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-----IIS----KPVGGLPETAKEqLEKFMDVY 7632
Cdd:PRK03918 526 EYEklkeklIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELaellkELEelgfESVEELEERLKE-LEPFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7633 AELEKLEPQVQSLNVMGEKLGGKskgpaLANLRQNLQHLNQRCDYIRSRACDRKKKLEDAE-GMATNFHGELNKFISWLT 7711
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEE-----LDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLR 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7712 DTEKTLNNlqpvsrLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKYFSQK 7767
Cdd:PRK03918 680 AELEELEK------RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7588-7690 |
4.20e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 60.42 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7588 QGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLgGKSKGPALANLRQN 7667
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727998 7668 LQHLNQRCDYIRSRACDRKKKLE 7690
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7040-7142 |
6.27e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 60.04 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7040 RHFHEAHTELVVWLDDVEPVLSELDVlSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMcGSKGAEQVQSM 7119
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727998 7120 LDDDNRRMDNVRTKVRDRSNSID 7142
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6062-6158 |
6.33e-10 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 60.02 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6062 QQAEKFEADCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPTTEvrA 6141
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE--E 77
|
90
....*....|....*..
gi 1397727998 6142 IADKVGELQGEWTRLQQ 6158
Cdd:pfam00435 78 IQERLEELNERWEQLLE 94
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7807-7909 |
8.47e-10 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 59.64 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7807 QFNDTWKDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQAML 7886
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727998 7887 TELKSHWNNVCSKSVDRQRKLEE 7909
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7130-7364 |
1.03e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7130 VRTKVRDRSNSIDQAMQQSAEFTDkLENMLDTLTVTAEQVRSAEPISAQPDK---LREQIEENKAMEEDL-----EMRHN 7201
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALrlwfaQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7202 ALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwdELHALNSSLKDLQEAL 7281
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---ELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7282 SSVD-QPALEPEAIREQQEELEALKEDIEASQAdfeevqqtgdtllgmvgtteqpEVQKNVDDAGASLAAISDQYSKRSQ 7360
Cdd:COG4913 369 AALGlPLPASAEEFAALRAEAAALLEALEEELE----------------------ALEEALAEAEAALRDLRRELRELEA 426
|
....
gi 1397727998 7361 ELES 7364
Cdd:COG4913 427 EIAS 430
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
5733-5838 |
3.27e-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: 58.10 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5733 IRTFMQDMQDILQWLDLKDHETDSaQPLPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQ 5812
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1397727998 5813 QQLQELDDKWHGLRALSEQQRKGLED 5838
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5351-5449 |
5.71e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5351 QAMNELVSWMDSAEQVVTTQlPISLRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELVKTCELDiARAVEQRLTSL 5430
Cdd:smart00150 5 RDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEEL 82
|
90
....*....|....*....
gi 1397727998 5431 DEKFSSLQAKCRQRDRDLE 5449
Cdd:smart00150 83 NERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7916-8016 |
7.06e-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: 56.94 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7916 QFTEALDALLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 7995
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|.
gi 1397727998 7996 ELNAAWDRVCKLSVSKQDRLE 8016
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLE 104
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6610-6712 |
8.02e-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: 56.94 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 KFQDAMASLLDWLAETEELVAMQKAPSPEQRVvRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAErKHIESEL 6689
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGKDLESV-QALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727998 6690 QQLNSRWEALTKRVVDRTAILEE 6712
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
648-747 |
1.84e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 55.80 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 648 EFLQGATAELTWLAEREEVeVTRDWVSKDL-NLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVLMA 726
Cdd:smart00150 2 QFLRDADELEAWLEEKEQL-LASEDLGKDLeSVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727998 727 SLQARWSWLLQLVTCLDAHLK 747
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
418-645 |
1.85e-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: 55.91 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 418 AEKIQRESKQAGESLHDLERQIQEAEVRGDKQHPYEAKHNCDAMDRALHTIEENLRAMFRDVQTLQDNHFPQSQQLYTRI 497
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 498 SELQSRVSSLRTRLysgvvqpllsrayveegrtVTRRTEIMTEVRLVDTnpaFRHVQDCLDWIEAQQQMIVGQDYSSDLQ 577
Cdd:cd00176 82 EELNQRWEELRELA-------------------EERRQRLEEALDLQQF---FRDADDLEQWLEEKEAALASEDLGKDLE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 578 QVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAEEQ----KLYTQKLSSVEVAYSLLLNTSSRRLKFLES 645
Cdd:cd00176 140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHpdadEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7209-7636 |
2.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7209 AAEELLRQAGDEQDEaVKDVRQKLEELTKLYKDIQERGRGRQRALE--ETLAVAEKFWDELHALNSSLKDLQEALssvdq 7286
Cdd:COG4717 75 ELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERL----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7287 palepEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAIsdqyskrsQELESAL 7366
Cdd:COG4717 149 -----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL--------AELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7367 AQAvhfQDQLMKllvwLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRvepknVEIESLNQHVTELTKSSTPEQASVL 7446
Cdd:COG4717 216 EEA---QEELEE----LEEELEQLENELEAAALEERLKEARLLLLIAAAL-----LALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7447 REPMTQLNIRWNNLLtnigDRQRELQMALLTAGQFDHAHKELKNWMDLVDVtLDEITPVYGDPKLVEIELAKLRIVQNDI 7526
Cdd:COG4717 284 GLLALLFLLLAREKA----SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7527 TAHQESVESISKEAQRLMTSEGIAQAQGLKTKMEDMEKtWENIQAKSRAKQDMLE--DGLREAQGFTGELQDILAKINDI 7604
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEelLGELEELLEALDEEELEEELEEL 437
|
410 420 430
....*....|....*....|....*....|..
gi 1397727998 7605 EGQLiiskpvgglpETAKEQLEKFMDVYAELE 7636
Cdd:COG4717 438 EEEL----------EELEEELEELREELAELE 459
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7585-7691 |
4.87e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 51.94 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7585 REAQGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLgGKSKGPALANL 7664
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1397727998 7665 RQNLQHLNQRCDYIRSRACDRKKKLED 7691
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
4974-5631 |
5.40e-07 |
|
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: 57.04 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 4974 PFVGRLADSFDSIVQELMTEQEhLGDLEQILKHDSQMGDEASKVK---LQLEAHKSTHEKIQSQQQPILSLVYKAEQLTE 5050
Cdd:pfam05483 48 PMLEQVANSGDCHYQEGLKDSD-FENSEGLSRLYSKLYKEAEKIKkwkVSIEAELKQKENKLQENRKIIEAQRKAIQELQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5051 NYQEELTPEQVTQLTTQASLLKatlekvSKTSERRLSHLTK-----AADELAKFEEESKKFRTwmgaAFSELTNQ-EDYL 5124
Cdd:pfam05483 127 FENEKVSLKLEEEIQENKDLIK------ENNATRHLCNLLKetcarSAEKTKKYEYEREETRQ----VYMDLNNNiEKMI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5125 KRFEDLKVlgekhrelasdisshQADHRFMSMAVQKYMEEAKLYKLEMDSFRADRARPARHSLISMECVAADNVKDKLTD 5204
Cdd:pfam05483 197 LAFEELRV---------------QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5205 LTEEYHDlsnRCNLLGDRLADLSGKHRQFNDVAFKLLTWLTDMEGQLS-SVKQDAGLSEpqQLQVHLDRLKSLSMDALSQ 5283
Cdd:pfam05483 262 LLEESRD---KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrSMSTQKALEE--DLQIATKTICQLTEEKEAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5284 kllLDEMQKrgqdltnslsGQAAEQQQVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAAVTHSQDITQAMNELVSWMDSA 5363
Cdd:pfam05483 337 ---MEELNK----------AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5364 EqvvttqlpislrrpelnAQLQSFSAVDADVTNHQSALDAVKALANELVKTCE--LDIARAVEQRLTSLDEKFSSLQAKC 5441
Cdd:pfam05483 404 E-----------------VELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQelIFLLQAREKEIHDLEIQLTAIKTSE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5442 RQRDRDLEEVDSSLRefQEKLEQTNLWVHDGILQLDSKELSKLSSD---DMKQQLEKLAREKHNRLRTIQEIQVAAEQLL 5518
Cdd:pfam05483 467 EHYLKEVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5519 QdprtgegeavknlvsdLKKNLEAFDSLLAAKENEASDKEQQGAdfENAKTIALLWLSQMEARLDEFQPVAIDVGIVEQQ 5598
Cdd:pfam05483 545 N----------------LRDELESVREEFIQKGDEVKCKLDKSE--ENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
650 660 670
....*....|....*....|....*....|...
gi 1397727998 5599 KMELQPMLQEYEDYAPKIDEVNDLGNAYEAMIN 5631
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1111-1302 |
1.10e-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: 53.60 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 1111 LDDVKQMIHDYQHTLASQDNAtSDLSSLKLAHTELTDVQTSMKQQQPRIEHLKSDVSSLRVLveksrsgvtSHHDLDAVE 1190
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---------GHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 1191 REVINLASQWATVSSQAAERLQMVRSIQDLLSMYEHGLgAEEQWLEQIQKTVASQPPlTGDVVDAKNQLQTTMAIYNRLV 1270
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|..
gi 1397727998 1271 ERKHQIEAVNRLGGQYIREAKIFEKKQTKYRQ 1302
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7371-7472 |
3.14e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7371 HFQDQLMKLLVWLQEAEdEFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSStPEQASVLREPM 7450
Cdd:smart00150 2 QFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7451 TQLNIRWNNLLTNIGDRQRELQ 7472
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
8346-8394 |
8.57e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 46.77 E-value: 8.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1397727998 8346 GRVTRKEFIEGIISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:cd00051 15 GTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
8138-8193 |
8.75e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 48.08 E-value: 8.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 8138 LEDLLAWLNNAEMTLADVDrqtIPQDMAIIQQLIKEHQDFQNEMSSRQPDVDRLTK 8193
Cdd:pfam00435 10 ADDLESWIEEKEALLSSED---YGKDLESVQALLKKHKALEAELAAHQDRVEALNE 62
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8138-8193 |
1.06e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 8138 LEDLLAWLNNAEMTLADVDrqtIPQDMAIIQQLIKEHQDFQNEMSSRQPDVDRLTK 8193
Cdd:smart00150 7 ADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNE 59
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4997-5148 |
1.79e-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: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 4997 LGDLEQILKHDsQMGDEASKVKLQLEAHKSTHEKIQSQQQPILSLVYKAEQLTENYQEEltpeqVTQLTTQASLLKATLE 5076
Cdd:cd00176 16 LSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-----AEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5077 KVSKTSERRLSHLTKAADeLAKFEEESKKFRTWMGAAFSELtNQEDYLKRFEDLKVLGEKHRELASDISSHQ 5148
Cdd:cd00176 90 ELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
5808-6236 |
2.75e-05 |
|
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: 51.65 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5808 EEML---QQQLQELDDKWHGLRALSEQQRKGLEDMvSDLRDMREHE-QQLTLWLAQKDRMLDvlgpvamepnmlasQMEQ 5883
Cdd:pfam05483 362 EELLrteQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVElEELKKILAEDEKLLD--------------EKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5884 VKVLREELSAQEPTYDHFLNCAHgilERCGDKSQDGIAVSRRLDTVSKAWNKLQSRL-NERSKNL---SSVEGISVEFAS 5959
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQARE---KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIeltAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5960 LTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELK----QLESELIVQQPRLARARDLCRQLCDKAKDasTKTDLRSK 6035
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekemNLRDELESVREEFIQKGDEVKCKLDKSEE--NARSIEYE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6036 LTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLK 6115
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6116 EPEIRQLLEkgDKLVKEsspTTEVRAIADKVGELQGEW-TRLQQEVTvqdSRLTMAGSHAQQFTERLDKMAMWLQMTEEK 6194
Cdd:pfam05483 662 EIEDKKISE--EKLLEE---VEKAKAIADEAVKLQKEIdKRCQHKIA---EMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1397727998 6195 LEKMKPEDVDQNTVVHKLK-ELQGVQNEMMKKSHDRERLNSEG 6236
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
646-739 |
3.38e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 46.54 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 646 LSEFLQGATAELTWLAEREEvEVTRDWVSKDL-NLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVL 724
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEA-LLSSEDYGKDLeSVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81
|
90
....*....|....*
gi 1397727998 725 MASLQARWSWLLQLV 739
Cdd:pfam00435 82 LEELNERWEQLLELA 96
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
550-644 |
5.09e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 46.16 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 550 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE---EQKLYTQKLSSVE 626
Cdd:pfam00435 7 FRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghyASEEIQERLEELN 86
|
90
....*....|....*...
gi 1397727998 627 VAYSLLLNTSSRRLKFLE 644
Cdd:pfam00435 87 ERWEQLLELAAERKQKLE 104
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
5986-6383 |
5.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5986 DKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDTTRKLEICKAAVEE------ 6059
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelee 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6060 ----ASQQAEKFEADCKELLTWISEAAnnLQESEPLSSDLDILREQMRQnrtLQQELSLKEPEIRQLLEKGDKLVKESSP 6135
Cdd:COG4717 164 eleeLEAELAELQEELEELLEQLSLAT--EEELQDLAEELEELQQRLAE---LEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6136 TTEVRAIADKVGELQGEWTRL---QQEVTVQDSRLTMAGshAQQFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKL 6212
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLallGLGGSLLSLILTIAG--VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6213 KElQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERwdAVNKALSERASHLEDLGQRLGEVQDSLAEA 6292
Cdd:COG4717 317 EE-EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6293 TSALNKWENKLAVHNSLgLSAKDPKHINRIKDLLEDTgwLASQLNNTETMLNSIEvdgGETSNLRDELNKLRGQHQTL-- 6370
Cdd:COG4717 394 AEEYQELKEELEELEEQ-LEELLGELEELLEALDEEE--LEEELEELEEELEELE---EELEELREELAELEAELEQLee 467
|
410
....*....|...
gi 1397727998 6371 QGELSELVAEMET 6383
Cdd:COG4717 468 DGELAELLQELEE 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5036-5520 |
5.73e-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: 50.44 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5036 QPILSLVYKAEQLTE--NYQEELTPEQ--VTQ----LTTQASLLKATLEKVSKTSERR--LSHLTKAADELAKFEEESKK 5105
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNalELAKKLRPGYriVTLdgdlVRPGGVITGGSAKTNSSILERRreIEELEEKIEELEEKIAELEK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5106 FRTWMGAAFSELTNQEDYLKRFEDlkvlgekhrELASDISSHQADHRFMSMAVQKYMEEAKLYKLEMDSFRADRArpARH 5185
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELE---------ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE--ELE 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5186 SLISMECVAADNVKDKLTDLTEEYHDLSNRCNLLGDRLADLSGKHRQFNDVAFKLLTWLTDMEGQLSSVKQDAGLSEpQQ 5265
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-EQ 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5266 LQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNslsgqaaeqqQVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAAvth 5345
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLN----------ERASLEEALALLRSELEELSEELRELESKRSEL--- 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5346 sqdiTQAMNELvswMDSAEQVVTTQLPISLRRPELNAQLQSfsavdadvtNHQSALDAVKALANELvktcELDIARAvEQ 5425
Cdd:TIGR02168 914 ----RRELEEL---REKLAQLELRLEGLEVRIDNLQERLSE---------EYSLTLEEAEALENKI----EDDEEEA-RR 972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5426 RLTSLDEKFSSLQakcrqrdrdleEVD-SSLREFQEKLEQTnlwvhdgilqldskelsklssDDMKQQLEKLAREKHNRL 5504
Cdd:TIGR02168 973 RLKRLENKIKELG-----------PVNlAAIEEYEELKERY---------------------DFLTAQKEDLTEAKETLE 1020
|
490
....*....|....*.
gi 1397727998 5505 RTIQEIQVAAEQLLQD 5520
Cdd:TIGR02168 1021 EAIEEIDREARERFKD 1036
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
8346-8394 |
9.69e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.32 E-value: 9.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1397727998 8346 GRVTRKEFIEGIISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:COG5126 48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
7128-7321 |
1.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7128 DNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLtvtaeqVRSAEPISAQPDKLREQIEEnkaMEEDLEMRHNALESVK 7207
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7208 NAA-------------EELLRQAG---------DEQDEAVKDVRQKLEELTKLYKDIQErgrgRQRALEETLAVAEKFWD 7265
Cdd:PHA02562 262 TAAakikskieqfqkvIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDT----AIDELEEIMDEFNEQSK 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727998 7266 ELHALNSSLKDLQEALSSVDQPALEPEA-IREQQEELEALKEDIEASQADFEEVQQT 7321
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAaIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
550-644 |
1.35e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 44.63 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 550 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE---EQKLYTQKLSSVE 626
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEghpDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1397727998 627 VAYSLLLNTSSRRLKFLE 644
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
7111-7392 |
1.61e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7111 KGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMldtltvTAEQVRSAEPISAQPDKLREQIEENK 7190
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK------YKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7191 A----MEEDLEM-------RHNALESVKNAAEELLRQAGDEQDEAvKDVRQKLE----ELTKLYKDIQE-RGRGRQRAle 7254
Cdd:pfam07888 129 ArireLEEDIKTltqrvleRETELERMKERAKKAGAQRKEEEAER-KQLQAKLQqteeELRSLSKEFQElRNSLAQRD-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7255 etlavaekfwDELHALNSSLKDLQEALSSVDQPALEPEAIREQ----QEELEALKEDIEASQADFEEVQQTGDTLLGMVG 7330
Cdd:pfam07888 206 ----------TQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslQERLNASERKVEGLGEELSSMAAQRDRTQAELH 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 7331 TTEQPEVQKNVDDAGASLAAISDQySKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSE 7392
Cdd:pfam07888 276 QARLQAAQLTLQLADASLALREGR-ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6525-6602 |
1.99e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 44.24 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6525 GGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQALIKTAVAGSNTtgLETDLESLAERWAGLVEKVAEHEKNLD 6602
Cdd:smart00150 27 GKDLESVEALLKKHEAF-EAELEAHEERVEALNELGEQLIEEGHPDAEE--IEERLEELNERWEELKELAEERRQKLE 101
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
7172-7412 |
3.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7172 AEPISAQPDKLREQIEENKAMEEDLEMRHNALESV------------KNAAEELLRQAGDEQDEAVKDVRQKLEELTKLY 7239
Cdd:PRK04863 788 IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafeadPEAELRQLNRRRVELERALADHESQEQQQRSQL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7240 KDIQERGRGRQRALEE-TLAVAEKFWDELHALNSSLKDLQEALSSVDQ-----PALEPEA--IREQQEELEALKEDIEAS 7311
Cdd:PRK04863 868 EQAKEGLSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKRFVQQhgnalAQLEPIVsvLQSDPEQFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7312 QADFEEVQQTGDTLLGMVgtteQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQlmkllvwLQEAEDEFS 7391
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVV----QRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ-------LRQAQAQLA 1016
|
250 260
....*....|....*....|....*
gi 1397727998 7392 EFEPV----ASEFETIKKQWDELKN 7412
Cdd:PRK04863 1017 QYNQVlaslKSSYDAKRQMLQELKQ 1041
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
8368-8394 |
3.52e-04 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 41.21 E-value: 3.52e-04
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
8368-8394 |
4.57e-04 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 40.85 E-value: 4.57e-04
10 20
....*....|....*....|....*..
gi 1397727998 8368 EMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLK 27
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6932-7033 |
1.49e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6932 EVVNELGDLVDWFVDADSRLQnQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAmEDNSAIRNKM 7011
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7012 DELKQWVDTVSGSANERQSLLE 7033
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
5930-6171 |
2.46e-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: 44.75 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5930 SKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQ-ELKQLESELIVQQPR 6008
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6009 LARARDLCRQLCDKAKDASTKTDLRSKLTAleKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQEs 6088
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6089 eplssdldiLREQMRQNRTLQQELSLKEPEIRQLLEKGDKlvKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLT 6168
Cdd:COG4942 176 ---------LEALLAELEEERAALEALKAERQKLLARLEK--ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 1397727998 6169 MAG 6171
Cdd:COG4942 245 AAG 247
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2215-2244 |
2.91e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|
gi 1397727998 2215 SITGIVHPKSGARLTVSQAIQNGILDQEKG 2244
Cdd:smart00250 9 AIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4599-4623 |
2.94e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 2.94e-03
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6683-7019 |
3.43e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6683 KHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDplttwldaANKRFTALEPHSPDAEgiEHLIQELKKLQ 6762
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD--------EKKQFEKIAEELKGKE--QELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6763 KEVNEHEpamKQLATAGKKLQDYCKgeDVIMIQLKIDGVQKQNGELRSHIEDCL----EQMEEALPLAKHFQEAHAEFLS 6838
Cdd:pfam05483 450 KEIHDLE---IQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNIELTAHCDKLLlenkELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6839 WASKVEPELRALElGVPDEETNIEELANQLTEEMQPLLDIINS--EGAELAEVAPGDAGLRVEDIINRDNKRFDNLRDQI 6916
Cdd:pfam05483 525 CKKQEERMLKQIE-NLEEKEMNLRDELESVREEFIQKGDEVKCklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6917 EKRAQKVQLARQRSSEVVNElgdlvdwfVDADSRLQNQQPIASDLDLLQQQLAEQKvMNEEINNQKVKARDTLSASKKLL 6996
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLELELASAKQK-FEEIIDNYQKEIEDKKISEEKLL 674
|
330 340
....*....|....*....|...
gi 1397727998 6997 SDsaMEDNSAIRNKMDELKQWVD 7019
Cdd:pfam05483 675 EE--VEKAKAIADEAVKLQKEID 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5337-5581 |
9.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5337 TQLQAAVTHSQDITQAMNELVswmDSAEQVVTtqlpisLRRpeLNAQLQSFSAVDADVTNHQSALDAVKALANELvktce 5416
Cdd:COG4913 225 EAADALVEHFDDLERAHEALE---DAREQIEL------LEP--IRELAERYAAARERLAELEYLRAALRLWFAQR----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5417 ldIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEKleqtnlwvhdgILQLDSKELSKLssddmKQQLEKL 5496
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQL-----EREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5497 AREKHNRLRTIQEIQVAAEQL-LQDPrtGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWL 5575
Cdd:COG4913 351 ERELEERERRRARLEALLAALgLPLP--ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
....*.
gi 1397727998 5576 SQMEAR 5581
Cdd:COG4913 429 ASLERR 434
|
|
| |
|
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 ... |
178-282 |
1.02e-70 |
|
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: 233.44 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
178-281 |
9.90e-48 |
|
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: 167.97 E-value: 9.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|....
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
178-282 |
4.10e-47 |
|
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: 166.32 E-value: 4.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 257
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
178-282 |
9.73e-46 |
|
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: 162.49 E-value: 9.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21243 5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21243 85 EDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
178-281 |
2.40e-45 |
|
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: 161.02 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|....
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
177-282 |
5.46e-45 |
|
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: 160.19 E-value: 5.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 177 ISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
176-282 |
1.34e-44 |
|
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: 159.05 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 176 DISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLL 255
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1397727998 256 DPEDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
166-281 |
7.79e-44 |
|
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: 157.14 E-value: 7.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 166 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 245
Cdd:cd21216 1 IQDISV---EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVA 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727998 246 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21216 78 EKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
178-281 |
9.79e-42 |
|
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: 150.78 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
|
90 100
....*....|....*....|....
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21249 84 EDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
174-284 |
2.27e-41 |
|
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: 150.16 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 174 QEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTR 253
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1397727998 254 LLDPEDVDVPNPDEKSILTYVSSLYDVFPQV 284
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKM 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
178-282 |
8.56e-40 |
|
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: 145.26 E-value: 8.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21192 3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEV 82
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21192 83 EDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
8408-8475 |
1.19e-38 |
|
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: 140.42 E-value: 1.19e-38
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 8408 IQDEVRRQVCKCTCIKQFRIHKIGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLVKNDPCR 8475
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCR 68
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
177-275 |
1.26e-38 |
|
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: 141.90 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 177 ISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1397727998 257 PEDVDVPNPDEKSILTYVS 275
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
174-287 |
3.49e-38 |
|
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: 141.35 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 174 QEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTR 253
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|....
gi 1397727998 254 LLDPEDVDVPNPDEKSILTYVSSLYDVFPQVPSV 287
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKAL 114
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
183-282 |
1.58e-37 |
|
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: 138.72 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 183 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDV 262
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84
|
90 100
....*....|....*....|
gi 1397727998 263 PNPDEKSILTYVSSLYDVFP 282
Cdd:cd21187 85 EQPDKKSILMYVTSLFQVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
178-281 |
5.08e-37 |
|
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: 137.48 E-value: 5.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21253 1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
|
90 100
....*....|....*....|....*
gi 1397727998 258 ED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21253 81 EDmVALKVPDKLSILTYVSQYYNYF 105
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
174-287 |
5.76e-36 |
|
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: 135.18 E-value: 5.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 174 QEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQ-ARSNSNkQNLELAFTVAEKEFGVT 252
Cdd:cd21322 13 RETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKlTKSNAT-YNLQQAFNTAEQHLGLT 91
|
90 100 110
....*....|....*....|....*....|....*
gi 1397727998 253 RLLDPEDVDVPNPDEKSILTYVSSLYDVFPQVPSV 287
Cdd:cd21322 92 KLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKAL 126
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
166-281 |
5.90e-36 |
|
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: 134.58 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 166 ISDVvvpGQEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 245
Cdd:cd21291 1 IADI---NEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIA 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727998 246 EKEFGVTRLLDPEDV-DVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21291 78 SKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
8406-8475 |
7.45e-36 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 132.57 E-value: 7.45e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8406 ELIQDEVRRQVCKCTCIKQFRIHKIGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLVKNDPCR 8475
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
178-284 |
2.16e-34 |
|
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: 129.83 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|....*..
gi 1397727998 258 EDVDVPNPDEKSILTYVSSLYDVFPQV 284
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
181-281 |
2.11e-33 |
|
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: 127.02 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 181 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPED- 259
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|..
gi 1397727998 260 VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
179-281 |
7.97e-33 |
|
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: 125.34 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 179 AREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPE 258
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 1397727998 259 D-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21197 81 DmVTMHVPDRLSIITYVSQYYNHF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7699-7909 |
4.02e-32 |
|
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: 127.56 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7699 FHGELNKFISWLTDTEKTLNNLQPVSRLVErVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyFSQKQDVVLIKNLLS 7778
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7779 SIQHRWEKIVSRSAERTRHLERGYKEAKQFNDTWkDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQP 7858
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 7859 VYDGVNKAGRLLKERCPSDDVPTIQAMLTELKSHWNNVCSKSVDRQRKLEE 7909
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
179-281 |
5.12e-31 |
|
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: 120.36 E-value: 5.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 179 AREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPE 258
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|....
gi 1397727998 259 D-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
178-281 |
1.87e-30 |
|
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: 118.68 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 257
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPN-PDEKSILTYVSSLYDVF 281
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIRAHF 104
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
179-282 |
2.38e-30 |
|
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: 118.35 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 179 AREALLLWSRRTTEGYpGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPE 258
Cdd:cd21245 4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 1397727998 259 DVDVPNPDEKSILTYVSSLYDVFP 282
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
181-281 |
1.32e-29 |
|
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: 116.03 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 181 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDV 260
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1397727998 261 DVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
183-288 |
5.28e-29 |
|
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: 114.64 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 183 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNK-QNLELAFTVAEKEFGVTRLLDPEDVD 261
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPEDVA 84
|
90 100
....*....|....*....|....*..
gi 1397727998 262 VPNPDEKSILTYVSSLYDVFPQVPSVE 288
Cdd:cd21233 85 TAHPDKKSILMYVTSLFQVLPQQVSIE 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7916-8126 |
3.42e-28 |
|
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: 116.01 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7916 QFTEALDALLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 7995
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7996 ELNAAWDRVCKLSVSKQDRLEHAQRLAEEFHkKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEA 8075
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 8076 NLRETLNIGQDIMKRCHPDSVPIMKQWLSVIRARWEELTALGRQRSARLSN 8126
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7804-8018 |
3.80e-28 |
|
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: 116.01 E-value: 3.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7804 EAKQFNDTWKDLITWLIEAEKTLeTETSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQ 7883
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7884 AMLTELKSHWNNVCSKSVDRQRKLEEGLLLSGQFTEALDaLLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELG 7963
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7964 ARTTTIAFLQKSAKEIISRAEGDVC-SLQSDLIELNAAWDRVCKLSVSKQDRLEHA 8018
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
166-290 |
4.04e-28 |
|
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: 112.51 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 166 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 245
Cdd:cd21289 1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727998 246 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVFPQVPSVEQS 290
Cdd:cd21289 78 EKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAFAGAEQAETA 123
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
166-281 |
1.34e-27 |
|
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: 111.33 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 166 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 245
Cdd:cd21287 1 IQDISV---EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVA 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727998 246 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21287 78 EKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
183-282 |
5.62e-27 |
|
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: 108.51 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 183 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDV 262
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
|
90 100
....*....|....*....|
gi 1397727998 263 PNPDEKSILTYVSSLYDVFP 282
Cdd:cd21234 85 QLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
166-281 |
9.08e-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: 109.02 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 166 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 245
Cdd:cd21290 4 IQDISV---EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727998 246 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21290 81 EKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
166-290 |
1.39e-26 |
|
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: 108.24 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 166 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 245
Cdd:cd21288 1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727998 246 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVFPQVPSVEQS 290
Cdd:cd21288 78 EKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAFAGAEQAETA 123
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
178-278 |
1.85e-26 |
|
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: 107.04 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1397727998 258 EDVDV--PNPDEKSILTYVSSLY 278
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
178-282 |
1.47e-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: 104.68 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGY-PGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSN--SNKQNLELAFTVAEKEFGVTR- 253
Cdd:pfam00307 2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKv 81
|
90 100
....*....|....*....|....*....
gi 1397727998 254 LLDPEDVDvpNPDEKSILTYVSSLYDVFP 282
Cdd:pfam00307 82 LIEPEDLV--EGDNKSVLTYLASLFRRFQ 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7480-7692 |
2.52e-25 |
|
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: 107.92 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7480 QFDHAHKELKNWMDLVDVTLDEITPVyGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMtSEGIAQAQGLKTKM 7559
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7560 EDMEKTWENIQAKSRAKQDMLEDGLREAQgFTGELQDILAKINDIEGQLIiSKPVGGLPETAKEQLEKFMDVYAELEKLE 7639
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1397727998 7640 PQVQSLNVMGEKLGGKSKGPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDA 7692
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7039-7257 |
4.62e-25 |
|
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: 107.15 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7039 ARHFHEAHTELVVWLDDVEPVLSELDVLSvDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMcGSKGAEQVQS 7118
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7119 MLDDDNRRMDNVRTKVRDRSNSIDQAMQQsAEFTDKLENMLDTLTvTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEM 7198
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727998 7199 RHNALESVKNAAEELLRqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETL 7257
Cdd:cd00176 158 HEPRLKSLNELAEELLE---EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
178-281 |
7.08e-25 |
|
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: 102.82 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 257
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTI 86
|
90 100
....*....|....*....|....*
gi 1397727998 258 ED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21199 87 DEmVSMERPDWQSVMSYVTAIYKHF 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6610-6823 |
2.17e-24 |
|
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: 105.22 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 KFQDAMASLLDWLAETEELVAMQKAPSPEQrVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITgLDPAERKHIESEL 6689
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6690 QQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDpLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHE 6769
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 6770 PAMKQLATAGKKLQDYCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAL 6823
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
175-281 |
3.55e-24 |
|
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: 100.79 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 175 EDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRL 254
Cdd:cd21251 2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81
|
90 100
....*....|....*....|....*...
gi 1397727998 255 LDPEDV-DVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21251 82 MTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7586-7799 |
3.82e-24 |
|
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: 104.45 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7586 EAQGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLGgKSKGPALANLR 7665
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7666 QNLQHLNQRCDYIRSRACDRKKKLEDAEGMATNFHgELNKFISWLTDTEKTLNNlQPVSRLVERVTSQIEDHRDLQKDIS 7745
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 7746 KHREAMVALEKMGTHLKYFSQKQDVVLIKNLLSSIQHRWEKIVSRSAERTRHLE 7799
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
178-281 |
3.97e-24 |
|
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: 100.63 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEkEFGVTRLLDP 257
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|....*
gi 1397727998 258 ED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQLRAHF 104
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
183-281 |
9.57e-24 |
|
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: 99.73 E-value: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 183 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLD-PEDVD 261
Cdd:cd21195 9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMAS 88
|
90 100
....*....|....*....|
gi 1397727998 262 VPNPDEKSILTYVSSLYDVF 281
Cdd:cd21195 89 AQEPDKLSMVMYLSKFYELF 108
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
174-324 |
1.97e-23 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 110.03 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 174 QEDISAREALLLWSRRTTEGY-PGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFR--QARSNSNKQNLELAFTVAEKEFG 250
Cdd:COG5069 121 EGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNvlDLQKKNKALNNFQAFENANKVIG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 251 VTRLLDPEDV-DVPNPDEKSILTYVSSLYDVFPQVPSVEQSLRDNERQLKVEEYRDLA-----SSLLRWLSDVTVFMQNR 324
Cdd:COG5069 201 IARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGLLEKIDIALHRVYRLLEADETLIQLrlpyeIILLRLLNLIHLKQANW 280
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6063-6277 |
2.75e-22 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 99.06 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6063 QAEKFEADCKELLTWISEAANNLQESEPlSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPttEVRAI 6142
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP--DAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6143 ADKVGELQGEWTRLQQEVTVQDSRLTMAgSHAQQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEM 6222
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 6223 MKKSHDRERLNSEGTSLVE-CVDSGKEAIKQQVAVINERWDAVNKALSERASHLED 6277
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEeGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
178-283 |
2.92e-22 |
|
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: 95.44 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|....*..
gi 1397727998 258 ED-VDVPNPDEKSILTYVSSLYDVFPQ 283
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEFYRCLVQ 107
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8021-8210 |
1.38e-21 |
|
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: 97.13 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8021 LAEEFHKKAQQLLSWLADAERQLHYRGPIPDEEpLILQQMEEHKKFEESLLRQEANLRETLNIGQDIMKRCHPDSVPImK 8100
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8101 QWLSVIRARWEELTALGRQRSARLSNGLTDLRHNNvLLEDLLAWLNNAEmtlADVDRQTIPQDMAIIQQLIKEHQDFQNE 8180
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKE---AALASEDLGKDLESVEELLKKHKELEEE 154
|
170 180 190
....*....|....*....|....*....|
gi 1397727998 8181 MSSRQPDVDRLTKADKRRPSSVTQDSLSHI 8210
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEI 184
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
178-279 |
1.53e-21 |
|
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: 93.11 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
|
90 100
....*....|....*....|....
gi 1397727998 258 EDVDV--PNPDEKSILTYVSSLYD 279
Cdd:cd21261 81 EDMMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
183-281 |
2.71e-21 |
|
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: 92.64 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 183 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDV 262
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAS 88
|
90 100
....*....|....*....|
gi 1397727998 263 PN-PDEKSILTYVSSLYDVF 281
Cdd:cd21250 89 AEePDKLSMVMYLSKFYELF 108
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
178-276 |
3.21e-21 |
|
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: 91.91 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21184 1 SGKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1397727998 257 PEDVDVPNPDEKSILTYVSS 276
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5736-5947 |
5.92e-21 |
|
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: 95.21 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5736 FMQDMQDILQWLDLKDHETDSAQPlPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQQQL 5815
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5816 QELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEqQLTLWLAQKDRMLDVLGPVAMEPNmLASQMEQVKVLREELSAQE 5895
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5896 PTYDHFLNCAHGILERCGDKSQDGIAvsRRLDTVSKAWNKLQSRLNERSKNL 5947
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIE--EKLEELNERWEELLELAEERQKKL 209
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
178-281 |
6.07e-21 |
|
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: 91.45 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 257
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|....*
gi 1397727998 258 EDVDVPN-PDEKSILTYVSSLYDVF 281
Cdd:cd21254 80 SDMVLLAvPDKLTVMTYLYQIRAHF 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
178-279 |
1.05e-20 |
|
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: 90.88 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
|
90 100
....*....|....*....|....
gi 1397727998 258 EDVDV--PNPDEKSILTYVSSLYD 279
Cdd:cd21258 81 EDMMImgKKPDSKCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6498-6712 |
1.41e-20 |
|
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: 94.05 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6498 QHLTQALNLVWGDIDKASSTLDAMGPaGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQALIKTAVAGSNTtgLE 6577
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEEGHPDAEE--IQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6578 TDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMaSLLDWLAETEELVAMQKAPSPEQRVvRAQLQEQKLVQKMVT 6657
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 6658 DRTPSMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEE 6712
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
181-277 |
5.04e-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: 88.53 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 181 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSN----KQNLELAFTVAEKEFGVTRLLD 256
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSL 277
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
178-281 |
5.87e-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: 88.93 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEkEFGVTRLLDP 257
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|....*
gi 1397727998 258 ED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIYKYF 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6932-7145 |
6.06e-20 |
|
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: 92.12 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6932 EVVNELGDLVDWFVDADSRLQNQQPIaSDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAmEDNSAIRNKM 7011
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7012 DELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHtELVVWLDDVEPVLSELDVLSvDADQVKKQQEKAKVLKQEVADRK 7091
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 7092 PIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAM 7145
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7260-7475 |
7.34e-20 |
|
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: 92.12 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7260 AEKFWDELHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMvGTTEQPEVQK 7339
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7340 NVDDAGASLAAISDQYSKRSQELESALAQAVHFQDqLMKLLVWLQEAEDEFSEFEPVASEfETIKKQWDELKNFKTRVEP 7419
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDL-ESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7420 KNVEIESLNQHVTELTKSSTPEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMAL 7475
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7368-7582 |
7.63e-20 |
|
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: 92.12 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7368 QAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEfETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSStPEQASVLR 7447
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7448 EPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHkELKNWMDLVDVTLDEiTPVYGDPKLVEIELAKLRIVQNDIT 7527
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 7528 AHQESVESISKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQAKSRAKQDMLED 7582
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
180-278 |
1.22e-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: 88.22 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 180 REALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPED 259
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1397727998 260 -VDVPNPDEKSILTYVSSLY 278
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
178-281 |
2.27e-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: 87.44 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEkEFGVTRLLDP 257
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|....*
gi 1397727998 258 ED-VDVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIYKYF 117
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7150-7366 |
4.27e-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: 89.81 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7150 EFTDKLENMLDTLTVTAEQVRSAEPISAqPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEavkdVR 7229
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE----IQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7230 QKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDeLHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIE 7309
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727998 7310 ASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESAL 7366
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
820-884 |
6.16e-19 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 84.24 E-value: 6.16e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 820 PLSLRAQPVRSPLRLRTLCSCHLPEVNLQRGEECFLISNSQLVKWRIKTLKGIETECPSVCLLIP 884
Cdd:pfam17902 1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
646-812 |
4.00e-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: 87.12 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 646 LSEFLQGATAELTWLAEREEVEVTRDWVSKDLNLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVLM 725
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 726 ASLQARWSWLLQLVTCLDAHLKHTIAHNQFFEEARHCEQWMARHTELLQNRFARDNIpmEQAELLIRELQELQEQLREYE 805
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHE 159
|
....*..
gi 1397727998 806 RRIASLT 812
Cdd:cd00176 160 PRLKSLN 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6420-7318 |
6.46e-17 |
|
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: 90.12 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6420 AELGSQLadmkDFLTRLGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQH 6499
Cdd:TIGR02168 196 NELERQL----KSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6500 LTQALNLVWGDIDKASSTLDAmgpaggnvttVKALQEEL---KGFVKSTMEPLQKQFESVSRQGQALIKTAV-AGSNTTG 6575
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYA----------LANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6576 LETDLESLAERWAGLVEKVAEHEKnldsallrtgKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKM 6655
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEA----------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6656 VTDRtpsMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAAN 6735
Cdd:TIGR02168 412 LEDR---RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6736 KRFTALEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQL------------ATAGKKLQDY-CKGEDVIMiqlKIDGVQ 6802
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieAALGGRLQAVvVENLNAAK---KAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6803 KQNGELRSHIedcleqMEEALPLAKHFQEAHAEFLSWASKVepelraleLGVPDEetnIEELANQLTEEMQPLLdiinse 6882
Cdd:TIGR02168 566 KQNELGRVTF------LPLDSIKGTEIQGNDREILKNIEGF--------LGVAKD---LVKFDPKLRKALSYLL------ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6883 gaelaevapgdAGLRVediinrdnkrFDNLRDQIEKRAQKVQLARqrsseVVNELGDLV--DWFVDADSRLQNQQPIA-- 6958
Cdd:TIGR02168 623 -----------GGVLV----------VDDLDNALELAKKLRPGYR-----IVTLDGDLVrpGGVITGGSAKTNSSILErr 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6959 SDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSaIRNKMDELKQWVDTVSgsaNERQSLLEQAVPF 7038
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLE---AEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7039 ARHFHEAHTELVVWLDDVEpvlSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALvamcgSKGAEQVQS 7118
Cdd:TIGR02168 753 SKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-----NEEAANLRE 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7119 MLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAepiSAQPDKLREQIEENKAMEEDLEM 7198
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7199 RHNALESVKNAAEELLrqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGR-QRALEETLAVAEKFWDELHALNSSLKDL 7277
Cdd:TIGR02168 902 ELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1397727998 7278 QEALSS---VDQPALEP-EAIREQQEELEALKEDIEASQADFEEV 7318
Cdd:TIGR02168 978 ENKIKElgpVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6098-6917 |
1.08e-16 |
|
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: 89.35 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6098 LREQMRQNRTLQQELSLKEpeIRQLLEKGDKL-VKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQ 6176
Cdd:TIGR02168 215 YKELKAELRELELALLVLR--LEELREELEELqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6177 FTERLDKMAMWLQMTEEKLEKmkpedvdqntVVHKLKELQG-VQNEMMKKSHDRERLNsegtslvecvdsgkeAIKQQVA 6255
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLAN----------LERQLEELEAqLEELESKLDELAEELA---------------ELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6256 VINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNslglsakdpKHINRIKDLLEDtgwLASQ 6335
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---------NEIERLEARLER---LEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6336 LNNTETMLNSIEVD---------GGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELE 6406
Cdd:TIGR02168 416 RERLQQEIEELLKKleeaelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6407 SELGSKTPVSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQASSLC----NAGYVSDPELLKSQVEALSNqhaSLTER 6482
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALggrlQAVVVENLNAAKKAIAFLKQ---NELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6483 ATQRQSDVVANQHSIQHLTQALNLVWG------DIDKASSTLD-AMGPAGGNVTTVKALQE--ELKGFVKSTMEPLQKQF 6553
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRkALSYLLGGVLVVDDLDNalELAKKLRPGYRIVTLDG 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6554 ESVSRQGQALIKTAVAGSNTTGLETDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETE-ELVAMQ 6632
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6633 KAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAE--RKHIESELQQLNSRWEALTKRVVDRTAIL 6710
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeIEELEAQIEQLKEELKALREALDELRAEL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6711 EEVQGLAGEFQDVLDPLTTWLDAANKRFTALEPHSPDAEG--------IEHLIQELKKLQKEVNEHEPAMKQLATAGKKL 6782
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieslaaeIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6783 QD--YCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFlswASKVEPELRALELGVPDEETN 6860
Cdd:TIGR02168 893 RSelEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEE 969
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727998 6861 IEELANQLTEEMQPLldiinsegaelaevapGDAGLRVEDIINRDNKRFDNLRDQIE 6917
Cdd:TIGR02168 970 ARRRLKRLENKIKEL----------------GPVNLAAIEEYEELKERYDFLTAQKE 1010
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5990-6167 |
1.49e-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: 82.49 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5990 KQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKtdLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEa 6069
Cdd:cd00176 37 ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6070 DCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPTTEvRAIADKVGEL 6149
Cdd:cd00176 114 DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEEL 191
|
170
....*....|....*...
gi 1397727998 6150 QGEWTRLQQEVTVQDSRL 6167
Cdd:cd00176 192 NERWEELLELAEERQKKL 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5229-5450 |
3.55e-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: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5229 KHRQFNDVAFKLLTWLTDMEGQLSSvkqDAGLSEPQQLQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNSLSGQAAEq 5308
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5309 qqvakLQSTMNDLSVRYSTLTKDINSHVTQLQAAVTHSQDITQAMnELVSWMDSAEQVVTTQLPISLRrPELNAQLQSFS 5388
Cdd:cd00176 77 -----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDL-ESVEELLKKHK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5389 AVDADVTNHQSALDAVKALANELVKTCELDIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEE 5450
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6716-6924 |
6.79e-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: 80.57 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6716 LAGEFQDVLDPLTTWLDAANKRFTALEPhSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYcKGEDVIMIQ 6795
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6796 LKIDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHaEFLSWASKVEPELRALELGvpDEETNIEELANQL------T 6869
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLG--KDLESVEELLKKHkeleeeL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 6870 EEMQPLLDIINSEGAELAEVAPGDAGLRVEDIINRDNKRFDNLRDQIEKRAQKVQ 6924
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6897-7645 |
8.22e-16 |
|
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: 86.26 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6897 RVEDIINRDNKRFDNLRDQIEKrAQKVQLARQRSSEVvnELGDLVDWFVDADSRLQNqqpiasdldlLQQQLAEQKVMNE 6976
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQAEK-AERYKELKAELREL--ELALLVLRLEELREELEE----------LQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6977 EINNQKVKardtlsaskkllSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFAR-HFHEAHTELVVWLDD 7055
Cdd:TIGR02168 257 ELTAELQE------------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILReRLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7056 VEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRkpiVDRLNKTgtalvamcgskgAEQVQSMLDDDNRRMDNVRTKVR 7135
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAE---LEELEAE------------LEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7136 DRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSA--EPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEEL 7213
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7214 LRQAGDEQDEAVKDVRQKLEELTKLyKDIQERGRGRQRALEETLAVAEKF-------WDELH-----------ALNSSL- 7274
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLsgilgvlSELISvdegyeaaieaALGGRLq 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7275 ----KDLQEALSSVDQPA--------------LEPEAIREQQEELEALKEDIEASQADFEE------------------- 7317
Cdd:TIGR02168 549 avvvENLNAAKKAIAFLKqnelgrvtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvv 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7318 -------------------VQQTGDTLLG---MVGTTEQP-----EVQKNVDDAGASLAAISDQYSKRSQELESALAQAV 7370
Cdd:TIGR02168 629 ddldnalelakklrpgyriVTLDGDLVRPggvITGGSAKTnssilERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7371 HFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQW-DELKNFKTRVEPKNVEIESLNQHVTEL--TKSSTPEQASVLR 7447
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeERIAQLSKELTELEAEIEELEERLEEAeeELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7448 EPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHKELKNWMDLVDVTLDEITPVYGDPKLVEIELAK-LRIVQNDI 7526
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7527 TAHQESVESISKEaqRLMTSEGIAQAQGLKTKMEDMEKTWEN----IQAKSRAKQDMLEDGLREAQGFTGELQDILAKIN 7602
Cdd:TIGR02168 869 EELESELEALLNE--RASLEEALALLRSELEELSEELRELESkrseLRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1397727998 7603 D---IEGQLIISKPVGGLPETAKeqlekfmdVYAELEKLEPQVQSL 7645
Cdd:TIGR02168 947 EeysLTLEEAEALENKIEDDEEE--------ARRRLKRLENKIKEL 984
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5696-5840 |
1.10e-15 |
|
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: 79.80 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5696 DDLSEVQQQLLDITQRYEIVGERLADRQQELQLMLtSIRTFMQDMQDILQWLDLKDHETDSaQPLPTNEKDAKKRLKEHE 5775
Cdd:cd00176 72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHK 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 5776 VFHREILSKEGLVEDIRKKAQDLLKTRHGVPGEEmLQQQLQELDDKWHGLRALSEQQRKGLEDMV 5840
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7807-7908 |
4.37e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 74.67 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7807 QFNDTWKDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQAML 7886
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7887 TELKSHWNNVCSKSVDRQRKLE 7908
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
180-279 |
5.48e-15 |
|
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: 74.30 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 180 REALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSN---KQNLELAFTVAEKEF-GVTRLL 255
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLGlPELDLF 80
|
90 100
....*....|....*....|....
gi 1397727998 256 DPEDVdVPNPDEKSILTYVSSLYD 279
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6576-7320 |
9.15e-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: 82.80 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6576 LETDLESLaERWAGLVEKVAEHEKNLDSALLR--TGKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQ 6653
Cdd:TIGR02168 198 LERQLKSL-ERQAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6654 KMVTDRTPSMKAVQDSGNQLITGLDpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDA 6733
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLE-QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6734 ANKRFTALEPHSPDAEGIEH---------------LIQELKKLQKEVNEHEPAMKQLATAGKKLQDYCKGEDVIMIQLKI 6798
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEeleeqletlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6799 DGVQKQNGELRSHIED---CLEQMEEALP-LAKHFQEAHAEFLSWASKVE---PELRALE------LGVPDEETNIEELA 6865
Cdd:TIGR02168 436 KELQAELEELEEELEElqeELERLEEALEeLREELEEAEQALDAAERELAqlqARLDSLErlqenlEGFSEGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6866 NQLTEEMQPLLDIINS-EGAELA-EVApgdAGLRVEDII-NRDNKRFDNLRDQIEKRAQKV----------QLARQRSSE 6932
Cdd:TIGR02168 516 SGLSGILGVLSELISVdEGYEAAiEAA---LGGRLQAVVvENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6933 VVNELGDLVDW---FVDADSRLQNQ-QPIASDL---DLLQQQLAEQKVMNEEINNQkVKARDTLSASKKLLSDSAMEDNS 7005
Cdd:TIGR02168 593 ILKNIEGFLGVakdLVKFDPKLRKAlSYLLGGVlvvDDLDNALELAKKLRPGYRIV-TLDGDLVRPGGVITGGSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7006 AI--RNKMDELKQWVDTVSGSANErqslLEQAVPFARHFHEAHTELVVWLDDVEPVLS-ELDVLSVDADQVKKQQEKA-- 7080
Cdd:TIGR02168 672 ILerRREIEELEEKIEELEEKIAE----LEKALAELRKELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLee 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7081 ------KVLKQEVADRKPIVDRLNKTGTALVAmcGSKGAEQVQSMLDDDNRRMDNVRTKVRDRSNsidQAMQQSAEFTDK 7154
Cdd:TIGR02168 748 riaqlsKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7155 LENMLDTLTVTAEQVRSAEPISAQPDKLREQIEE-NKAME------EDLEMRHNALESVKNAAEELLRQAGDEQDEAVKD 7227
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESlAAEIEeleeliEELESELEALLNERASLEEALALLRSELEELSEE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7228 VRQKLEELTKLYKDIQERgRGRQRALEETLAVAEKFWDEL-HALNSSLKD-LQEALSSVDQPALEPEAIREQQEELEALK 7305
Cdd:TIGR02168 903 LRELESKRSELRRELEEL-REKLAQLELRLEGLEVRIDNLqERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
810
....*....|....*....
gi 1397727998 7306 EDI----EASQADFEEVQQ 7320
Cdd:TIGR02168 982 KELgpvnLAAIEEYEELKE 1000
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5347-5556 |
9.96e-15 |
|
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: 77.10 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5347 QDITQAMNELVSWMDSAEQVVTTQLPISlRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELVKTCELDiARAVEQR 5426
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5427 LTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEkLEQTNLWVHDGILQLDSKELSKL--SSDDMKQQLEKLAREKHNRL 5504
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDleSVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5505 RTIQEIQVAAEQLLQDPRTGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASD 5556
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
178-281 |
1.50e-14 |
|
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: 73.16 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 257
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|....
gi 1397727998 258 EDVdVPNPDEKSILTYVSSLYDVF 281
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHFHSAF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
550-739 |
3.36e-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: 75.56 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 550 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE--EQKLYTQ-KLSSVE 626
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghPDAEEIQeRLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 627 VAYSLLLNTSSRRLKFLE---SLSEFLQGATAELTWLAEREEVEVTRDWVSKDLNLADLDDHHKNLIRQVEARERHFNAV 703
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1397727998 704 QEKGGAMILDRHPAASM-VEVLMASLQARWSWLLQLV 739
Cdd:cd00176 166 NELAEELLEEGHPDADEeIEEKLEELNERWEELLELA 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6680-7475 |
2.25e-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: 78.17 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6680 AERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEPHspdaegIEHLIQELK 6759
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ------KQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6760 KLQKEVNEHEpamKQLATAGKKLQDYckGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEalpLAKHFQEAHAEFLSW 6839
Cdd:TIGR02168 313 NLERQLEELE---AQLEELESKLDEL--AEELAELEEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6840 ASKVEPELRALELgVPDEETNIEELANQLTEEMQPLLDIINSEGAELAEVAPGDAGLRVEDII----------NRDNKRF 6909
Cdd:TIGR02168 385 RSKVAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEeeleelqeelERLEEAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6910 DNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSR-------LQNQQPIASDLDLLQQQLaeqkvmneeinnqK 6982
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvkalLKNQSGLSGILGVLSELI-------------S 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6983 VKARDTLSASKKL---LSDSAMEDNSAIRNKMDELKQwvdtvsgSANERQSLLEQAVPFARHFHEAHTELVVWLDDVEPV 7059
Cdd:TIGR02168 531 VDEGYEAAIEAALggrLQAVVVENLNAAKKAIAFLKQ-------NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7060 LSELDvlsvdadqvkKQQEKAKVLKQEVADRKPIVDRLNktgTALvAMCGSKGAEQVQSMLDDD--------NRRMDNVR 7131
Cdd:TIGR02168 604 AKDLV----------KFDPKLRKALSYLLGGVLVVDDLD---NAL-ELAKKLRPGYRIVTLDGDlvrpggviTGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7132 TKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSaepisaqpdkLREQIEENKAMEEDLEMRHNALESVKNAAE 7211
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE----------LEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7212 ELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrgrqraLEETLAVAEkfwDELHALNSSLKDLQEALssvdqpalep 7291
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEE--------AEEELAEAE---AEIEELEAQIEQLKEEL---------- 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7292 EAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVH 7371
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7372 FQDQLMKLLVWLQEAEDEFSEFEPVASEFET-IKKQWDELKNFKTRVEPKNVEIESLNQHVTELtKSSTPEQASVLREPM 7450
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESkRSELRRELEELREKLAQLELRLEGLEVRIDNL-QERLSEEYSLTLEEA 956
|
810 820
....*....|....*....|....*
gi 1397727998 7451 TQLNIRWNNLLTNIGDRQRELQMAL 7475
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5881-6603 |
3.48e-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: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5881 MEQVKVLREELSAQEPTydhflncahgiLERCGDKSQDGIAVSRRLDTVSKAW--NKLQSRLNERSKNLSSVEGISVEFA 5958
Cdd:TIGR02168 188 LDRLEDILNELERQLKS-----------LERQAEKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5959 SLTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELKQ----LESELIVQQPRLARA-RDLCRQLCDKAKDASTKTDLR 6033
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrLEQQKQILRERLANLeRQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6034 SKLTALEKDMNDTTRKLEICKAAVEEASQQAE----KFEADCKELLTWISEAANNLQESEPLSSDLDILREQM-RQNRTL 6108
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLeRLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6109 QQELSLKEPEIRQLLEKGDKLVKESSPTTEvRAIAdkvgELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKMAMWL 6188
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELE-EELE----ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6189 QMTEEKLEKMKPEDVDQNTVVHKLKELQGV---------------------------------------------QNEMM 6223
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGIlgvlselisvdegyeaaieaalggrlqavvvenlnaakkaiaflkQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6224 K--------------KSHDRERLNSEGT-----------------------SLVECVDSGKEAIKQQVA----------- 6255
Cdd:TIGR02168 572 RvtflpldsikgteiQGNDREILKNIEGflgvakdlvkfdpklrkalsyllGGVLVVDDLDNALELAKKlrpgyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6256 --VINERW------DAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKL-AVHNSLGLSAKDPKHINR-IKDL 6325
Cdd:TIGR02168 652 gdLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRqISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6326 LEDTGWLASQLNNTETMLNSIEvdgGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLEL 6405
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6406 ESELgsktpvSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQAsslcnagyvsdpELLKSQVEALSNQHASLTERATQ 6485
Cdd:TIGR02168 809 RAEL------TLLNEEAANLRERLESLERRIAATERRLEDLEEQI------------EELSEDIESLAAEIEELEELIEE 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6486 RQSDVVANQHSIQHLTQALNLVWGDIDKASSTLDAMGpaggnvTTVKALQEELkgfvkstmEPLQKQFESVSRQGQALik 6565
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELE------SKRSELRREL--------EELREKLAQLELRLEGL-- 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 1397727998 6566 tavagsnTTGLETDLESLAERWAGLVEKVAEHEKNLDS 6603
Cdd:TIGR02168 935 -------EVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6825-7036 |
4.17e-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: 72.48 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6825 LAKHFQEAHAEFLSWASKVEPELRALELGvpDEETNIEELANQ---LTEEMQPL---LDIINSEGAELAEVAPGDAGlRV 6898
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKheaLEAELAAHeerVEALNELGEQLIEEGHPDAE-EI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6899 EDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVvNELGDLVDWFVDADSRLQNQQPIaSDLDLLQQQLAEQKVMNEEI 6978
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6979 NNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAV 7036
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
178-284 |
9.97e-13 |
|
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: 67.79 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWsrrTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21230 1 TPKQRLLGW---IQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90 100
....*....|....*....|....*...
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSlydvFPQV 284
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLSQ----FPKA 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5734-5837 |
1.53e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 67.35 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5734 RTFMQDMQDILQWLDLKDhETDSAQPLPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQQ 5813
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEE 77
|
90 100
....*....|....*....|....
gi 1397727998 5814 QLQELDDKWHGLRALSEQQRKGLE 5837
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7916-8016 |
2.42e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 66.58 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7916 QFTEALDALLDWLAKVEPALADDaPVHGDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 7995
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727998 7996 ELNAAWDRVCKLSVSKQDRLE 8016
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6065-6167 |
2.42e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 66.58 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6065 EKFEADCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPttEVRAIAD 6144
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|...
gi 1397727998 6145 KVGELQGEWTRLQQEVTVQDSRL 6167
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6173-6376 |
3.33e-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: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6173 HAQQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQ 6252
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6253 QVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLaEATSALNKWENKLAVHNSLGLSAKDPKHINRIKDLLEDTGWL 6332
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1397727998 6333 ASQLNNTETMLNSIEVDGGETS--NLRDELNKLRGQHQTLQGELSE 6376
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDAdeEIEEKLEELNERWEELLELAEE 204
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5843-6060 |
3.55e-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: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5843 LRDMREHEQqltlWLAQKDRMLDVLGPVAmEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDgiaV 5922
Cdd:cd00176 6 LRDADELEA----WLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5923 SRRLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRgLADWLSDFSDKLDGQGKVSSQPDKQhKQLQELKQLESEL 6002
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVE-ELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6003 IVQQPRLARARDLCRQLCDKAKDASTKtDLRSKLTALEKDMNDTTRKLEICKAAVEEA 6060
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
195-275 |
1.31e-11 |
|
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: 64.71 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 195 PGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDVPNPDEKSILTY 273
Cdd:cd21229 17 PELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDLSSPHLDELSGMTY 96
|
..
gi 1397727998 274 VS 275
Cdd:cd21229 97 LS 98
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8023-8124 |
2.36e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 63.89 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8023 EEFHKKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEANLRETLNIGQDIMKRCHPDSVPImKQW 8102
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI-EER 78
|
90 100
....*....|....*....|..
gi 1397727998 8103 LSVIRARWEELTALGRQRSARL 8124
Cdd:smart00150 79 LEELNERWEELKELAEERRQKL 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7167-8118 |
2.36e-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: 71.63 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7167 EQVRSAEPISAQPDKLREQIEE---------------NK--AMEEDLEMRHNALESVKNAAEELLRQAgdEQDEAVKDVR 7229
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEaagiskykerrketeRKleRTRENLDRLEDILNELERQLKSLERQA--EKAERYKELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7230 QKLEELTK--LYKDIQERgRGRQRALEETLAVAEkfwDELHALNSSLKDLQEALSSVD--QPALEpEAIREQQEELEALK 7305
Cdd:TIGR02168 220 AELRELELalLVLRLEEL-REELEELQEELKEAE---EELEELTAELQELEEKLEELRleVSELE-EEIEELQKELYALA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7306 EDIEASQADFEEVQQTgdtllgmvgtteqpevQKNVDDAGASLAAISDQYSKRSQELESALAQAvhfQDQLMKLLVWLQE 7385
Cdd:TIGR02168 295 NEISRLEQQKQILRER----------------LANLERQLEELEAQLEELESKLDELAEELAEL---EEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7386 AEDEFSEFEpvasefetikkqwDELKNFKTRVEPKNVEIESLNQHVTELTKS--STPEQASVLREPMTQLNIRWNNLLTN 7463
Cdd:TIGR02168 356 LEAELEELE-------------AELEELESRLEELEEQLETLRSKVAQLELQiaSLNNEIERLEARLERLEDRRERLQQE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7464 IGDRQRELQMAlltagqfdhahkelknwmdlvdvtldeitpvygDPKLVEIELAKLRIVQNDITAHQESVESISKEAQrl 7543
Cdd:TIGR02168 423 IEELLKKLEEA---------------------------------ELKELQAELEELEEELEELQEELERLEEALEELR-- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7544 mtsEGIAQAQGLKTKMEDMEktweniqAKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-----IISKPVGGlp 7618
Cdd:TIGR02168 468 ---EELEEAEQALDAAEREL-------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEGY-- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7619 ETAKEQ-LEKFMDvYAELEKLEPQVQSLNVMGEKLGGKSKGPALANLRQNlqhlnqrcdYIRSRACDRKKKLEDaegmat 7697
Cdd:TIGR02168 536 EAAIEAaLGGRLQ-AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT---------EIQGNDREILKNIEG------ 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7698 nFHGELNKFISWLTDTEKTLNNLQPVSRLVERVTSQIEDHRDLqkdisKHREAMVALE-----KMGTHLKYFSQKQDVVL 7772
Cdd:TIGR02168 600 -FLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKL-----RPGYRIVTLDgdlvrPGGVITGGSAKTNSSIL 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7773 IKNllSSIQHRWEKIvSRSAERTRHLERGYKEAKQFNDTWKDLITWLIEAEKTLETETSVAnepdkiKAQISKHKEFQRR 7852
Cdd:TIGR02168 674 ERR--REIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL------RKDLARLEAEVEQ 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7853 LGAKQpvydgvnkaGRLLKERCPSDDVPTIQ-AMLTELKSHWNNVCSKSVDRQRKLEEGLLLSGQFTEALDALLDWLAKV 7931
Cdd:TIGR02168 745 LEERI---------AQLSKELTELEAEIEELeERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7932 EPALADDAPVHGDIdtvngfldihkafQQELGARTTTIAFLQKSAK---EIISRAEGDVCSLQSDLIELNAAWDRVCKLS 8008
Cdd:TIGR02168 816 NEEAANLRERLESL-------------ERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNER 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8009 VSKQDRLEHAQRLAEEFHKKAQQLLSWLADAERQLhyrgpipDEEPLILQQMEEHK-KFEESLLRQEANLRETLNIGQDI 8087
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLeGLEVRIDNLQERLSEEYSLTLEE 955
|
970 980 990
....*....|....*....|....*....|..
gi 1397727998 8088 MKRCHPDSVPIMKQW-LSVIRARwEELTALGR 8118
Cdd:TIGR02168 956 AEALENKIEDDEEEArRRLKRLE-NKIKELGP 986
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6404-6605 |
2.62e-11 |
|
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: 67.09 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6404 ELESELgSKTPVSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQASSLCNAGYvSDPELLKSQVEALSNQHASLTERA 6483
Cdd:cd00176 18 EKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6484 TQRQSDvVANQHSIQHLTQALNLVWGDIDKASSTLDAMgPAGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQAL 6563
Cdd:cd00176 96 EERRQR-LEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKEL-EEELEAHEPRLKSLNELAEEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1397727998 6564 IKTAVAGSNTTgLETDLESLAERWAGLVEKVAEHEKNLDSAL 6605
Cdd:cd00176 173 LEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6610-6711 |
3.72e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 63.50 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 KFQDAMASLLDWLAETEELVAmQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITgLDPAERKHIESEL 6689
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 6690 QQLNSRWEALTKRVVDRTAILE 6711
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6680-7310 |
4.42e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6680 AER-KHIESELQQLnsRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEphspdaEGIEHLIQEL 6758
Cdd:COG1196 212 AERyRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR------LELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6759 KKLQKEVNEHEpamKQLATAGKKLQDYCkgEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAlplakhfQEAHAEFls 6838
Cdd:COG1196 284 EEAQAEEYELL---AELARLEQDIARLE--ERRRELEERLEELEEELAELEEELEELEEELEEL-------EEELEEA-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6839 waskvEPELRALELgvpdEETNIEELANQLTEEMQPLLDIINSEGAELAEVApgDAGLRVEDIINRDNKRFDNLRDQIEK 6918
Cdd:COG1196 350 -----EEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEAL--RAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6919 RAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQpiASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSD 6998
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE--EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6999 SAMEDNSAirnkmdelkqwvdtvsgsANERQSLLEQAVPFARHFHEAHTELVVWLDDVEPVL------SELDVLSVDADQ 7072
Cdd:COG1196 497 LEAEADYE------------------GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7073 VKKQQEKAKVLKQEVADRKPI--VDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVRTKVRDRSnsidqamqqsaE 7150
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLdkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT-----------L 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7151 FTDKLENMLDTLTVTAEQVRSAEpisaqpdKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQ 7230
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVT-------LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7231 KLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNssLKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEA 7310
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL--LEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6978-7756 |
4.48e-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: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6978 INNQKVKARDTLSaskkLLSDSAMEDNS-AI--RNKMDELkqwvdtVSGSANERQSLLEQAVPFARHF---HEAHTELVV 7051
Cdd:TIGR02168 114 INGQPCRLKDIQD----LFLDTGLGKRSySIieQGKISEI------IEAKPEERRAIFEEAAGISKYKerrKETERKLER 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7052 W---LDDVEPVLSEL----DVLSVDADQVKKQQEKAKVLKQevADRKPIVDRLNKTGTALvamcgskgaEQVQSMLDDDN 7124
Cdd:TIGR02168 184 TrenLDRLEDILNELerqlKSLERQAEKAERYKELKAELRE--LELALLVLRLEELREEL---------EELQEELKEAE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7125 RRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKAMEEDLEMRHNALE 7204
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEAQLEELE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7205 SVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSV 7284
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7285 DQPALEPEAIREQQEELEAlkediEASQADFEEVQQTGDTLlgmvgTTEQPEVQKNVDDAGASLAAISDQYSKRSQELES 7364
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLK-----KLEEAELKELQAELEEL-----EEELEELQEELERLEEALEELREELEEAEQALDA 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7365 ALAQAVHFQDQLmKLLVWLQEAEDEFsefepvaseFETIKKQWDELKNFKT---------RVEPK---NVEI---ESLNQ 7429
Cdd:TIGR02168 480 AERELAQLQARL-DSLERLQENLEGF---------SEGVKALLKNQSGLSGilgvlseliSVDEGyeaAIEAalgGRLQA 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7430 HVTELTKS-----STPEQASVLREPMTQLNIRWNNLLT-NIGDRQRELQMALLTAGQFDHAHKELKNWMD-------LVD 7496
Cdd:TIGR02168 550 VVVENLNAakkaiAFLKQNELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlVVD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7497 ------------------VTLDE--ITP---VYGDPKLVE-------IELAKLRivqNDITAHQESVESISKEAQRLMTs 7546
Cdd:TIGR02168 630 dldnalelakklrpgyriVTLDGdlVRPggvITGGSAKTNssilerrREIEELE---EKIEELEEKIAELEKALAELRK- 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7547 egiaQAQGLKTKMEDMEKTWENIQAKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-IISKPVGGLPETAKEQL 7625
Cdd:TIGR02168 706 ----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeELEERLEEAEEELAEAE 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7626 EKFMDVYAELEKLEPQVQSLNVMGEKLGGKSK--GPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEGMATNFHGEL 7703
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 7704 NKFISWLTDTEKTLNNLQPVSRLVERVTSQIEDHRD-LQKDISKHREAMVALEK 7756
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEeLSEELRELESKRSELRR 915
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
6780-7565 |
6.76e-11 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 70.47 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6780 KKLQDYckGEDVIMIQLKIDGVQKQNgelrshiedcLEQMEEALPLAKHFQEAHAEFLSWASKVEPELRALELGVPDEET 6859
Cdd:TIGR01612 565 KELEEE--NEDSIHLEKEIKDLFDKY----------LEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENN 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6860 N--IEELAN----QLTEEMQPLLDIINSEGAELAEVAPGD---------AGLRVEDIINRDNK-RFDNLRDQIEKRAQKV 6923
Cdd:TIGR01612 633 NayIDELAKispyQVPEHLKNKDKIYSTIKSELSKIYEDDidalynelsSIVKENAIDNTEDKaKLDDLKSKIDKEYDKI 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6924 Q-----LARQRSSEVVNELGDLVDWFVDADSRLQNQqpIASDLD-LLQQQLAEQKVMNEEINNQKvKARDTLSASKKLLS 6997
Cdd:TIGR01612 713 QnmetaTVELHLSNIENKKNELLDIIVEIKKHIHGE--INKDLNkILEDFKNKEKELSNKINDYA-KEKDELNKYKSKIS 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6998 D--SAMEDNSAIRNKMDE--------LKQWVDTVSGSANERQSLLEQaVPFARHFHEAHTELVVWLDD--VEPVLSELDV 7065
Cdd:TIGR01612 790 EikNHYNDQINIDNIKDEdakqnydkSKEYIKTISIKEDEIFKIINE-MKFMKDDFLNKVDKFINFENncKEKIDSEHEQ 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7066 LSVDADQVKKQ--QEKAKVLKQEVADRKPIVDRLNKT-------------GTALVAMCGSKgAEQVQSMLDDDNRRMD-- 7128
Cdd:TIGR01612 869 FAELTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSieeeyqnintlkkVDEYIKICENT-KESIEKFHNKQNILKEil 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7129 NVRTKVRDRSNSIDQAmqqsaeFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLemrhnalesvKN 7208
Cdd:TIGR01612 948 NKNIDTIKESNLIEKS------YKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANL----------GK 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7209 AAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQ----------------ERGRGRQRALEETLAVAE----------- 7261
Cdd:TIGR01612 1012 NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEiaihtsiyniideiekEIGKNIELLNKEILEEAEinitnfneike 1091
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7262 ----------------KFWDELHALNSSLKDLQEalsSVDQPALEPEAIREQQE----ELEALKEDIEA------SQADF 7315
Cdd:TIGR01612 1092 klkhynfddfgkeeniKYADEINKIKDDIKNLDQ---KIDHHIKALEEIKKKSEnyidEIKAQINDLEDvadkaiSNDDP 1168
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7316 EEVQQTGDTLLGMVgtteqpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSE--- 7392
Cdd:TIGR01612 1169 EEIEKKIENIVTKI------DKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmi 1242
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7393 --FEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLN-------QHVTelTKSSTPEQASVLREPMTQLnIRWNNLLTN 7463
Cdd:TIGR01612 1243 kaMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNishdddkDHHI--ISKKHDENISDIREKSLKI-IEDFSEESD 1319
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7464 IGDRQRELQMALLTAGQFDHAhkelknwmdlVDVTLDEITPVYGDPKLVEIE--LAKLRIVQNDITAHQESVESISKEAQ 7541
Cdd:TIGR01612 1320 INDIKKELQKNLLDAQKHNSD----------INLYLNEIANIYNILKLNKIKkiIDEVKEYTKEIEENNKNIKDELDKSE 1389
|
890 900
....*....|....*....|....
gi 1397727998 7542 RLMTSegIAQAQGLKTKMEDMEKT 7565
Cdd:TIGR01612 1390 KLIKK--IKDDINLEECKSKIEST 1411
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7181-7767 |
1.03e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7181 KLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrgrqraLEETLAVA 7260
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE--------LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7261 EKFWDELHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEasqaDFEEVQQTGDTLLGMVGTTEQPEVQKN 7340
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELE------ERIEELKKEIEELEEKVK----ELKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7341 VDDAGASlaaisdQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRVEPK 7420
Cdd:PRK03918 311 EIEKRLS------RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7421 nvEIESLNQHVTELTKSSTPeqasvLREPMTQLNIRWNNLLTNIGDRQR---ELQMAL----LTAGQFDHAHKElknwmD 7493
Cdd:PRK03918 385 --TPEKLEKELEELEKAKEE-----IEEEISKITARIGELKKEIKELKKaieELKKAKgkcpVCGRELTEEHRK-----E 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7494 LVDVTLDEItpvygdpKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMTSEGIA-QAQGLKTKM-----EDMEKTWE 7567
Cdd:PRK03918 453 LLEEYTAEL-------KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeQLKELEEKLkkynlEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7568 NIQ------AKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-----IIS----KPVGGLPETAKEqLEKFMDVY 7632
Cdd:PRK03918 526 EYEklkeklIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELaellkELEelgfESVEELEERLKE-LEPFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7633 AELEKLEPQVQSLNVMGEKLGGKskgpaLANLRQNLQHLNQRCDYIRSRACDRKKKLEDAE-GMATNFHGELNKFISWLT 7711
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEE-----LDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLR 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7712 DTEKTLNNlqpvsrLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKYFSQK 7767
Cdd:PRK03918 680 AELEELEK------RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5882-6451 |
1.71e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5882 EQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDGIAVSRRLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASL- 5960
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELe 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5961 ---------TRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELKQLESELIvqqpRLARARDlcrqlcdkakdastktD 6031
Cdd:PRK03918 245 keleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYE----------------E 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6032 LRSKLTALEKDMNDTTRKLEickaAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQE 6111
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6112 LSLKEPE-IRQLLEKGDKLVKESspTTEVRAIADKVGELQGEWTRLQ-----------------QEVTVQDSRLTMAGSH 6173
Cdd:PRK03918 381 LTGLTPEkLEKELEELEKAKEEI--EEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgRELTEEHRKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6174 A---------QQFTERLDK-----------------------MAMWLQMTEEKLEKMKPEDVDQNTvvhklKELQGVQNE 6221
Cdd:PRK03918 459 AelkriekelKEIEEKERKlrkelrelekvlkkeseliklkeLAEQLKELEEKLKKYNLEELEKKA-----EEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6222 MMKKSHDRERLNSEGTSLvecvdsgkEAIKQQVAVINERWDAVNKALSERASHLEDLG-QRLGEVQDSLAEATSALNKWe 6300
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKL--------EELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEY- 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6301 nklavhnslgLSAKD-PKHINRIKDLLEDtgwLASQLNNTETMLNSIEVDGGETSNLRDELNK---------LRGQHQTL 6370
Cdd:PRK03918 605 ----------LELKDaEKELEREEKELKK---LEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeeLREEYLEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6371 QGELSELVAEMETGAQIVEQFQGLLKivggqflELESELGsktpvSRDDAELGSQ-LADMKDFLTRLGEKVETLKDLEQQ 6449
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLE-------KLKEELE-----EREKAKKELEkLEKALERVEELREKVKKYKALLKE 739
|
..
gi 1397727998 6450 AS 6451
Cdd:PRK03918 740 RA 741
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7699-7799 |
1.87e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 61.19 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7699 FHGELNKFISWLTDTEKTLNNlQPVSRLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyFSQKQDVVLIKNLLS 7778
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727998 7779 SIQHRWEKIVSRSAERTRHLE 7799
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6892-7434 |
2.66e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6892 GDAGLRVEDIinRDNKR--FDNLRDQIEKRAQKvqlarqrssevvnelgDLVDwfvdadsrlqnqqpiasDLDLLQQQLA 6969
Cdd:PRK02224 172 SDARLGVERV--LSDQRgsLDQLKAQIEEKEEK----------------DLHE-----------------RLNGLESELA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6970 EQKVMNEEINNQKVKARDTLSASkkllsDSAMEDNSAIRNKMDELKQWVD----TVSGSANERQSLLEQAvpfarhfHEA 7045
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEA-----DEVLEEHEERREELETLEAEIEdlreTIAETEREREELAEEV-------RDL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7046 HTELVVWLDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADR----KPIVDRLNKTGTALV--AMCGSKGAEQVQSM 7119
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRleecRVAAQAHNEEAESLRedADDLEERAEELREE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7120 LDDDNRRMDNVRTKVRDRSNSID----QAMQQSAEFTD------KLENMLDTLTVTAEQVRSAE---------------- 7173
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEeleeEIEELRERFGDapvdlgNAEDFLEELREERDELREREaeleatlrtarervee 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7174 ----------PISAQP----------DKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAG--------------- 7218
Cdd:PRK02224 445 aealleagkcPECGQPvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrierleerredleel 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7219 -DEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQ 7297
Cdd:PRK02224 525 iAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7298 QEELEALKEDIEASQADFEEVQQTGDTLlgmvgTTEQPEVQKNVDDAgaslaaisdqyskRSQELESALAQAVHFQDQLM 7377
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLAEK-----RERKRELEAEFDEA-------------RIEEAREDKERAEEYLEQVE 666
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 7378 KLLVWLQEAEDEF-SEFEPVASEFETIKKQWDELKNFKTRVEpknvEIESLNQHVTEL 7434
Cdd:PRK02224 667 EKLDELREERDDLqAEIGAVENELEELEELRERREALENRVE----ALEALYDEAEEL 720
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7588-7690 |
4.20e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 60.42 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7588 QGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLgGKSKGPALANLRQN 7667
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727998 7668 LQHLNQRCDYIRSRACDRKKKLE 7690
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7040-7142 |
6.27e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 60.04 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7040 RHFHEAHTELVVWLDDVEPVLSELDVlSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMcGSKGAEQVQSM 7119
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727998 7120 LDDDNRRMDNVRTKVRDRSNSID 7142
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6062-6158 |
6.33e-10 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 60.02 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6062 QQAEKFEADCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPTTEvrA 6141
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE--E 77
|
90
....*....|....*..
gi 1397727998 6142 IADKVGELQGEWTRLQQ 6158
Cdd:pfam00435 78 IQERLEELNERWEQLLE 94
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7083-7756 |
6.89e-10 |
|
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: 67.02 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7083 LKQEVADRKPIVDRLNKTGTALVAMCgSKGAEQVQSMLDDDNRRmdnVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTL 7162
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLL-EELNKKIKDLGEEEQLR---VKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7163 TVTAEQVRSaepISAQPDKLREQIEENKAMEEDLEmrhNALESVKNAAEELLRQAGDEQDEA------VKDVRQKLEELT 7236
Cdd:TIGR02169 325 AKLEAEIDK---LLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEEVDKEFaetrdeLKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7237 KLYKDIQergRGRQRALEEtlavAEKFWDELHALNSSLKDLQEALSSVDQPALEP-EAIREQQEELEALKEDIEASQADF 7315
Cdd:TIGR02169 399 REINELK---RELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKaLEIKKQEWKLEQLAADLSKYEQEL 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7316 EEVQQTGDTLlgmvgTTEQPEVQKNVDDAGASLAAISD--QYSKRSQELESALAQAVHfqdqlmKLLVWLQEAEDEFSEF 7393
Cdd:TIGR02169 472 YDLKEEYDRV-----EKELSKLQRELAEAEAQARASEErvRGGRAVEEVLKASIQGVH------GTVAQLGSVGERYATA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7394 EPVASefetikkqwdelknfKTRVEPKNVEIESLNQHVTELTKSstpEQASvlrePMTQLNirwnnlLTNIGDRQRELQm 7473
Cdd:TIGR02169 541 IEVAA---------------GNRLNNVVVEDDAVAKEAIELLKR---RKAG----RATFLP------LNKMRDERRDLS- 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7474 ALLTAGQFDHAhkelknwMDLVD----------------------------------VTLD------------------- 7500
Cdd:TIGR02169 592 ILSEDGVIGFA-------VDLVEfdpkyepafkyvfgdtlvvedieaarrlmgkyrmVTLEgelfeksgamtggsraprg 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7501 -EITPVYGDPKLVEI--ELAKLRIVQNDITAHQESVESISKEAQRLM------TSEGIAQAQGLKTKMEDMEKTWENIQA 7571
Cdd:TIGR02169 665 gILFSRSEPAELQRLreRLEGLKRELSSLQSELRRIENRLDELSQELsdasrkIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7572 KSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQLiiskpvgGLPEtAKEQLEKFMDVYAELEKLEPQVQSLNVMGEK 7651
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-------NDLE-ARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7652 LGGK--SKGPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEGmatnfhgELNKFISWLTDTEKTLNNLqpvsrlver 7729
Cdd:TIGR02169 817 IEQKlnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDL--------- 880
|
730 740
....*....|....*....|....*..
gi 1397727998 7730 vtsqIEDHRDLQKDISKHREAMVALEK 7756
Cdd:TIGR02169 881 ----ESRLGDLKKERDELEAQLRELER 903
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7053-7889 |
8.15e-10 |
|
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: 66.63 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7053 LDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKT-GTALV----AMCGSKgaEQVQSMLDDDNRRM 7127
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYeGYELLkekeALERQK--EAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7128 DNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLD--TLTVTAEqvrsAEPISAQPDKLREQIEENKAMEEDLEmrhnalES 7205
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeQLRVKEK----IGELEAEIASLERSIAEKERELEDAE------ER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7206 VKNAAEELLRQAGD--EQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSS 7283
Cdd:TIGR02169 324 LAKLEAEIDKLLAEieELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7284 V----DQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVgTTEQPEVQKNVDDAGASLAAISDQYSKRS 7359
Cdd:TIGR02169 404 LkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7360 QELESAlaqavhfQDQLMKLLVWLQEAEDEFSEFEPVASEFET----IKKQWDELknfkTRVEPKNV-EIES-----LNQ 7429
Cdd:TIGR02169 483 KELSKL-------QRELAEAEAQARASEERVRGGRAVEEVLKAsiqgVHGTVAQL----GSVGERYAtAIEVaagnrLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7430 HVTElTKSSTPEQASVLRE----PMTQLNirwnnlLTNIGDRQRELQmALLTAGQFDHAhkelknwMDLVDVTlDEITP- 7504
Cdd:TIGR02169 552 VVVE-DDAVAKEAIELLKRrkagRATFLP------LNKMRDERRDLS-ILSEDGVIGFA-------VDLVEFD-PKYEPa 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7505 ---VYGDPKLVE-IELAK-LRIVQNDITAHQESVE--------SISKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQA 7571
Cdd:TIGR02169 616 fkyVFGDTLVVEdIEAARrLMGKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7572 KSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQLiiskpvgglpETAKEQLEKFMDVYAELEKlepqvqslnvmgek 7651
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE----------EKLKERLEELEEDLSSLEQ-------------- 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7652 lggkskgpALANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEGMATnfHGELNKFISWLTDTEKTlnnlqpVSRLVERVt 7731
Cdd:TIGR02169 752 --------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEE------VSRIEARL- 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7732 sqiedhRDLQKDISKHREAMVALEKMGTHLkyfsqKQDVVLIKNLLSSIQHRWEKIVSRSAERTRHLERGYKEAKQFNDT 7811
Cdd:TIGR02169 815 ------REIEQKLNRLTLEKEYLEKEIQEL-----QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7812 WKDLITWLIEAEKTLEtetSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKA-----GRLLKERCPSDDVPTIQAML 7886
Cdd:TIGR02169 884 LGDLKKERDELEAQLR---ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAEL 960
|
...
gi 1397727998 7887 TEL 7889
Cdd:TIGR02169 961 QRV 963
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7807-7909 |
8.47e-10 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 59.64 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7807 QFNDTWKDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQAML 7886
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727998 7887 TELKSHWNNVCSKSVDRQRKLEE 7909
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
6622-7396 |
9.67e-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: 66.30 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6622 LAETEELVAMQKApSPEQRVVRAQ--LQEQKLVQKMVTD-RTPSMKAVQDSGNQLITGLDPAE--RKHIESELQQLNSRW 6696
Cdd:pfam15921 94 LNESNELHEKQKF-YLRQSVIDLQtkLQEMQMERDAMADiRRRESQSQEDLRNQLQNTVHELEaaKCLKEDMLEDSNTQI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6697 EALTKRVVDRTAILEEVQGLAGEFQD--------------------------VLDPLTTWLDAANKRFTALEPH-----S 6745
Cdd:pfam15921 173 EQLRKMMLSHEGVLQEIRSILVDFEEasgkkiyehdsmstmhfrslgsaiskILRELDTEISYLKGRIFPVEDQlealkS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6746 PDAEGIEHLIQELK-KLQKEVNEHEPAMKQLAtagKKLQDYCKGEDVIMIQLKIDGVQKQNGE---LR--SHIEDCLEQM 6819
Cdd:pfam15921 253 ESQNKIELLLQQHQdRIEQLISEHEVEITGLT---EKASSARSQANSIQSQLEIIQEQARNQNsmyMRqlSDLESTVSQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6820 EEALPLAKHFQEAHAEflswasKVEPELRALELGVPDEETNIEELANQ---LTEEMQPLLDIINSEGAELAEVAPGDAGL 6896
Cdd:pfam15921 330 RSELREAKRMYEDKIE------ELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6897 RVEDIINrdNKRFDNLRDQIEKRAQKVQlarqRSSEVVNELgdlvdwfvdaDSRLQNQqpiasdldlLQQQLAEQKVMNE 6976
Cdd:pfam15921 404 WDRDTGN--SITIDHLRRELDDRNMEVQ----RLEALLKAM----------KSECQGQ---------MERQMAAIQGKNE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6977 EInnQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAvpfarhfheaHTELVVWLDDV 7056
Cdd:pfam15921 459 SL--EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT----------NAEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7057 EPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKG-------AEQVQSMLDDDNRRMDN 7129
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGrtagamqVEKAQLEKEINDRRLEL 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7130 VRTKVRDrsnsidqamqqsaeftdklenmldtltvtaeqvrsaepisaqpDKLREQIEENKAMEEDLEmrhnaLESVK-- 7207
Cdd:pfam15921 607 QEFKILK-------------------------------------------DKKDAKIRELEARVSDLE-----LEKVKlv 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7208 NAAEELLRQAGD---EQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSV 7284
Cdd:pfam15921 639 NAGSERLRAVKDikqERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7285 DqpALEPEAIR---EQQEELEALKEDIEASQADFEEVQQTGDTllgmvGTTEQPEVQKNVDDAGASLAAISDQYSKRSQE 7361
Cdd:pfam15921 719 E--GSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTN-----ANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
810 820 830
....*....|....*....|....*....|....*
gi 1397727998 7362 LESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPV 7396
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDI 826
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7130-7364 |
1.03e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7130 VRTKVRDRSNSIDQAMQQSAEFTDkLENMLDTLTVTAEQVRSAEPISAQPDK---LREQIEENKAMEEDL-----EMRHN 7201
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALrlwfaQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7202 ALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwdELHALNSSLKDLQEAL 7281
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---ELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7282 SSVD-QPALEPEAIREQQEELEALKEDIEASQAdfeevqqtgdtllgmvgtteqpEVQKNVDDAGASLAAISDQYSKRSQ 7360
Cdd:COG4913 369 AALGlPLPASAEEFAALRAEAAALLEALEEELE----------------------ALEEALAEAEAALRDLRRELRELEA 426
|
....
gi 1397727998 7361 ELES 7364
Cdd:COG4913 427 EIAS 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
5806-6647 |
1.14e-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: 65.91 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5806 PGEEMLQQQLQELddkwhglralsEQQRKGLEDMVSDLRDMreHEQQlTLWLAQKDRMLDV-LGPVAMEPNMLASQMEQV 5884
Cdd:pfam15921 71 PGKEHIERVLEEY-----------SHQVKDLQRRLNESNEL--HEKQ-KFYLRQSVIDLQTkLQEMQMERDAMADIRRRE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5885 KVLREELSAQEPTYDHFLNCAHGILERCGDKSQDGIAVSRRL-----DTVSKAWNKLQSRLNERSKNLSSVEGIS-VEFA 5958
Cdd:pfam15921 137 SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlsheGVLQEIRSILVDFEEASGKKIYEHDSMStMHFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5959 SLTRGLADWLSDFSDKLDG-QGKVSSQPDkQHKQLQELKQLESELIVQQprlarARDLCRQLCdkAKDASTKTDLRSKLT 6037
Cdd:pfam15921 217 SLGSAISKILRELDTEISYlKGRIFPVED-QLEALKSESQNKIELLLQQ-----HQDRIEQLI--SEHEVEITGLTEKAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6038 ALEKDMNDTTRKLEICKaavEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDldilreqmrQNRTLQQELSLKEP 6117
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED---------KIEELEKQLVLANS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6118 EIRQLLEKGDKLVKESSpttevrAIADKVGELQGEWTRLQQEVTV---QDSRL---TMAGSHAQQFTER-LDKMAMWLQM 6190
Cdd:pfam15921 357 ELTEARTERDQFSQESG------NLDDQLQKLLADLHKREKELSLekeQNKRLwdrDTGNSITIDHLRReLDDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6191 TEEKLEKMKPEDvdQNTVVHKLKELQGvQNEMMKKShdrerlnsegTSLVECVDSGKEAIKQQVavinERWDAVNKALSE 6270
Cdd:pfam15921 431 LEALLKAMKSEC--QGQMERQMAAIQG-KNESLEKV----------SSLTAQLESTKEMLRKVV----EELTAKKMTLES 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6271 RASHLEDLGQRLGEVQDSLAEATSALNKWENKLavhnslGLSAKDPKHINRIKDlledtgwlasQLNNTETMLNSIEVDG 6350
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRV------DLKLQELQHLKNEGD----------HLRNVQTECEALKLQM 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6351 GETSNLrdeLNKLRGQHQTLqgelSELVAE--METGAQIVEQFQgLLKIVGGQFLELESelgSKTPVSRDDA---ELGSQ 6425
Cdd:pfam15921 558 AEKDKV---IEILRQQIENM----TQLVGQhgRTAGAMQVEKAQ-LEKEINDRRLELQE---FKILKDKKDAkirELEAR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6426 LADMKDFLTRL----GEKVETLKDLEQQASSLCNAGYVSdpellKSQVEALSNQHASLTE--RATQRQSDVVANQHSIQh 6499
Cdd:pfam15921 627 VSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTS-----RNELNSLSEDYEVLKRnfRNKSEEMETTTNKLKMQ- 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6500 ltqaLNLVWGDIDKASSTLDAMGPAGGNVTTV---------------KALQEELKgFVKSTMEPLQKQF----ESVSRQG 6560
Cdd:pfam15921 701 ----LKSAQSELEQTRNTLKSMEGSDGHAMKVamgmqkqitakrgqiDALQSKIQ-FLEEAMTNANKEKhflkEEKNKLS 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6561 QALIKTAVAGSNTTGletDLESLAERWAGLVEKVAEHEKNLDSALLRtgkfqdamaslldwLAETEELVAMQkapspEQR 6640
Cdd:pfam15921 776 QELSTVATEKNKMAG---ELEVLRSQERRLKEKVANMEVALDKASLQ--------------FAECQDIIQRQ-----EQE 833
|
....*..
gi 1397727998 6641 VVRAQLQ 6647
Cdd:pfam15921 834 SVRLKLQ 840
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7480-7581 |
1.28e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 58.88 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7480 QFDHAHKELKNWMDLVDVTLDEiTPVYGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMtSEGIAQAQGLKTKM 7559
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7560 EDMEKTWENIQAKSRAKQDMLE 7581
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6094-6918 |
2.24e-09 |
|
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: 65.09 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6094 DLDILREQMrqnrtlqQELSLKEPEIRQLLekgDKLVKESSPTTEVRAIADKVGELQG-----EWTRLQQEVTVQDSRLT 6168
Cdd:TIGR02169 178 ELEEVEENI-------ERLDLIIDEKRQQL---ERLRREREKAERYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6169 MAGSHAQQFTERLDKMAMWLQMTEEKLEK-----MKPEDVDQNTVVHKLKELQG----------VQNEMMKKSHDRERln 6233
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRVKEKIGELEAeiaslersiaEKERELEDAEERLA-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6234 sEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAvhnslGLSA 6313
Cdd:TIGR02169 326 -KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-----KLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6314 KDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEVD----GGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVE 6389
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6390 QFQGLLKIVGGQFLELESELGSKTPVSRDDA----ELGSQLADMKDFLTRLGE-KVETLKDLEQQASSLCNAGYVSDPEL 6464
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGRaveeVLKASIQGVHGTVAQLGSvGERYATAIEVAAGNRLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6465 LKSQVEALSNQHAS------LTE-RATQRQSDVVANQHSIQHltqALNLVwgDIDkasstlDAMGPAggnvtTVKALQEE 6537
Cdd:TIGR02169 560 AKEAIELLKRRKAGratflpLNKmRDERRDLSILSEDGVIGF---AVDLV--EFD------PKYEPA-----FKYVFGDT 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6538 LkgfVKSTME---PLQKQFESVSRQGQALIKTAV----------AGSNTTGLETDLESLAER-------WAGLVEKVAEH 6597
Cdd:TIGR02169 624 L---VVEDIEaarRLMGKYRMVTLEGELFEKSGAmtggsraprgGILFSRSEPAELQRLRERleglkreLSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6598 EKNLDSAllrTGKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQ-----------EQKLVQKMVTDRTPSMKAV 6666
Cdd:TIGR02169 701 ENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeienvksELKELEARIEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6667 QDSGNQLITGLDPAERKHIESELQQLN---SRWEAltkRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEp 6743
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEeevSRIEA---RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6744 hspdaEGIEHLIQELKKLQKEVNEHEPAMKQLataGKKLQDyckgedvimIQLKIDGVQKQNGELRSHIEDCLEQMEEAL 6823
Cdd:TIGR02169 854 -----KEIENLNGKKEELEEELEELEAALRDL---ESRLGD---------LKKERDELEAQLRELERKIEELEAQIEKKR 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6824 PLAKHFQEAHAEFLSWASKVEPELRALElGVPDEETNIEELANQ---LTEEMQPLLDIINSEGAELAEVApgdaglrved 6900
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAElqrVEEEIRALEPVNMLAIQEYEEVL---------- 985
|
890
....*....|....*...
gi 1397727998 6901 iinrdnKRFDNLRDQIEK 6918
Cdd:TIGR02169 986 ------KRLDELKEKRAK 997
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6749-7473 |
2.69e-09 |
|
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: 64.70 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6749 EGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAlplAKH 6828
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKIGELEAEIASLERSIAEKERELEDA---EER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6829 FQEAHAEFlswaSKVEPELRALElgvpdeeTNIEELA---NQLTEEMQPLLDIINSEGAELAEVAPGDAGLRVE-----D 6900
Cdd:TIGR02169 324 LAKLEAEI----DKLLAEIEELE-------REIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDElkdyrE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6901 IINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRL-----------QNQQPIASDLDLLQQQL- 6968
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKedkaleikkqeWKLEQLAADLSKYEQELy 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6969 ---AEQKVMNEEINnQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVS--GSANER-QSLLEQAVPFARHF 7042
Cdd:TIGR02169 473 dlkEEYDRVEKELS-KLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAqlGSVGERyATAIEVAAGNRLNN 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7043 HEAHTELV------------------VWLDDVEPVLSELDVLSVDA------DQVKKQQEKAKVLKQ-----------EV 7087
Cdd:TIGR02169 552 VVVEDDAVakeaiellkrrkagratfLPLNKMRDERRDLSILSEDGvigfavDLVEFDPKYEPAFKYvfgdtlvvediEA 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7088 ADRKPIVDRL------------NKTGTALVAMCGS----KGAEQVQSM------LDDDNRRMDNVRTKVRDRSNSIDQAM 7145
Cdd:TIGR02169 632 ARRLMGKYRMvtlegelfeksgAMTGGSRAPRGGIlfsrSEPAELQRLrerlegLKRELSSLQSELRRIENRLDELSQEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7146 QQSAEFTDKLENMLDTLTVTAEQVRS-AEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDE-QDE 7223
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHS 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7224 AVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQP---------ALEPE-- 7292
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlngkkeELEEEle 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7293 ----AIREQQEELEALKEDIEASQADFEEVQQTGDTLlgmvgTTEQPEVQKNVDDAGASLAAISDQYSkrsqELESALAQ 7368
Cdd:TIGR02169 872 eleaALRDLESRLGDLKKERDELEAQLRELERKIEEL-----EAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGE 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7369 AVHFQDQLM---KLLVWLQEAEDEFSEFEPV----ASEFETIKKQWDELKNFKTRVEPKNVEIEslnqhvtELTKSSTPE 7441
Cdd:TIGR02169 943 DEEIPEEELsleDVQAELQRVEEEIRALEPVnmlaIQEYEEVLKRLDELKEKRAKLEEERKAIL-------ERIEEYEKK 1015
|
810 820 830
....*....|....*....|....*....|..
gi 1397727998 7442 QASVLREPMTQLNIRWNNLLTNIGDRQRELQM 7473
Cdd:TIGR02169 1016 KREVFMEAFEAINENFNEIFAELSGGTGELIL 1047
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
5733-5838 |
3.27e-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: 58.10 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5733 IRTFMQDMQDILQWLDLKDHETDSaQPLPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQ 5812
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1397727998 5813 QQLQELDDKWHGLRALSEQQRKGLED 5838
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5416-6217 |
3.36e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5416 ELDIARAVeQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEKLEQTNLwvhdgilqldskelsklssddmkqqlek 5495
Cdd:TIGR02168 224 ELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL---------------------------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5496 larEKHNRLRTIQEIQvaaeqllqdprtGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWL 5575
Cdd:TIGR02168 275 ---EVSELEEEIEELQ------------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5576 SQMEARLDEFQPVaidvgiVEQQKMELQPMLQEYEDYAPKIDEVNDLGNAYEAMINPGDRPISPIR-RIGRsrrlpgiLS 5654
Cdd:TIGR02168 340 AELEEKLEELKEE------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNnEIER-------LE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5655 PRLRSpsptfptspSTQRASPLssessgVSSRKSSADNLLLDDLSEVQQQLLDITQRYEIVGERLADRQQELQLMLTSIR 5734
Cdd:TIGR02168 407 ARLER---------LEDRRERL------QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5735 TFMQDMQDILQWLDLKDHETDSAQPLPTNEKDAKKRLKEhevfhrEILSKEGLvEDIRKKAQDLLKTRHG-------VPG 5807
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA------LLKNQSGL-SGILGVLSELISVDEGyeaaieaALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5808 EEM-------LQQQLQELD-DKWH----------------GLRALSEQQRKGLEDMVSDLRDMREHEQQLTLWLAqkdrm 5863
Cdd:TIGR02168 545 GRLqavvvenLNAAKKAIAfLKQNelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS----- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5864 lDVLGPVAMEPNmLASQMEQVKVLREELSAQepTYDHFLNCAHGILERCGDKSQDGI-AVSRRLDTVSKAWNKLQSRLNE 5942
Cdd:TIGR02168 620 -YLLGGVLVVDD-LDNALELAKKLRPGYRIV--TLDGDLVRPGGVITGGSAKTNSSIlERRREIEELEEKIEELEEKIAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5943 RSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGQ-----------GKVSSQPDKQHKQLQELKQ----LESELIVQQP 6007
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarleaevEQLEERIAQLSKELTELEAeieeLEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6008 RLARARDLCRQLCDKAKDAST-KTDLRSKLTALEKDMNDTTRKLeickAAVEEASQQAEKFEADCKELLTWISEAANNLQ 6086
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEeLKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6087 ES-EPLSSDLDILREQMRQ-NRTLQQELSLKEPEIRQLLEKGDKLVKESsptTEVRAIADKVGELQGEWTRLQQEVTVQD 6164
Cdd:TIGR02168 852 EDiESLAAEIEELEELIEElESELEALLNERASLEEALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLE 928
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 6165 SRLTMAGSHAQQFTERLdkmAMWLQMTEEKLEKMKPEDVDQNTVVH-KLKELQG 6217
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARrRLKRLEN 979
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5351-5449 |
5.71e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5351 QAMNELVSWMDSAEQVVTTQlPISLRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELVKTCELDiARAVEQRLTSL 5430
Cdd:smart00150 5 RDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEEL 82
|
90
....*....|....*....
gi 1397727998 5431 DEKFSSLQAKCRQRDRDLE 5449
Cdd:smart00150 83 NERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7916-8016 |
7.06e-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: 56.94 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7916 QFTEALDALLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 7995
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|.
gi 1397727998 7996 ELNAAWDRVCKLSVSKQDRLE 8016
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLE 104
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
178-283 |
7.81e-09 |
|
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: 57.39 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....*..
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSlydvFPQ 283
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQ----FPK 110
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6610-6712 |
8.02e-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: 56.94 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 KFQDAMASLLDWLAETEELVAMQKAPSPEQRVvRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAErKHIESEL 6689
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGKDLESV-QALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727998 6690 QQLNSRWEALTKRVVDRTAILEE 6712
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6801-7452 |
8.28e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6801 VQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFLSWASKVEPELRALElgvpdeetniEELAN--QLTEEMQPLLDI 6878
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR----------EELEKleKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6879 INSEGAELAEVApGDAGLRVEDIINRDnKRFDNLRDQIEKRAQKVQLAR--QRSSEVVNELGDLVDWFVDADSRLQNQqp 6956
Cdd:PRK03918 240 IEELEKELESLE-GSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKR-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6957 iasdLDLLQQQLAEQKVMNEEINNQKVKARDTlsasKKLLSDsamednsaIRNKMDELKQWVDTVsgsaNERQSLLEQAV 7036
Cdd:PRK03918 316 ----LSRLEEEINGIEERIKELEEKEERLEEL----KKKLKE--------LEKRLEELEERHELY----EEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7037 PF-ARHFHEAHTELVVWLDDVEPVLSELDvlsvdaDQVKKQQEKAKVLKQEVADRKPIVDRLNKT-GTALVamCGSKGAE 7114
Cdd:PRK03918 376 RLkKRLTGLTPEKLEKELEELEKAKEEIE------EEISKITARIGELKKEIKELKKAIEELKKAkGKCPV--CGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7115 QVQ-SMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENM--LDTLTVTAEQVRSAEpisaqpDKLR----EQIE 7187
Cdd:PRK03918 448 EHRkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELE------EKLKkynlEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7188 ENKAMEEDLEMRHNALES-VKNAAEELLRQAGDEQDEAV--KDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFW 7264
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGeIKSLKKELEKLEELKKKLAEleKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7265 DELHALNSSLKDLQEalssvdqpalEPEAIREQQEELEALKEDIEASQADFEEVQQtgdtllgmvgttEQPEVQKNVDDa 7344
Cdd:PRK03918 602 NEYLELKDAEKELER----------EEKELKKLEEELDKAFEELAETEKRLEELRK------------ELEELEKKYSE- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7345 gASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRV-EPKNVE 7423
Cdd:PRK03918 659 -EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVkKYKALL 737
|
650 660
....*....|....*....|....*....
gi 1397727998 7424 IESLNQHVTELtksstpeqASVLREPMTQ 7452
Cdd:PRK03918 738 KERALSKVGEI--------ASEIFEELTE 758
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6030-6486 |
1.04e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6030 TDLRSKLTALEKDMNDTTRKLEICkaavEEASQQAEKFEADCKELLTwisEAANNLQESEPLSSDLDILREQM----RQN 6105
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERY----EEQREQARETRDEADEVLE---EHEERREELETLEAEIEDLRETIaeteRER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6106 RTLQQELSLKEPEIRQLLEKGDKLVKESSPTT-EVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKM 6184
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6185 amwlqmtEEKLEKMKPEdvdqntvvhklkelqgvqnemmkkshdRERLNSEGTSLVECVDSGK---EAIKQQVAVINERW 6261
Cdd:PRK02224 355 -------EERAEELREE---------------------------AAELESELEEAREAVEDRReeiEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6262 DAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNSL---------GLSAKDPKHINRIKDLLEDTGWL 6332
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecGQPVEGSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6333 ASQLNNTETMLNSIE--VDGGET-SNLRDELNKLRGQHQTLQgelsELVAEMETGA-QIVEQFQGLLKIVGgqflELESE 6408
Cdd:PRK02224 481 EAELEDLEEEVEEVEerLERAEDlVEAEDRIERLEERREDLE----ELIAERRETIeEKRERAEELRERAA----ELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6409 LGSKtpvsRDDAELGSQLAD-----MKDFLTRLGEKVETLKDLEQQASSLcnagyvSDPELLKSQVEALSNQHASLTERA 6483
Cdd:PRK02224 553 AEEK----REAAAEAEEEAEeareeVAELNSKLAELKERIESLERIRTLL------AAIADAEDEIERLREKREALAELN 622
|
...
gi 1397727998 6484 TQR 6486
Cdd:PRK02224 623 DER 625
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
648-747 |
1.84e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 55.80 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 648 EFLQGATAELTWLAEREEVeVTRDWVSKDL-NLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVLMA 726
Cdd:smart00150 2 QFLRDADELEAWLEEKEQL-LASEDLGKDLeSVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727998 727 SLQARWSWLLQLVTCLDAHLK 747
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
8020-8124 |
2.27e-08 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 55.40 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8020 RLAEEFHKKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEANLRETLNIGQDIMKRCHPDSvPIM 8099
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEI 78
|
90 100
....*....|....*....|....*
gi 1397727998 8100 KQWLSVIRARWEELTALGRQRSARL 8124
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKL 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6780-7411 |
2.85e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6780 KKLQDYCKGEDVI----MIQLKIDGVQKQNGELRSHIEdcleQMEEALPLAKHFQ------EAHAEFLSWASKVEPELRA 6849
Cdd:PTZ00121 1030 EELTEYGNNDDVLkekdIIDEDIDGNHEGKAEAKAHVG----QDEGLKPSYKDFDfdakedNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6850 LELGVPDEETNIEElANQLTEEMQPLLDIINSEGAELAEVA-------PGDAGLRVEDI----INR---DNKRFDNLRDQ 6915
Cdd:PTZ00121 1106 TETGKAEEARKAEE-AKKKAEDARKAEEARKAEDARKAEEArkaedakRVEIARKAEDArkaeEARkaeDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6916 IE-KRAQKVQLARQ-RSSEVVNELGDLVDwfVDADSRLQNQQPIAS--DLDLLQQQLAEQKVMNEEINNQKVKARDTLSA 6991
Cdd:PTZ00121 1185 EEvRKAEELRKAEDaRKAEAARKAEEERK--AEEARKAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6992 SKKLLSDSAMEDNSAirNKMDELKQwVDTVSGSANERQSLLEQAVPFARHFHEAHTELVVWLDDVEPVLSELDVLSVDA- 7070
Cdd:PTZ00121 1263 AHFARRQAAIKAEEA--RKADELKK-AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAe 1339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7071 -----DQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVqsmldddnRRMDNVRTKVRDRSNSIDQAM 7145
Cdd:PTZ00121 1340 eakkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK--------KKADEAKKKAEEDKKKADELK 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7146 QQSAEftdklENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDL---EMRHNALESVKnaAEELLRQAgdEQD 7222
Cdd:PTZ00121 1412 KAAAA-----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeEAKKKAEEAKK--ADEAKKKA--EEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7223 EAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQ----------------EALSSVDQ 7286
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadelkkaEELKKAEE 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7287 PALEPEAIREQQEELEALKEDIEASQAdfEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAI--SDQYSKRSQELES 7364
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKK 1640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1397727998 7365 ALAQAVHFQDQLMKllvwlqEAEDEFSEFEPVASEFETIKKQWDELK 7411
Cdd:PTZ00121 1641 KEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6347-6851 |
3.75e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6347 EVDGGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELEsELGSKTPVSRDD-AELGSQ 6425
Cdd:PRK02224 195 QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-TLEAEIEDLRETiAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6426 LADMKDfltRLGEKVETLKDLEQQASSLcnagyVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQ-HLTQAL 6504
Cdd:PRK02224 274 REELAE---EVRDLRERLEELEEERDDL-----LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6505 NLVWGDIDKASSTLDAMGPAGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRqgqaliktAVAGSNTT--GLETDLES 6582
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRE--------RFGDAPVDlgNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6583 LAERWAGLVEKVAEHEKNLDSALLRtgkfqdamaslldwLAETEELVAMQKAPSPEQRV-----VRAQLQEQKLVQKMVT 6657
Cdd:PRK02224 417 LREERDELREREAELEATLRTARER--------------VEEAEALLEAGKCPECGQPVegsphVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6658 DRTpSMKAVQDSGNQLITGLDPAerKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTwlDAANKR 6737
Cdd:PRK02224 483 ELE-DLEEEVEEVEERLERAEDL--VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA--EAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6738 FTALEPHSpDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYckGEDVIMIQLKIDGVQKQNGELRSHIEDCLE 6817
Cdd:PRK02224 558 EAAAEAEE-EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA--EDEIERLREKREALAELNDERRERLAEKRE 634
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1397727998 6818 QMEEalpLAKHFQEA--------HAEFLSWASKVEPELRALE 6851
Cdd:PRK02224 635 RKRE---LEAEFDEArieearedKERAEEYLEQVEEKLDELR 673
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6175-6276 |
5.80e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 54.26 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6175 QQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQV 6254
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 6255 AVINERWDAVNKALSERASHLE 6276
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6354-6944 |
7.96e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6354 SNLRDELNKLRGQHQTLQgELSELVAEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTpVSRDDAELGSQLADMKDFL 6433
Cdd:COG4913 238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-LEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6434 TRLGEKVETLKDLEQQASslcNAGYvSDPELLKSQVEALSNQHASLTERATQRQ--------------SDVVANQHSIQH 6499
Cdd:COG4913 316 ARLDALREELDELEAQIR---GNGG-DRLEQLEREIERLERELEERERRRARLEallaalglplpasaEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6500 LTQALNLVWGDIDKASSTLDAmgpaggnvtTVKALQEELkgfvkstmEPLQKQFESVSRQG------QALIKTAVAGSnt 6573
Cdd:COG4913 392 LLEALEEELEALEEALAEAEA---------ALRDLRREL--------RELEAEIASLERRKsniparLLALRDALAEA-- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6574 TGL-ETDLESLAE---------RWAGLVEKVaeheknldsalLRTGKF-----QDAMASLLDWLAET--EELVAMQKAPS 6636
Cdd:COG4913 453 LGLdEAELPFVGElievrpeeeRWRGAIERV-----------LGGFALtllvpPEHYAAALRWVNRLhlRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6637 PEQRVVRAQLQEQKLVQKMVTDRTP-------SM-------------------KAVQDSG------------------NQ 6672
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLDFKPHPfrawleaELgrrfdyvcvdspeelrrhpRAITRAGqvkgngtrhekddrrrirSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6673 LITGLDPAER-KHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAAnkrftalephsPDAEGI 6751
Cdd:COG4913 602 YVLGFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----------SAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6752 EHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgedvimIQLKIDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQE 6831
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEE---------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6832 AHAEFLSW----------ASKVEPELRA-LELGVPDEETNIEELANQLTEEMQpllDIINSEGAELAEVAPGDAGLRved 6900
Cdd:COG4913 742 LARLELRAlleerfaaalGDAVERELREnLEERIDALRARLNRAEEELERAMR---AFNREWPAETADLDADLESLP--- 815
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1397727998 6901 iinrdnkRFDNLRDQIEKR---AQKVQLARQRSSEVVNELGDLVDWF 6944
Cdd:COG4913 816 -------EYLALLDRLEEDglpEYEERFKELLNENSIEFVADLLSKL 855
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
418-645 |
1.85e-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: 55.91 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 418 AEKIQRESKQAGESLHDLERQIQEAEVRGDKQHPYEAKHNCDAMDRALHTIEENLRAMFRDVQTLQDNHFPQSQQLYTRI 497
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 498 SELQSRVSSLRTRLysgvvqpllsrayveegrtVTRRTEIMTEVRLVDTnpaFRHVQDCLDWIEAQQQMIVGQDYSSDLQ 577
Cdd:cd00176 82 EELNQRWEELRELA-------------------EERRQRLEEALDLQQF---FRDADDLEQWLEEKEAALASEDLGKDLE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 578 QVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAEEQ----KLYTQKLSSVEVAYSLLLNTSSRRLKFLES 645
Cdd:cd00176 140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHpdadEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7699-7800 |
2.32e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 52.71 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7699 FHGELNKFISWLTDTEKTLNNlQPVSRLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKYfSQKQDVVLIKNLLS 7778
Cdd:pfam00435 6 FFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQERLE 83
|
90 100
....*....|....*....|..
gi 1397727998 7779 SIQHRWEKIVSRSAERTRHLER 7800
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLEE 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
5809-6437 |
2.45e-07 |
|
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: 58.44 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5809 EMLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEQQLTLWLAQKDRMLD-------VLGPVAMEPNMLASQM 5881
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqlkkqqLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5882 EQVKVLREELSAQEPTYDHFLNCAHgiLERCGDKSQDGIAvsrrldtvskawnKLQSRLNERSKNLSSVEGISVEFASLT 5961
Cdd:TIGR00618 277 AVLEETQERINRARKAAPLAAHIKA--VTQIEQQAQRIHT-------------ELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5962 ---RGLADWLSD---FSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKT----D 6031
Cdd:TIGR00618 342 eqrRLLQTLHSQeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsafrD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6032 LRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNL--------QESEPLSSDLDILREQMR 6103
Cdd:TIGR00618 422 LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkeqihlQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6104 QNRTLQQELSLKEPEIRQL------------LEKGDKLVKESSPTT--EVRAIADKVGELQGEWTRLQQE---VTVQDSR 6166
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDIdnpgpltrrmqrGEQTYAQLETSEEDVyhQLTSERKQRASLKEQMQEIQQSfsiLTQCDNR 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6167 LTMAGSHAQQFTERLDKmamWLQMtEEKLEKMKPEDVDQntvvhKLKELQGVQNEMMKKSHDR---ERLNSEGTSLV--- 6240
Cdd:TIGR00618 582 SKEDIPNLQNITVRLQD---LTEK-LSEAEDMLACEQHA-----LLRKLQPEQDLQDVRLHLQqcsQELALKLTALHalq 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6241 -----ECVDSGKEAIKQQVAVINERWDAVNKALSERASHL----EDLGQ---RLGEVQDSLAEATSALNKWENKLAVHNS 6308
Cdd:TIGR00618 653 ltltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAQcqtLLRELETHIEEYDREFNEIENASSSLGS 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6309 lGLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEV----DGGETSNLRDELNKLRGQHQTLQGELSELVAEM--- 6381
Cdd:TIGR00618 733 -DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTaalqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgqe 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6382 ------------ETGAQIVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGSQLADMKDFLTRLG 6437
Cdd:TIGR00618 812 ipsdedilnlqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5095-5343 |
2.61e-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: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5095 ELAKFEEESKKFRTWMGAAFSELTnQEDYLKRFEDLKVLGEKHRELASDISSHQAdhrfmsmAVQKYMEEAKlyklemds 5174
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEE-------RVEALNELGE-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5175 fradrarparhSLISMECVAADNVKDKLTDLTEEYHDLSNRCNLLGDRLADLSGKHRQFNDvAFKLLTWLTDMEGQLSSv 5254
Cdd:cd00176 65 -----------QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5255 kQDAGlSEPQQLQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNSLSGQAAEQqqvakLQSTMNDLSVRYSTLTKDINS 5334
Cdd:cd00176 132 -EDLG-KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-----IEEKLEELNERWEELLELAEE 204
|
....*....
gi 1397727998 5335 HVTQLQAAV 5343
Cdd:cd00176 205 RQKKLEEAL 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7209-7636 |
2.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7209 AAEELLRQAGDEQDEaVKDVRQKLEELTKLYKDIQERGRGRQRALE--ETLAVAEKFWDELHALNSSLKDLQEALssvdq 7286
Cdd:COG4717 75 ELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERL----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7287 palepEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAIsdqyskrsQELESAL 7366
Cdd:COG4717 149 -----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL--------AELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7367 AQAvhfQDQLMKllvwLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRvepknVEIESLNQHVTELTKSSTPEQASVL 7446
Cdd:COG4717 216 EEA---QEELEE----LEEELEQLENELEAAALEERLKEARLLLLIAAAL-----LALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7447 REPMTQLNIRWNNLLtnigDRQRELQMALLTAGQFDHAHKELKNWMDLVDVtLDEITPVYGDPKLVEIELAKLRIVQNDI 7526
Cdd:COG4717 284 GLLALLFLLLAREKA----SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7527 TAHQESVESISKEAQRLMTSEGIAQAQGLKTKMEDMEKtWENIQAKSRAKQDMLE--DGLREAQGFTGELQDILAKINDI 7604
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEelLGELEELLEALDEEELEEELEEL 437
|
410 420 430
....*....|....*....|....*....|..
gi 1397727998 7605 EGQLiiskpvgglpETAKEQLEKFMDVYAELE 7636
Cdd:COG4717 438 EEEL----------EELEEELEELREELAELE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7113-7369 |
2.92e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7113 AEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEP----ISAQPDKLREQIEE 7188
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErleeLEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7189 NKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELH 7268
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7269 ALNSSLKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTgdtllgmvGTTEQPEVQKNVDDAGASL 7348
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE--------LLEEAALLEAALAELLEEL 486
|
250 260
....*....|....*....|.
gi 1397727998 7349 AAISDQYSKRSQELESALAQA 7369
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFL 507
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7585-7691 |
4.87e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 51.94 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7585 REAQGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLgGKSKGPALANL 7664
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1397727998 7665 RQNLQHLNQRCDYIRSRACDRKKKLED 7691
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6681-7637 |
5.33e-07 |
|
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: 57.37 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6681 ERKHiESElQQLNSRWEALtKRVVDrtaILEEVQG----------LAGEFQDVLDPLTTW-LDAANKRFTALEphspdaE 6749
Cdd:TIGR02168 172 ERRK-ETE-RKLERTRENL-DRLED---ILNELERqlkslerqaeKAERYKELKAELRELeLALLVLRLEELR------E 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6750 GIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYcKGEDvimiQLKIDGVQKQNGELRSHIEDcLEQMEEalplakHF 6829
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLE-VSEL----EEEIEELQKELYALANEISR-LEQQKQ------IL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6830 QEAHAEFLSWASKVEPELRALElgvpDEETNIEELANQLTEEMQPLLDIINSEGAELAEVAPGDAGLrvediinrdNKRF 6909
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL---------ESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6910 DNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQPIASDLD--LLQQQLAEQKVMNEEINNQKVKARD 6987
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6988 TLSASKKLLSdSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARH----FHEAHtelvvWLDDVEPVLSEL 7063
Cdd:TIGR02168 455 ELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkalLKNQS-----GLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7064 dvLSVDAdqvkkQQEKA----------KVLKQEVADRKPIVDRLNKTGTALVAMCgskgAEQVQSMLDDDNRRMdNVRTK 7133
Cdd:TIGR02168 529 --ISVDE-----GYEAAieaalggrlqAVVVENLNAAKKAIAFLKQNELGRVTFL----PLDSIKGTEIQGNDR-EILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7134 VRDRSNSIDQAMQQSAEFTDKLENMLDTLTVtAEQVRSAEpisaqpdklreqieeNKAMEEDLEMRHNALESVKNAAEEL 7213
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLLGGVLV-VDDLDNAL---------------ELAKKLRPGYRIVTLDGDLVRPGGV 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7214 LRQAGDEQDEAVKDVRQKLEELTKlykdiqergrgRQRALEETLAVAEKfwdelhALNSSLKDLQEALSSVDQPALEPEA 7293
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEE-----------KIEELEEKIAELEK------ALAELRKELEELEEELEQLRKELEE 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7294 IREQQEELEALKEDIEAsqadfeEVQQtgdtllgmvgtteqpevqknvddagaslaaISDQYSKRSQELESALAQAVHFQ 7373
Cdd:TIGR02168 724 LSRQISALRKDLARLEA------EVEQ------------------------------LEERIAQLSKELTELEAEIEELE 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7374 DQLMKLLVWLQEAEDEFSEFEpvasefETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELT--KSSTPEQASVLREPMT 7451
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELE------AQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATERRLE 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7452 QLNIRWnnlltnigdRQRELQMALLTAGQFD------HAHKELKNWMDLVDVtldeitpvygdpklVEIELAKLRIVQND 7525
Cdd:TIGR02168 842 DLEEQI---------EELSEDIESLAAEIEEleelieELESELEALLNERAS--------------LEEALALLRSELEE 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7526 ITAHQESVESISKEAQRLMTSEGIAQAQgLKTKMEDMEKTWENIQAKSRAK-QDMLEDGLREAQGFTGELQDILAKINDI 7604
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQ-LELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRL 977
|
970 980 990
....*....|....*....|....*....|...
gi 1397727998 7605 EGQLiisKPVGGLPETAKEQLEKFMDVYAELEK 7637
Cdd:TIGR02168 978 ENKI---KELGPVNLAAIEEYEELKERYDFLTA 1007
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
4974-5631 |
5.40e-07 |
|
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: 57.04 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 4974 PFVGRLADSFDSIVQELMTEQEhLGDLEQILKHDSQMGDEASKVK---LQLEAHKSTHEKIQSQQQPILSLVYKAEQLTE 5050
Cdd:pfam05483 48 PMLEQVANSGDCHYQEGLKDSD-FENSEGLSRLYSKLYKEAEKIKkwkVSIEAELKQKENKLQENRKIIEAQRKAIQELQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5051 NYQEELTPEQVTQLTTQASLLKatlekvSKTSERRLSHLTK-----AADELAKFEEESKKFRTwmgaAFSELTNQ-EDYL 5124
Cdd:pfam05483 127 FENEKVSLKLEEEIQENKDLIK------ENNATRHLCNLLKetcarSAEKTKKYEYEREETRQ----VYMDLNNNiEKMI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5125 KRFEDLKVlgekhrelasdisshQADHRFMSMAVQKYMEEAKLYKLEMDSFRADRARPARHSLISMECVAADNVKDKLTD 5204
Cdd:pfam05483 197 LAFEELRV---------------QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5205 LTEEYHDlsnRCNLLGDRLADLSGKHRQFNDVAFKLLTWLTDMEGQLS-SVKQDAGLSEpqQLQVHLDRLKSLSMDALSQ 5283
Cdd:pfam05483 262 LLEESRD---KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrSMSTQKALEE--DLQIATKTICQLTEEKEAQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5284 kllLDEMQKrgqdltnslsGQAAEQQQVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAAVTHSQDITQAMNELVSWMDSA 5363
Cdd:pfam05483 337 ---MEELNK----------AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5364 EqvvttqlpislrrpelnAQLQSFSAVDADVTNHQSALDAVKALANELVKTCE--LDIARAVEQRLTSLDEKFSSLQAKC 5441
Cdd:pfam05483 404 E-----------------VELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQelIFLLQAREKEIHDLEIQLTAIKTSE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5442 RQRDRDLEEVDSSLRefQEKLEQTNLWVHDGILQLDSKELSKLSSD---DMKQQLEKLAREKHNRLRTIQEIQVAAEQLL 5518
Cdd:pfam05483 467 EHYLKEVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5519 QdprtgegeavknlvsdLKKNLEAFDSLLAAKENEASDKEQQGAdfENAKTIALLWLSQMEARLDEFQPVAIDVGIVEQQ 5598
Cdd:pfam05483 545 N----------------LRDELESVREEFIQKGDEVKCKLDKSE--ENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
650 660 670
....*....|....*....|....*....|...
gi 1397727998 5599 KMELQPMLQEYEDYAPKIDEVNDLGNAYEAMIN 5631
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7150-7254 |
5.61e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.56 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7150 EFTDKLENMLDTLTvTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLrqagDEQDEAVKDVR 7229
Cdd:smart00150 2 QFLRDADELEAWLE-EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI----EEGHPDAEEIE 76
|
90 100
....*....|....*....|....*
gi 1397727998 7230 QKLEELTKLYKDIQERGRGRQRALE 7254
Cdd:smart00150 77 ERLEELNERWEELKELAEERRQKLE 101
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
178-283 |
5.79e-07 |
|
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: 51.63 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVIT 84
|
90 100
....*....|....*....|....*..
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSlydvFPQ 283
Cdd:cd21313 85 PEEIIHPDVDEHSVMTYLSQ----FPK 107
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
195-275 |
5.88e-07 |
|
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: 52.09 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 195 PGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDVPNPDEKSILTY 273
Cdd:cd21315 30 PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPEEMVNPKVDELSMMTY 109
|
..
gi 1397727998 274 VS 275
Cdd:cd21315 110 LS 111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
6533-7262 |
6.36e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6533 ALQEELKGFVKSTMEPLQ-KQFESVSRQGQALiKTAVAGSNTTGLeTDLESLAERWAglvEKVAEHEKNLDSAL-LRTGK 6610
Cdd:TIGR00606 374 ATRLELDGFERGPFSERQiKNFHTLVIERQED-EAKTAAQLCADL-QSKERLKQEQA---DEIRDEKKGLGRTIeLKKEI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6611 FQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLitGLDPAERKhIESELQ 6690
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRK-LDQEME 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6691 QLNSRWEALTKRVV---DRTAILEEVQGLAGEFQDVLDPLTTwlDAANKRFTALEPHSPDAEgIEHLIQELKKLQKEV-- 6765
Cdd:TIGR00606 526 QLNHHTTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLG--YFPNKKQLEDWLHSKSKE-INQTRDRLAKLNKELas 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6766 ---------NEHEPAMKQLATAGKKLQDYCKGE----DVIMIQLKIDGVQKQNGELR-------SHIEDCLEQMEEALPL 6825
Cdd:TIGR00606 603 leqnknhinNELESKEEQLSSYEDKLFDVCGSQdeesDLERLKEEIEKSSKQRAMLAgatavysQFITQLTDENQSCCPV 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6826 AKHFQEAHAEFLSWASKVEPELRALelgvPDEETNIEELANQLTEEMQPLLDIINSEGAELAEVAPGDAGLRVED-IINR 6904
Cdd:TIGR00606 683 CQRVFQTEAELQEFISDLQSKLRLA----PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNR 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6905 DNKRFDNLRDQIEKRAQKVqLARQRSSEV----VNELGDLVDWFVDADSRLQNQ--QPIASDLDLLQQQLAEQKvmnEEI 6978
Cdd:TIGR00606 759 DIQRLKNDIEEQETLLGTI-MPEEESAKVcltdVTIMERFQMELKDVERKIAQQaaKLQGSDLDRTVQQVNQEK---QEK 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6979 NNQKVKARDTLSASKKLLSDSaMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHTELVVWLDDVEP 7058
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7059 VLSELDvlsvdadqvKKQQEKAKVLKQEVADRKPIVDRLNktgtalvamcgskgaeQVQSMLDDDNRRMDNVRTKVRDRS 7138
Cdd:TIGR00606 914 LETFLE---------KDQQEKEELISSKETSNKKAQDKVN----------------DIKEKVKNIHGYMKDIENKIQDGK 968
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7139 NsiDQAMQQsaeftdklENMLDTLTVTAEQV-RSAEPISAQPDKLREQIEENKAMEEDLE------MRHNALESVKNAAE 7211
Cdd:TIGR00606 969 D--DYLKQK--------ETELNTVNAQLEECeKHQEKINEDMRLMRQDIDTQKIQERWLQdnltlrKRENELKEVEEELK 1038
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 7212 ELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEK 7262
Cdd:TIGR00606 1039 QHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7480-7582 |
1.00e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 50.78 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7480 QFDHAHKELKNWMDLVDVTLDEiTPVYGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMTSEGIAQAQgLKTKM 7559
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-IQERL 82
|
90 100
....*....|....*....|...
gi 1397727998 7560 EDMEKTWENIQAKSRAKQDMLED 7582
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1111-1302 |
1.10e-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: 53.60 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 1111 LDDVKQMIHDYQHTLASQDNAtSDLSSLKLAHTELTDVQTSMKQQQPRIEHLKSDVSSLRVLveksrsgvtSHHDLDAVE 1190
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---------GHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 1191 REVINLASQWATVSSQAAERLQMVRSIQDLLSMYEHGLgAEEQWLEQIQKTVASQPPlTGDVVDAKNQLQTTMAIYNRLV 1270
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|..
gi 1397727998 1271 ERKHQIEAVNRLGGQYIREAKIFEKKQTKYRQ 1302
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
6900-7592 |
1.23e-06 |
|
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: 56.28 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6900 DIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNelgdlvdwfvDADSRLQNQQPIASDLDLLQQQLAEQKVMNEEIN 6979
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLE----------DSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6980 NQKVKARDTLSASKkllsdsamednsaIRNKmdelkqwvdtvsGSAnerqslleqavpFARHFHEAHTELVVWLDDVEPV 7059
Cdd:pfam15921 201 GKKIYEHDSMSTMH-------------FRSL------------GSA------------ISKILRELDTEISYLKGRIFPV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7060 LSELDVLSVDAdqvkkqQEKAKVLKQEVADRkpivdrlnktgtalvamcgskgAEQVQSMLDDDNRRMDNVRTKVRDRSN 7139
Cdd:pfam15921 244 EDQLEALKSES------QNKIELLLQQHQDR----------------------IEQLISEHEVEITGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7140 SI--------DQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPIsaqpdkLREQIEEnkaMEEDLEMRHNALESVKNAAE 7211
Cdd:pfam15921 296 SIqsqleiiqEQARNQNSMYMRQLSDLESTVSQLRSELREAKRM------YEDKIEE---LEKQLVLANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7212 ELLRQAGDEQDEAVK---DVRQKLEELTkLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPA 7288
Cdd:pfam15921 367 QFSQESGNLDDQLQKllaDLHKREKELS-LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7289 LEPE--AIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEvqKNVDDAGASLaaisdqySKRSQELESAL 7366
Cdd:pfam15921 446 MERQmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE--RTVSDLTASL-------QEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7367 AQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDElknfktrvepKNVEIESLNQHVTELTK--SSTPEQAS 7444
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE----------KDKVIEILRQQIENMTQlvGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7445 VLREPMTQLNirwnnllTNIGDRQRELQmalltagqfdhahkELKNWMDLVDVTLDEItpvygDPKLVEIELAKLRIVqN 7524
Cdd:pfam15921 587 AMQVEKAQLE-------KEINDRRLELQ--------------EFKILKDKKDAKIREL-----EARVSDLELEKVKLV-N 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7525 DITAHQESVESISKEAQRL-------------MTSEGIAQAQGLKTKMEDMEKTWENIQAKSRAKQDMLE---DGLREAQ 7588
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLlnevktsrnelnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEqtrNTLKSME 719
|
....
gi 1397727998 7589 GFTG 7592
Cdd:pfam15921 720 GSDG 723
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6686-7213 |
2.16e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6686 ESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEPHSPDAEGIEHLIQELKK----L 6761
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereeL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6762 QKEVNEHEPAMKQLATAGKKLQDYCKGE--DVIMIQLKIDGVQKQNGELRSHIEDC-------LEQMEEALPLAKHFQEA 6832
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDdaDAEAVEARREELEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6833 HAEFLSWASKVEPELRALELGVPDEETNIEELANQLTEemqplldiiNSEGAELAEVAPGDAGLRVEDIinRDNKrfDNL 6912
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEE---------LRERFGDAPVDLGNAEDFLEEL--REER--DEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6913 RDQIEKRAQKVQLARQRSSEVVN--------ELGDLVDWFVDADSRLQNQQPIASdldlLQQQLAEQKVMNEEINNQKVK 6984
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEAlleagkcpECGQPVEGSPHVETIEEDRERVEE----LEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6985 ARDTLSASKKLlsdsamednSAIRNKMDELKQWVDTVSGSANERQSLLEQavpfarhFHEAHTELVVWLDDVEPVLSELd 7064
Cdd:PRK02224 501 AEDLVEAEDRI---------ERLEERREDLEELIAERRETIEEKRERAEE-------LRERAAELEAEAEEKREAAAEA- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7065 vlsvdADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGT--ALVAMCGSK------GAEQVQSMLDDDNRRMDNVRTKVRD 7136
Cdd:PRK02224 564 -----EEEAEEAREEVAELNSKLAELKERIESLERIRTllAAIADAEDEierlreKREALAELNDERRERLAEKRERKRE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7137 RSNSIDQA--------MQQSAEFTDKLENMLDTLTVTAEQVRSAepISAQPDKLrEQIEENKAMEEDLEMRHNALESVKN 7208
Cdd:PRK02224 639 LEAEFDEArieearedKERAEEYLEQVEEKLDELREERDDLQAE--IGAVENEL-EELEELRERREALENRVEALEALYD 715
|
....*
gi 1397727998 7209 AAEEL 7213
Cdd:PRK02224 716 EAEEL 720
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7371-7472 |
3.14e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7371 HFQDQLMKLLVWLQEAEdEFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSStPEQASVLREPM 7450
Cdd:smart00150 2 QFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7451 TQLNIRWNNLLTNIGDRQRELQ 7472
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5285-6156 |
3.39e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5285 LLLDEMQKRGQDLTNSLSGQAAEQQQVAKLQSTMNDLSVRYSTLtkdiNSHVTQLQAAVTHSQDITQAMNELVSWMDSAE 5364
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5365 QVvttqlpISLRRPELNAQLQsfsAVDADVTNHQSALDAVKALANELvktceldiaravEQRLTSLDEKFSSLQAKCRQR 5444
Cdd:TIGR02168 305 QI------LRERLANLERQLE---ELEAQLEELESKLDELAEELAEL------------EEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5445 DRDLEEVDSSLREFQEKLEQTNLWVHDGILQLDS--KELSKLSSDdmKQQLEklarekHNRLRTIQEIqvaaEQLLQDPR 5522
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASlnNEIERLEAR--LERLE------DRRERLQQEI----EELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5523 TGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWLSQMEARLD-------EFQPVAIDVGIV 5595
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslerlqeNLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5596 EQQKMEL---QPMLQEY----EDYAPKIDEVndLGNAYEAMI----NPGDRPISPIR--RIGRSRRLPgilsprLRSPSP 5662
Cdd:TIGR02168 512 LKNQSGLsgiLGVLSELisvdEGYEAAIEAA--LGGRLQAVVvenlNAAKKAIAFLKqnELGRVTFLP------LDSIKG 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5663 TFPTSPSTQRAsplssessGVSSRKSSADNLLLDDLSEVQQQLLDITQRYEIVgERLADRQQELQLMLTSIRTFMQDMQD 5742
Cdd:TIGR02168 584 TEIQGNDREIL--------KNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV-DDLDNALELAKKLRPGYRIVTLDGDL 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5743 IL-QWLDLKDHETDSAQPLPTnekdaKKRLKEHEvfhREILSKEGLVEDIRKKAQDLLKtrhgvpgeemlqqQLQELDDK 5821
Cdd:TIGR02168 655 VRpGGVITGGSAKTNSSILER-----RREIEELE---EKIEELEEKIAELEKALAELRK-------------ELEELEEE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5822 WHGLRALSEQQRKGLEDMVSDLRDMREHEQQLtlwlaqkdrmldvlgpvamepnmlASQMEQVKVLREELSAQEPTYDHF 5901
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQL------------------------EERIAQLSKELTELEAEIEELEER 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5902 LNCAHGILERCGDKSQDgiaVSRRLDTVSKAWNKLQSRLNERSKNLSSVegiSVEFASLTRGLADWLSDFSDKldgqgkv 5981
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEE---LEAQIEQLKEELKALREALDELRAELTLL---NEEAANLRERLESLERRIAAT------- 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5982 ssqpdkqHKQLQELKQLESELIVQQPRLARARDlcrqlcdkakdastktDLRSKLTALEKDMNDTTRKLEICKAAVEEAS 6061
Cdd:TIGR02168 837 -------ERRLEDLEEQIEELSEDIESLAAEIE----------------ELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6062 QQAEKFEADCKELLTWISEAANNLQESEPLSSDLdilreQMRQNRTLQQELSLKEpeirQLLEKG-----DKLVKESSPT 6136
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQL-----ELRLEGLEVRIDNLQE----RLSEEYsltleEAEALENKIE 964
|
890 900
....*....|....*....|
gi 1397727998 6137 TEVRAIADKVGELQGEWTRL 6156
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKEL 984
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
5967-6504 |
3.59e-06 |
|
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: 54.59 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5967 WLSDFSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDT 6046
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6047 TRKLEICKAAV------EEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLKEPEIR 6120
Cdd:TIGR00618 324 AKLLMKRAAHVkqqssiEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6121 QLLE---KGDKLVKESSPTTEVRAIADKVGELQGEWTRLQQE-VTVQDSRLTMAGSHAQQFTERLDKMAMWLQMTEEKLE 6196
Cdd:TIGR00618 404 ILQReqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6197 KmkpEDVDQNTVVHKLKELQGVQNEMMKK-SHDRERLNSEGTSLVECvdSGKEAIKQQVAVINERWDAVNKALSERASHL 6275
Cdd:TIGR00618 484 Q---ETRKKAVVLARLLELQEEPCPLCGScIHPNPARQDIDNPGPLT--RRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6276 EDLGQRLGEVQDSLAEATSALNKwenklavhnslgLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEVDGGETSN 6355
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNR------------SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6356 LRDELNKLRGQHQTLQGELSELVAEMETGAQiVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGSQLADMKDFLTR 6435
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQ-ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727998 6436 LGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQHLTQAL 6504
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAAL 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5697-6450 |
3.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5697 DLSEVQQQLLDITQRYEIVGERLADRQQELQLMLTSIRTFMQDMQDILQwLDLKDHETDSAQ------PLPTNEKDAKKR 5770
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK-EKIGELEAEIASlersiaEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5771 LKEHEVFHREILSK-EGLVEDIRKKAQDL--LKTRHGVPGEEM--LQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRD 5845
Cdd:TIGR02169 324 LAKLEAEIDKLLAEiEELEREIEEERKRRdkLTEEYAELKEELedLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5846 MREHEQQLTLWLAQKD-RMLDVLGPVAMEPNMLASQMEQVKVLREELSAQEptydhflncahGILERCgdkSQDGIAVSR 5924
Cdd:TIGR02169 404 LKRELDRLQEELQRLSeELADLNAAIAGIEAKINELEEEKEDKALEIKKQE-----------WKLEQL---AADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5925 RLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGqgkvssqpdkQHKQLQELKQLESELIV 6004
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG----------VHGTVAQLGSVGERYAT 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6005 QQPRLARAR--------DLCRQLCD---KAKDASTKTDLrskltALEKdMNDTTRKLEIC--KAAVEEASQQAE---KFE 6068
Cdd:TIGR02169 540 AIEVAAGNRlnnvvvedDAVAKEAIellKRRKAGRATFL-----PLNK-MRDERRDLSILseDGVIGFAVDLVEfdpKYE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6069 ADCKELLtwiseaannlqESEPLSSDLDILREQMRQNR--TLQQELSLKEPEIR--QLLEKGDKLVKESSPtTEVRAIAD 6144
Cdd:TIGR02169 614 PAFKYVF-----------GDTLVVEDIEAARRLMGKYRmvTLEGELFEKSGAMTggSRAPRGGILFSRSEP-AELQRLRE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6145 KVGELQGEWTRLQQEVTVQDSRL---------------------TMAGSHAQQFTERLDKMAMWLQMTEEKLEKMKPEdv 6203
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLdelsqelsdasrkigeiekeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE-- 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6204 dQNTVVHKLKELQGVQNEMMKKSHDRERlnSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLG 6283
Cdd:TIGR02169 760 -LKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6284 EVQDSLAEATSalNKWENKLAVHNSLGLSAKdpkhinrikdlledtgwLASQLNNTETMLNSIEvdgGETSNLRDELNKL 6363
Cdd:TIGR02169 837 ELQEQRIDLKE--QIKSIEKEIENLNGKKEE-----------------LEEELEELEAALRDLE---SRLGDLKKERDEL 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6364 RGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGsqlaDMKDFLTRLGEKVETL 6443
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE----DVQAELQRVEEEIRAL 970
|
....*..
gi 1397727998 6444 KDLEQQA 6450
Cdd:TIGR02169 971 EPVNMLA 977
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6931-7441 |
5.67e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6931 SEVVNELGDLVDWFVDADSRL-QNQQPIASDLDLLQqqlAEQKVMNE-EINNQKV--KARDTLSASKKLLsdsamEDNSA 7006
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELkQKENKLQENRKIIE---AQRKAIQElQFENEKVslKLEEEIQENKDLI-----KENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7007 IRNKMDELKQwvdTVSGSAnERQSLLEqavpfarhfHEAHTELVVWLD---DVEPVLSELDVLSVDAD--------QVKK 7075
Cdd:pfam05483 153 TRHLCNLLKE---TCARSA-EKTKKYE---------YEREETRQVYMDlnnNIEKMILAFEELRVQAEnarlemhfKLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7076 QQEKAKVLKQEVadRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNR-RMDNVRTKVRDRSNSIDQAMQQSAEFTDK 7154
Cdd:pfam05483 220 DHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRdKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7155 LENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENK--AMEEDLEMRH------NALESVKNAAEELLRQAgdeqdeavk 7226
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeaQMEELNKAKAahsfvvTEFEATTCSLEELLRTE--------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7227 dvRQKLE-----------ELTKLYKDIQERGR---GRQRALEE---TLAVAEKFWDElhalNSSLKDLQEALSSVDQPAL 7289
Cdd:pfam05483 369 --QQRLEknedqlkiitmELQKKSSELEEMTKfknNKEVELEElkkILAEDEKLLDE----KKQFEKIAEELKGKEQELI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7290 EPEAIREQQ-------------------EELEALKEDIEASQADFEEVQQTGDTLLgmvgtTEQPEVQKNVDDAGASLAA 7350
Cdd:pfam05483 443 FLLQAREKEihdleiqltaiktseehylKEVEDLKTELEKEKLKNIELTAHCDKLL-----LENKELTQEASDMTLELKK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7351 ISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEF-------------SEFEPVASEFETIKKQ------WDELK 7411
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgdevkckldkSEENARSIEYEVLKKEkqmkilENKCN 597
|
570 580 590
....*....|....*....|....*....|
gi 1397727998 7412 NFKTRVEPKNVEIESLNQHVTELTKSSTPE 7441
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7177-7371 |
6.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7177 AQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDeaVKDVRQKLEELTKLYKDIqERGRGRQRALEET 7256
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERL-DASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7257 LAVAEKfwdELHALNSSLKDLQEALSSVDQpalEPEAIREQQEELEALKEDIEASQAdfEEVQQTGDTLLgmvgttEQPE 7336
Cdd:COG4913 694 LEELEA---ELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF------AAAL 759
|
170 180 190
....*....|....*....|....*....|....*
gi 1397727998 7337 VQKNVDDAGASLAAISDQYSKRSQELESALAQAVH 7371
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6574-7231 |
6.42e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6574 TGLEtDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVamqKAPSPEQRVVRAQLQeqklvq 6653
Cdd:PRK03918 155 LGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI---NEISSELPELREELE------ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6654 kMVTDRTPSMKAVQDSGNQL--ITGLDPAERKHIESELQQLNSRWEALTKRVVD---RTAILEEVQGLAGEFQDVLDPLT 6728
Cdd:PRK03918 225 -KLEKEVKELEELKEEIEELekELESLEGSKRKLEEKIRELEERIEELKKEIEEleeKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6729 TWLDAANKRFTALEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYCKG-EDVIMIQLKIDGVQKQNGE 6807
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6808 LRshIEDCLEQMEEAlplakhfQEAHAEFLSWASKVEPELRALELGVPDEETNIEEL----------ANQLTEEMQplLD 6877
Cdd:PRK03918 384 LT--PEKLEKELEEL-------EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRELTEEHR--KE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6878 IINSEGAELAEvapgdaglrvediINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELgDLVDWFVDADSRLQnqqpi 6957
Cdd:PRK03918 453 LLEEYTAELKR-------------IEKELKEIEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLK----- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6958 ASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKL--LSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQA 7035
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7036 VPFARHFHEAHTELVVWLDDVEPVLSELdvlsvdadqvKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQ 7115
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKEL----------KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7116 VQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQsaefTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEED 7195
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKT----LEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
650 660 670
....*....|....*....|....*....|....*.
gi 1397727998 7196 lemrhNALESVKNAAEELLRQAGDEQDEAVKDVRQK 7231
Cdd:PRK03918 740 -----RALSKVGEIASEIFEELTEGKYSGVRVKAEE 770
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7071-7588 |
6.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7071 DQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAmcgskgAEQVQSMLDDDNRRMDNVRtKVRDRSNSIDQAMQQSAE 7150
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEE------LEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7151 FTDKLEnmldtltvtaeqvrsaepisaqpdKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQ 7230
Cdd:COG4717 144 LPERLE------------------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7231 KLEELtklykdiqergRGRQRALEETLAVAEkfwDELHALNSSLKDLQEalssvdqpALEPEAIREQQEELEALKEdIEA 7310
Cdd:COG4717 200 ELEEL-----------QQRLAELEEELEEAQ---EELEELEEELEQLEN--------ELEAAALEERLKEARLLLL-IAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7311 SQADFEEVQQTGDTLLGMVGtteqpevqkNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKL--LVWLQEAED 7388
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIA---------GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeeEELEELLAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7389 EFSEFEPVASEFETIKKQWDELKNFKTRVEPKN--VEIESLNQHVTELTKSSTPEQASVLREPMTQLNiRWNNLLtnigD 7466
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELK----E 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7467 RQRELQMALLTAGQFDHAhkelknwmDLVDVTLDEItpvygDPKLVEIElAKLRIVQNDITAHQESVESISKEAQRLMTS 7546
Cdd:COG4717 403 ELEELEEQLEELLGELEE--------LLEALDEEEL-----EEELEELE-EELEELEEELEELREELAELEAELEQLEED 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1397727998 7547 EGIAQA----QGLKTKMEDMEKTWeniqAKSRAKQDMLEDGLREAQ 7588
Cdd:COG4717 469 GELAELlqelEELKAELRELAEEW----AALKLALELLEEAREEYR 510
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
8346-8394 |
8.57e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 46.77 E-value: 8.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1397727998 8346 GRVTRKEFIEGIISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:cd00051 15 GTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
8138-8193 |
8.75e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 48.08 E-value: 8.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 8138 LEDLLAWLNNAEMTLADVDrqtIPQDMAIIQQLIKEHQDFQNEMSSRQPDVDRLTK 8193
Cdd:pfam00435 10 ADDLESWIEEKEALLSSED---YGKDLESVQALLKKHKALEAELAAHQDRVEALNE 62
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8138-8193 |
1.06e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 8138 LEDLLAWLNNAEMTLADVDrqtIPQDMAIIQQLIKEHQDFQNEMSSRQPDVDRLTK 8193
Cdd:smart00150 7 ADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNE 59
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
5974-6449 |
1.09e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5974 KLDGQGKVSSQpdkqhKQLQELKQLESELIVQqprLARARDLCRQLCDKAKDAST--KTDLRSKLTALEKDMNDTTRKLE 6051
Cdd:pfam05483 302 KMSLQRSMSTQ-----KALEEDLQIATKTICQ---LTEEKEAQMEELNKAKAAHSfvVTEFEATTCSLEELLRTEQQRLE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6052 ICKAAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVK 6131
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6132 E-----SSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKMAMWLQMTEEKL-------EKM- 6198
Cdd:pfam05483 454 DleiqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeERMl 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6199 KPEDVDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDL 6278
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6279 GQRLGEVQDSLAEATSALNKWENKLavhNSLGLSAKDPKH-----INRIKDLLEDtgwlasQLNNTETMLNSIE---VDG 6350
Cdd:pfam05483 614 HQENKALKKKGSAENKQLNAYEIKV---NKLELELASAKQkfeeiIDNYQKEIED------KKISEEKLLEEVEkakAIA 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6351 GETSNLRDELNKlRGQHQtlqgeLSELVAEMETGAQiveQFQGLLKivggqflELESELG----SKTPVSRDDAELGSQL 6426
Cdd:pfam05483 685 DEAVKLQKEIDK-RCQHK-----IAEMVALMEKHKH---QYDKIIE-------ERDSELGlyknKEQEQSSAKAALEIEL 748
|
490 500
....*....|....*....|...
gi 1397727998 6427 ADMKDFLTRLGEKVETLKDLEQQ 6449
Cdd:pfam05483 749 SNIKAELLSLKKQLEIEKEEKEK 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5769-6485 |
1.25e-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: 52.75 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5769 KRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTrhgvpgeemLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMRE 5848
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQE---------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5849 HEQQltlwlaQKDRMLDVLGPVAMEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDGIAVSRRLDT 5928
Cdd:TIGR02168 303 QKQI------LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5929 VSKAWNKLQSRLNERSKNLSS----VEGISVEFASLTRGLADWLSDFSDKLdgQGKVSSQPDKQHKQLQELKQLESELIV 6004
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASlnneIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6005 QQPRLARARDLCRQLCDKAKDASTKTD-----LRSKLTALEKDMNDTTRKLEICKAAVEEASQQA-------------EK 6066
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAErelaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlselisvdEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6067 FEAdckELLTWISEAANNL--QESEPLSSDLDILREQMRQNRTLQQELSLKEPEI----RQLLEKGDKLVK-----ESSP 6135
Cdd:TIGR02168 535 YEA---AIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIqgndREILKNIEGFLGvakdlVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6136 TTEVRAIADKVG------------ELQGEWTRLQQEVTVQDSRLT----MAGSHAQQFTERLDKMAMwLQMTEEKLEKMK 6199
Cdd:TIGR02168 612 PKLRKALSYLLGgvlvvddldnalELAKKLRPGYRIVTLDGDLVRpggvITGGSAKTNSSILERRRE-IEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6200 PEDVDQNTvvhKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLG 6279
Cdd:TIGR02168 691 EKIAELEK---ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6280 QRLGEVQDSLAEATSALNKWENKLAVHNSLGLSAKDpkhinRIKDLLEDTGWLASQLNNTETMLNSIEVDGGETsnlRDE 6359
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLERRIAAT---ERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6360 LNKLRGQHQTLQGELSELVAEME----TGAQIVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGSQLADMKDFLTR 6435
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6436 LGEKVETLK--------DLEQQASSLcNAGYVSDPELLKSQVEALSNQHASLTERATQ 6485
Cdd:TIGR02168 920 LREKLAQLElrleglevRIDNLQERL-SEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4997-5148 |
1.79e-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: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 4997 LGDLEQILKHDsQMGDEASKVKLQLEAHKSTHEKIQSQQQPILSLVYKAEQLTENYQEEltpeqVTQLTTQASLLKATLE 5076
Cdd:cd00176 16 LSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-----AEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 5077 KVSKTSERRLSHLTKAADeLAKFEEESKKFRTWMGAAFSELtNQEDYLKRFEDLKVLGEKHRELASDISSHQ 5148
Cdd:cd00176 90 ELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6916-7611 |
1.92e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6916 IEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTL-SASKK 6994
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAhIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6995 LLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAvPFARHFHEAHTELVVWLDDVEPVLSELDVLSVDADQVK 7074
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQR-RLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7075 KQQEKAKVLKQEVADRKPIVDRLNktgtalvamcgskgAEQVQSMldddnrrmdnvrtkVRDRSNSIDQAMQQSAEFTDK 7154
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQ--------------REQATID--------------TRTSAFRDLQGQLAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7155 LENMLDTLTVTAEQVRSAEPISAQP--DKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKL 7232
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIhlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7233 EELTKLYkdIQERGRGRQRALEETLAVAEKFWDEL-HALNSSLKDLQEalssvdqpaLEPEAIREQQEEL------EALK 7305
Cdd:TIGR00618 515 PARQDID--NPGPLTRRMQRGEQTYAQLETSEEDVyHQLTSERKQRAS---------LKEQMQEIQQSFSiltqcdNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7306 EDIEASQADFEEVQQTGDTLL----GMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLV 7381
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7382 WLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSSTpEQASVLREPMTQLNIRwNNLL 7461
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAR-EDAL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7462 TNIGDRQRELQMALLTAGQFDHAHKELKNWMDLvdVTLDEITPVYGDPKLvEIELAKLRIVQNDITAHQESVESISKEAQ 7541
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTEAHFNNNEEVTAAL--QTGAELSHLAAEIQF-FNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727998 7542 RLMTSEGIAQA-QGLKTKMEDMEKTWENIQ------AKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQLIIS 7611
Cdd:TIGR00618 819 LNLQCETLVQEeEQFLSRLEEKSATLGEIThqllkyEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIK 895
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
182-277 |
2.00e-05 |
|
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: 46.91 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 182 ALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTvAEKEFGVTRLLDPEDVD 261
Cdd:cd21185 5 ATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMA 80
|
90
....*....|....*.
gi 1397727998 262 VPNPDEKSILTYVSSL 277
Cdd:cd21185 81 DPEVEHLGIMAYAAQL 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7189-7380 |
2.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7189 NKAMEEDLEMRHNALESVKNAAEELLRQAGDEQD--EAVKDVRQKLEELTKLYKDIQERGRgRQRALEETLAVAEKFWDE 7266
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7267 LHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAG- 7345
Cdd:COG4913 687 LAALEEQLEELEAELEELE------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALg 760
|
170 180 190
....*....|....*....|....*....|....*.
gi 1397727998 7346 -ASLAAISDQYSKRSQELESALAQAvhfQDQLMKLL 7380
Cdd:COG4913 761 dAVERELRENLEERIDALRARLNRA---EEELERAM 793
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5455-5636 |
2.67e-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: 49.37 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5455 LREFQEKLEQTNLWVHDGILQLDSKELSKLSSD--DMKQQLEKLAREKHNRLRTIQEIQVAAEQLLQDpRTGEGEAVKNL 5532
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESveALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5533 VSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIaLLWLSQMEARLDEFQPVAiDVGIVEQQKMELQPMLQEYEDY 5612
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
|
170 180
....*....|....*....|....
gi 1397727998 5613 APKIDEVNDLGNAYEAMINPGDRP 5636
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADE 182
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6898-7503 |
2.69e-05 |
|
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: 51.56 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6898 VEDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQN--QQPIASDLDL--LQQQLAEQKV 6973
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKikNKLLKLELLLsnLKKKIQKNKS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6974 MNEEINNQKvKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDT---VSGSANERQSLLEQAvpfarhfHEAHTELV 7050
Cdd:TIGR04523 216 LESQISELK-KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQN-------NKKIKELE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7051 VWLDDVEPVLSEL------DVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLN-------KTGTALVAMCGSKGAE--- 7114
Cdd:TIGR04523 288 KQLNQLKSEISDLnnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNeqisqlkKELTNSESENSEKQRElee 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7115 ---QVQSMLDDDNRRMDNVrTKVRDRSNSIDQAMQQSaeftDKLENMLDTLTVTAEQvrSAEPISAQPDKLREQIEENKA 7191
Cdd:TIGR04523 368 kqnEIEKLKKENQSYKQEI-KNLESQINDLESKIQNQ----EKLNQQKDEQIKKLQQ--EKELLEKEIERLKETIIKNNS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7192 MEEDLEMRHNALE----SVKNAAEEL-------------LRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALE 7254
Cdd:TIGR04523 441 EIKDLTNQDSVKEliikNLDNTRESLetqlkvlsrsinkIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7255 ETLAVAEKFWDELHALNSSLKDLQEALSSVDQ----PALEPEaIREQQEELEALKEDIEASQADFEEVQQTGDtllgmvg 7330
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQELID------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7331 tteqpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLvwlqeaedefSEFEPVASEFETIKKQWDEL 7410
Cdd:TIGR04523 593 -----QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK----------SKKNKLKQEVKQIKETIKEI 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7411 KNFKTRVEPKNVEIESLNQHVTELTKSSTPEqASVLREPMTQLNIRwNNLLTNIGDRQRELQMALLTAGQFDhahKELKN 7490
Cdd:TIGR04523 658 RNKWPEIIKKIKESKTKIDDIIELMKDWLKE-LSLHYKKYITRMIR-IKDLPKLEEKYKEIEKELKKLDEFS---KELEN 732
|
650
....*....|...
gi 1397727998 7491 WMDLVDVTLDEIT 7503
Cdd:TIGR04523 733 IIKNFNKKFDDAF 745
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
5808-6236 |
2.75e-05 |
|
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: 51.65 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5808 EEML---QQQLQELDDKWHGLRALSEQQRKGLEDMvSDLRDMREHE-QQLTLWLAQKDRMLDvlgpvamepnmlasQMEQ 5883
Cdd:pfam05483 362 EELLrteQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVElEELKKILAEDEKLLD--------------EKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5884 VKVLREELSAQEPTYDHFLNCAHgilERCGDKSQDGIAVSRRLDTVSKAWNKLQSRL-NERSKNL---SSVEGISVEFAS 5959
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQARE---KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIeltAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5960 LTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELK----QLESELIVQQPRLARARDLCRQLCDKAKDasTKTDLRSK 6035
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekemNLRDELESVREEFIQKGDEVKCKLDKSEE--NARSIEYE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6036 LTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLK 6115
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6116 EPEIRQLLEkgDKLVKEsspTTEVRAIADKVGELQGEW-TRLQQEVTvqdSRLTMAGSHAQQFTERLDKMAMWLQMTEEK 6194
Cdd:pfam05483 662 EIEDKKISE--EKLLEE---VEKAKAIADEAVKLQKEIdKRCQHKIA---EMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1397727998 6195 LEKMKPEDVDQNTVVHKLK-ELQGVQNEMMKKSHDRERLNSEG 6236
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6244-6723 |
2.91e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6244 DSGKEAIKQQVAVINERWDAVNKALSER----------ASHLEDLGQRLGEVQDSLAEATSALNKWENKLavhNSLGLSA 6313
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEA---ESLREDA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6314 KDpkHINRIKDLLEDTGWLASQLNNTETML----------------NSIEVDGGETS--NLRDELNKLRGQHQTLQGELS 6375
Cdd:PRK02224 352 DD--LEERAEELREEAAELESELEEAREAVedrreeieeleeeieeLRERFGDAPVDlgNAEDFLEELREERDELREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6376 ELVAEMETGAQIVEQFQGLLKiVG-----GQFLElESELGSKTPVSRDD-AELGSQLADMKDFLTRLGEKVETLKDLEQQ 6449
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLE-AGkcpecGQPVE-GSPHVETIEEDRERvEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6450 ASslcnagyvsdpellksQVEALSNQHASLTERATQRQSDVVANQHSIQHL-TQALNLVWGDIDKASSTLDAMGPAGGNV 6528
Cdd:PRK02224 508 ED----------------RIERLEERREDLEELIAERRETIEEKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6529 TTVKALQEELkGFVKSTMEPLQKQFESVSRqgqaliktavagsnTTGLETDLESLAERWAGLVEKVAEHEKNLDSalLRT 6608
Cdd:PRK02224 572 EEVAELNSKL-AELKERIESLERIRTLLAA--------------IADAEDEIERLREKREALAELNDERRERLAE--KRE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6609 GKFQdamaslldwLAETEELVAMQKAPSPEQRVVRAQLQeqklvqkmVTDRTPSMKAVQDSGNQLITGldpaerkhIESE 6688
Cdd:PRK02224 635 RKRE---------LEAEFDEARIEEAREDKERAEEYLEQ--------VEEKLDELREERDDLQAEIGA--------VENE 689
|
490 500 510
....*....|....*....|....*....|....*...
gi 1397727998 6689 LQQLNS---RWEALTKRVVDRTAILEEVQGLAGEFQDV 6723
Cdd:PRK02224 690 LEELEElreRREALENRVEALEALYDEAEELESMYGDL 727
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
646-739 |
3.38e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 46.54 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 646 LSEFLQGATAELTWLAEREEvEVTRDWVSKDL-NLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVL 724
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEA-LLSSEDYGKDLeSVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81
|
90
....*....|....*
gi 1397727998 725 MASLQARWSWLLQLV 739
Cdd:pfam00435 82 LEELNERWEQLLELA 96
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
550-644 |
5.09e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 46.16 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 550 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE---EQKLYTQKLSSVE 626
Cdd:pfam00435 7 FRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghyASEEIQERLEELN 86
|
90
....*....|....*...
gi 1397727998 627 VAYSLLLNTSSRRLKFLE 644
Cdd:pfam00435 87 ERWEQLLELAAERKQKLE 104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
5784-6473 |
5.48e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5784 KEGLVEDIR-----KKAQDLLKTRHGvpgeemLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEQQLTLWLA 5858
Cdd:PRK02224 185 QRGSLDQLKaqieeKEEKDLHERLNG------LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5859 QKDRMLDVLGPVAMEPNMLAsqmEQVKVLREELSAQEPTYDHflncahgILERCGDKSQDGIAVSRRLDTVSKAWNKLQS 5938
Cdd:PRK02224 259 EIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5939 RLNERSKNlssvegisvefASLTRGLADWLSDFSDKLDGQGKvssqpDKQhkqlQELKQLESELivqqprlarardlcrq 6018
Cdd:PRK02224 329 RLEECRVA-----------AQAHNEEAESLREDADDLEERAE-----ELR----EEAAELESEL---------------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6019 lcdkAKDASTKTDLRSKLTALEKDMNDTtrkleicKAAVEEASQQAEKFEADCKELLTWISEAANNLQEsepLSSDLDIL 6098
Cdd:PRK02224 373 ----EEAREAVEDRREEIEELEEEIEEL-------RERFGDAPVDLGNAEDFLEELREERDELREREAE---LEATLRTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6099 REQMRQNRTLQQElsLKEPEIRQllekgdkLVKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGShAQQFT 6178
Cdd:PRK02224 439 RERVEEAEALLEA--GKCPECGQ-------PVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6179 ERLDKMAMWLQMTEEKLEKMKPE-DVDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDsgkeAIKQQVAVI 6257
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA----ELNSKLAEL 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6258 NERWDAVNKaLSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNslglsakdpkhiNRIKDLLEdtgwlasqln 6337
Cdd:PRK02224 585 KERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR------------ERKRELEA---------- 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6338 ntetmlnsiEVDGgetsnlrDELNKLRGQHQTLQGELSELVAEMEtgaQIVEQFQGLLKIVGGqfleLESELgsktpvsr 6417
Cdd:PRK02224 642 ---------EFDE-------ARIEEAREDKERAEEYLEQVEEKLD---ELREERDDLQAEIGA----VENEL-------- 690
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 6418 ddaelgSQLADMKDFLTRLGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALS 6473
Cdd:PRK02224 691 ------EELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
5986-6383 |
5.56e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5986 DKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDTTRKLEICKAAVEE------ 6059
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelee 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6060 ----ASQQAEKFEADCKELLTWISEAAnnLQESEPLSSDLDILREQMRQnrtLQQELSLKEPEIRQLLEKGDKLVKESSP 6135
Cdd:COG4717 164 eleeLEAELAELQEELEELLEQLSLAT--EEELQDLAEELEELQQRLAE---LEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6136 TTEVRAIADKVGELQGEWTRL---QQEVTVQDSRLTMAGshAQQFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKL 6212
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLallGLGGSLLSLILTIAG--VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6213 KElQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERwdAVNKALSERASHLEDLGQRLGEVQDSLAEA 6292
Cdd:COG4717 317 EE-EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6293 TSALNKWENKLAVHNSLgLSAKDPKHINRIKDLLEDTgwLASQLNNTETMLNSIEvdgGETSNLRDELNKLRGQHQTL-- 6370
Cdd:COG4717 394 AEEYQELKEELEELEEQ-LEELLGELEELLEALDEEE--LEEELEELEEELEELE---EELEELREELAELEAELEQLee 467
|
410
....*....|...
gi 1397727998 6371 QGELSELVAEMET 6383
Cdd:COG4717 468 DGELAELLQELEE 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6056-6729 |
5.57e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6056 AVEEASQQAEkfeadckeLLTWISEAANNLQEsepLSSDLDILREQMRQNR--TLQQELSLKEPEIRQLLEKGDKLvkes 6133
Cdd:COG4913 243 ALEDAREQIE--------LLEPIRELAERYAA---ARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARL---- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6134 spTTEVRAIADKVGELQGEWTRLQQEvtvqdsrltmagsHAQQFTERLdkmamwlqmteEKLEKmkpedvdqntvvhklk 6213
Cdd:COG4913 308 --EAELERLEARLDALREELDELEAQ-------------IRGNGGDRL-----------EQLER---------------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6214 ELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERwdavnkaLSERASHLEDLGQRLGEVQDSLAEAT 6293
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL-------LEALEEELEALEEALAEAEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6294 SALNKWENKLAvhnSLGLSAKD-PKHINRIKDLLedtgwlASQLNNTETML----NSIEVDGGEtSNLRDELNK-LRGQH 6367
Cdd:COG4913 419 RELRELEAEIA---SLERRKSNiPARLLALRDAL------AEALGLDEAELpfvgELIEVRPEE-ERWRGAIERvLGGFA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6368 QTLqgelseLVAEmetgaqivEQFQGLLKIV-----GG--QFLELESELGSKTPVSRDDAELGSQLA----DMKDFL-TR 6435
Cdd:COG4913 489 LTL------LVPP--------EHYAAALRWVnrlhlRGrlVYERVRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLeAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6436 LGE-----KVETLKDLEQQASSLCNAGYVSDP--------------------------ELLKSQVEALSNQHASLTERAT 6484
Cdd:COG4913 555 LGRrfdyvCVDSPEELRRHPRAITRAGQVKGNgtrhekddrrrirsryvlgfdnraklAALEAELAELEEELAEAEERLE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6485 QRQSDVVANQHSIQHLTQALNLVWGDIDkasstldamgpaggnvttVKALQEELkgfvkstmeplqkqfesvsRQGQALI 6564
Cdd:COG4913 635 ALEAELDALQERREALQRLAEYSWDEID------------------VASAEREI-------------------AELEAEL 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6565 KTAVAGSNttgletDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVamQKAPSPEQRVVRA 6644
Cdd:COG4913 678 ERLDASSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRA 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6645 QLqEQKLVQKMVTDRTPSM-KAVQDSGNQLITGLDPAERKhIESELQQLNSRWEALTkrvVDRTAILEEvqglAGEFQDV 6723
Cdd:COG4913 750 LL-EERFAAALGDAVERELrENLEERIDALRARLNRAEEE-LERAMRAFNREWPAET---ADLDADLES----LPEYLAL 820
|
....*.
gi 1397727998 6724 LDPLTT 6729
Cdd:COG4913 821 LDRLEE 826
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5036-5520 |
5.73e-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: 50.44 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5036 QPILSLVYKAEQLTE--NYQEELTPEQ--VTQ----LTTQASLLKATLEKVSKTSERR--LSHLTKAADELAKFEEESKK 5105
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNalELAKKLRPGYriVTLdgdlVRPGGVITGGSAKTNSSILERRreIEELEEKIEELEEKIAELEK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5106 FRTWMGAAFSELTNQEDYLKRFEDlkvlgekhrELASDISSHQADHRFMSMAVQKYMEEAKLYKLEMDSFRADRArpARH 5185
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELE---------ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE--ELE 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5186 SLISMECVAADNVKDKLTDLTEEYHDLSNRCNLLGDRLADLSGKHRQFNDVAFKLLTWLTDMEGQLSSVKQDAGLSEpQQ 5265
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-EQ 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5266 LQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNslsgqaaeqqQVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAAvth 5345
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLN----------ERASLEEALALLRSELEELSEELRELESKRSEL--- 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5346 sqdiTQAMNELvswMDSAEQVVTTQLPISLRRPELNAQLQSfsavdadvtNHQSALDAVKALANELvktcELDIARAvEQ 5425
Cdd:TIGR02168 914 ----RRELEEL---REKLAQLELRLEGLEVRIDNLQERLSE---------EYSLTLEEAEALENKI----EDDEEEA-RR 972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5426 RLTSLDEKFSSLQakcrqrdrdleEVD-SSLREFQEKLEQTnlwvhdgilqldskelsklssDDMKQQLEKLAREKHNRL 5504
Cdd:TIGR02168 973 RLKRLENKIKELG-----------PVNlAAIEEYEELKERY---------------------DFLTAQKEDLTEAKETLE 1020
|
490
....*....|....*.
gi 1397727998 5505 RTIQEIQVAAEQLLQD 5520
Cdd:TIGR02168 1021 EAIEEIDREARERFKD 1036
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7261-7363 |
6.69e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7261 EKFWDELHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMvGTTEQPEVQKN 7340
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727998 7341 VDDAGASLAAISDQYSKRSQELE 7363
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
7171-7376 |
6.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7171 SAEPISAQPD--KLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrg 7248
Cdd:COG3883 8 APTPAFADPQiqAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7249 RQRALEETLAVAEK------FWDELhaLNSslKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTG 7322
Cdd:COG3883 84 RREELGERARALYRsggsvsYLDVL--LGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 7323 DTLLGMVGTTEQpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQL 7376
Cdd:COG3883 160 EALKAELEAAKA-ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7186-8070 |
7.40e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7186 IEENKAMEEDLEMRHNALESVKnaAEELLRQAGDEQDEAVKDVR---QKLEELTKLYKDIQERGRGRQRALEETLAVAEK 7262
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIK--ALETLRQVRQTQGQKVQEHQmelKYLKQYKEKACEIRDQITSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7263 FWDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEASQadfEEVQQTGDTLLGMVGTTEQPEVQknvd 7342
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKM---EKVFQGTDEQLNDLYHNHQRTVR---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7343 DAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQE------AEDEFSEFEPVASEFETIKKQWD---ELKNF 7413
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirARDSLIQSLATRLELDGFERGPFserQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7414 KTRV-EPKNVEIESLNQHVTELTKSST--PEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHKELKN 7490
Cdd:TIGR00606 396 HTLViERQEDEAKTAAQLCADLQSKERlkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7491 WMDLVDVTLDEItPVYGDPKLVEIELAKLRIVQNDitaHQESVESISKEAQRLmtsegiAQAQGLKTKMEDMEKTwenIQ 7570
Cdd:TIGR00606 476 LDQELRKAEREL-SKAEKNSLTETLKKEVKSLQNE---KADLDRKLRKLDQEM------EQLNHHTTTRTQMEML---TK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7571 AKSRAKQDMLEDGLREAQGFTGELQDILAKindiegqLIISKPVGGLPETAKEQLEKFMDVYAELEKLEpqvQSLNVMGE 7650
Cdd:TIGR00606 543 DKMDKDEQIRKIKSRHSDELTSLLGYFPNK-------KQLEDWLHSKSKEINQTRDRLAKLNKELASLE---QNKNHINN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7651 KLggKSKGPALANLRQNLQHLNQrCDYIRSRACDRKKKLEDAEGMATNFHGELNKFISWLTDTEKTLNNLQPVSRLVERV 7730
Cdd:TIGR00606 613 EL--ESKEEQLSSYEDKLFDVCG-SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7731 TSQIED-HRDLQkdiSKHREAMVALEKMGTHLKYFSQKQDVVLIK-NLLSSIQHRWEKIVSRSAERTRHLERGYKEAK-- 7806
Cdd:TIGR00606 690 EAELQEfISDLQ---SKLRLAPDKLKSTESELKKKEKRRDEMLGLaPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKnd 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7807 -QFNDTWKDLITWLIEAEKTLETETSVANE--------PDKIKAQISK---------HKEFQRRLGAKQPVYDGVNKAGR 7868
Cdd:TIGR00606 767 iEEQETLLGTIMPEEESAKVCLTDVTIMERfqmelkdvERKIAQQAAKlqgsdldrtVQQVNQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7869 LLKeRCPSD---DVPTIQAMLTELKSHWNNVCSKSVDRQRKLEEGLLLSGQFTEALDALLDWLAKVEP---ALADDAPVH 7942
Cdd:TIGR00606 847 LNR-KLIQDqqeQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPletFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7943 GDI------------DTVNgflDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLIELNaawdrvcklsvS 8010
Cdd:TIGR00606 926 EELissketsnkkaqDKVN---DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECE-----------K 991
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 8011 KQDRLEHAQRLAEEFHKKAQQLLSWLADAERQLHYRGPIPD--EEPL----------ILQQMEEHKKFEESL 8070
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEveEELKqhlkemgqmqVLQMKQEHQKLEENI 1063
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
7162-7434 |
7.49e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7162 LTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESV---KNAAEELLRQAGDEQDEAvkdvRQKLEELTKL 7238
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAreeLEQLEEELEQARSELEQL----EEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7239 YKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEA-IREQQEELEALKEDIEASQadfEE 7317
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSeIAEREEELKELEEQLESLQ---EE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7318 VQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLvwLQEAEDEFSEFEPVA 7397
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE--AKLGLALSALLDALE 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1397727998 7398 SEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTEL 7434
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6748-7441 |
9.36e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6748 AEGIEHLIQELKKLQKEVNEHEPAMKQLA--------TAGKKLQDYCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQM 6819
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfarrQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6820 EE---ALPLAKHFQEAHAEFLSWASKVEPELRALELGVPDEETNIEELanQLTEEMQPLLDIINSEGAELAEVAPGDAgl 6896
Cdd:PTZ00121 1312 EEakkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA--EAAEEKAEAAEKKKEEAKKKADAAKKKA-- 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6897 rvediinRDNKRFDNLRDQIEKRAQKVQLARQRSSEV--VNELGDLVDWFVDADsRLQNQQPIASDLDLLQQQlAEQKVM 6974
Cdd:PTZ00121 1388 -------EEKKKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKK-AEEAKK 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6975 NEEINNQKVKARDTLSASKKL----LSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHTelV 7050
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK--A 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7051 VWLDDVEPVLSELDVLSvdADQVKKQQEKAKVLKQEVADRkpivDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNV 7130
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKK--AEELKKAEEKKKAEEAKKAEE----DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7131 RTKVRDRSNSIDQAMQQSAEFTDKLENMLDTltvTAEQVRSAEPI--SAQPDKLREQIEENKAMEE--DLEMRHNALESV 7206
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKK---EAEEKKKAEELkkAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDE 1687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7207 KNAAEELLRQAgdEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAE---KFWDELHALNSSLKDLQEALSS 7283
Cdd:PTZ00121 1688 KKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKE 1765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7284 VDQPALEPEAIREQQEELEALKED----------IEASQADFEEVQQTGDTLLGMVGTTEQPEVQ--KNVDDAGASLAAI 7351
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDekrrmevdkkIKDIFDNFANIIEGGKEGNLVINDSKEMEDSaiKEVADSKNMQLEE 1845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7352 SDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEfepvASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHV 7431
Cdd:PTZ00121 1846 ADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE----ADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDK 1921
|
730
....*....|
gi 1397727998 7432 TELTKSSTPE 7441
Cdd:PTZ00121 1922 DEYIKRDAEE 1931
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
8346-8394 |
9.69e-05 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 46.32 E-value: 9.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1397727998 8346 GRVTRKEFIEGIISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:COG5126 48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
7128-7321 |
1.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7128 DNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLtvtaeqVRSAEPISAQPDKLREQIEEnkaMEEDLEMRHNALESVK 7207
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7208 NAA-------------EELLRQAG---------DEQDEAVKDVRQKLEELTKLYKDIQErgrgRQRALEETLAVAEKFWD 7265
Cdd:PHA02562 262 TAAakikskieqfqkvIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDT----AIDELEEIMDEFNEQSK 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727998 7266 ELHALNSSLKDLQEALSSVDQPALEPEA-IREQQEELEALKEDIEASQADFEEVQQT 7321
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAaIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5765-6287 |
1.24e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5765 KDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRhgvpgeEMLQQQLQELDDKWHGLRALsEQQRKGLEDMVSDLR 5844
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS------EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5845 DMREHEQQLTLWLAQKDRMLDVLGPVAMEPNMLASQMEQVKVLREELSAQEPtydhflncaHGILERCGDKSQDGIAVSR 5924
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP---------EKLEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5925 RLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGL-----ADWLSDFSDKLDGQGKVSSQPDKQHKQLQ-ELKQL 5998
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKLRkELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5999 ESELiVQQPRLARARDLCRQLcdkakdastkTDLRSKLTALEkdmndttrkleickaaVEEASQQAEKFEADCKELLTWI 6078
Cdd:PRK03918 486 EKVL-KKESELIKLKELAEQL----------KELEEKLKKYN----------------LEELEKKAEEYEKLKEKLIKLK 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6079 SEAANnlqesepLSSDLDILREQMRQNRTLQQELSLKEPE----IRQLLEKGDKLVKE-SSPTTEVRAIADKVGELQGEW 6153
Cdd:PRK03918 539 GEIKS-------LKKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEElEERLKELEPFYNEYLELKDAE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6154 TRLQQEVTVQDSrltmagshaqqFTERLDKMAMWLQMTEEKLEKMKPEdVDQNTVVHKLKELQGVQNEMMKKSHDRERLN 6233
Cdd:PRK03918 612 KELEREEKELKK-----------LEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEYEELREEYLELSRELAGLR 679
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 6234 SEgtslVECVDSGKEAIKQQVAVINERWDAVNKALSErashLEDLGQRLGEVQD 6287
Cdd:PRK03918 680 AE----LEELEKRREEIKKTLEKLKEELEEREKAKKE----LEKLEKALERVEE 725
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
178-283 |
1.29e-04 |
|
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: 45.18 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 178 SAREALLLWSRRTtegYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 256
Cdd:cd21312 12 TPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 88
|
90 100
....*....|....*....|....*..
gi 1397727998 257 PEDVDVPNPDEKSILTYVSSlydvFPQ 283
Cdd:cd21312 89 PEEIVDPNVDEHSVMTYLSQ----FPK 111
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
550-644 |
1.35e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 44.63 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 550 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE---EQKLYTQKLSSVE 626
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEghpDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1397727998 627 VAYSLLLNTSSRRLKFLE 644
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7175-7448 |
1.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7175 ISAQPDKLREQIEE---------------NK--AMEEDLEmRHNALES-VKNAAEELLRQAgdEQDEAVKDVRQKLEELt 7236
Cdd:COG1196 150 IEAKPEERRAIIEEaagiskykerkeeaeRKleATEENLE-RLEDILGeLERQLEPLERQA--EKAERYRELKEELKEL- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7237 klykDIQERGRgRQRALEETLAVAEKfwdELHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEASQADFE 7316
Cdd:COG1196 226 ----EAELLLL-KLRELEAELEELEA---ELEELEAELEELEAELAELE------AELEELRLELEELELELEEAQAEEY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7317 EVQQTGDTLLG--MVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFE 7394
Cdd:COG1196 292 ELLAELARLEQdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1397727998 7395 pvaSEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSSTPEQASVLRE 7448
Cdd:COG1196 372 ---AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
6898-7322 |
1.38e-04 |
|
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: 49.57 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6898 VEDIINRDNKRFDNLRDQIEKRAQKVQLARQ------RSSEVVNELGDLVDWFVDADSRLQNQQPIA---SDLDLLQQQL 6968
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMAREleelsaRESDLEQDYQAASDHLNLVQTALRQQEKIEryqEDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6969 AEQKVMNEEINNQKVKARDTLSASkkllsdsamednsaiRNKMDELKqwvdtvSGSANERQSLLEQAVPfARHFHEAhte 7048
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAA---------------EEEVDSLK------SQLADYQQALDVQQTR-AIQYQQA--- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7049 lVVWLDDVEpVLSELDVLSvdADQVKKQQEKAKVLKQEVADRkpivdRLnktgtalvamcgskGAEQVQSMLDDDNRRMD 7128
Cdd:COG3096 419 -VQALEKAR-ALCGLPDLT--PENAEDYLAAFRAKEQQATEE-----VL--------------ELEQKLSVADAARRQFE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7129 NVRTKVR------DRSNSIDQAMQQSAEFTDkLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEE-NKAMEEDLEMRHN 7201
Cdd:COG3096 476 KAYELVCkiagevERSQAWQTARELLRRYRS-QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7202 aLESVKNAAEELLRQAGDEQDEAVKD---VRQKLEELTKLYKDIqergrgRQRALE--ETLAVAEKFWDELHAlnsSLKD 7276
Cdd:COG3096 555 -LEELLAELEAQLEELEEQAAEAVEQrseLRQQLEQLRARIKEL------AARAPAwlAAQDALERLREQSGE---ALAD 624
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1397727998 7277 LQEaLSSVDQPALEPEAIREQQE-ELEALKEDIEaSQAdfEEVQQTG 7322
Cdd:COG3096 625 SQE-VTAAMQQLLEREREATVERdELAARKQALE-SQI--ERLSQPG 667
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6058-6699 |
1.42e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6058 EEASQQAEKF-----EADCKELLTWISEAANNLQESEPLSSDLDILREQMRQnrtLQQELSLKEPEIRQLLEKGDKLvke 6132
Cdd:COG1196 206 ERQAEKAERYrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEEL--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6133 sspTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKL 6212
Cdd:COG1196 280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6213 KELQGVQNEmmkkshdrERLNSEgtslvecvdsgkEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEA 6292
Cdd:COG1196 357 EAELAEAEE--------ALLEAE------------AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6293 TSALNKWENKLAvhnslGLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEvdggetsNLRDELNKLRGQHQTLQG 6372
Cdd:COG1196 417 ERLEEELEELEE-----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-------ELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6373 ELSELVAEMETGAQIVEQFQGLLKIVGGQFLEleselgsktPVSRDDAELGSQLADmkdfltrLGEKVETlkDLEQQASS 6452
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLL---------AGLRGLAGAVAVLIG-------VEAAYEA--ALEAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6453 LCNAGYVSDPELLKSQVEALSNQHASlteRATQRQSDVVANQHSIQHLTQALNLVWGDIDKASS--TLDAMGPAGGNVTT 6530
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAG---RATFLPLDKIRARAALAAALARGAIGAAVDLVASDlrEADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6531 VKALQEELKGFVKSTMEPLQKQFESVSRQGQALI-KTAVAGSNTTGLETDLESLAERWAGLVEKVAEHEKNLDSALLRtg 6609
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSaGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA-- 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6610 kfqdamaslldwLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAERKHIESEL 6689
Cdd:COG1196 702 ------------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
650
....*....|
gi 1397727998 6690 QQLNSRWEAL 6699
Cdd:COG1196 770 ERLEREIEAL 779
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
7173-7810 |
1.42e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7173 EPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAgdEQDEAV-KDVRQKLEELTKLYKDIQERGRGRQR 7251
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI--ADDEKShSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7252 ALEETLAVAekfwDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEALKedieasqadfeevqqtgdtllgmvgt 7331
Cdd:PRK01156 240 ALNELSSLE----DMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDP-------------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7332 teqpeVQKNVDDAGASLAAISDQYSKRsQELESALAQAVHFQDQLMKLlvwlQEAEDEFSEFEPVASEFETIKKQWDELK 7411
Cdd:PRK01156 290 -----VYKNRNYINDYFKYKNDIENKK-QILSNIDAEINKYHAIIKKL----SVLQKDYNDYIKKKSRYDDLNNQILELE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7412 NFKTRVEPKNVEIESLNQHVTELTKSSTPEQASVlrepmtqlnirwnnlltnigdrQRELQMALLTAgqfdhahKELKNW 7491
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI----------------------SEILKIQEIDP-------DAIKKE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7492 MDLVDVTLDEITpvygdpklveielAKLRIVQNDITAHQESVESISKEAQrLMTSEGIAQAQGL---KTKMEDMEKTWEN 7568
Cdd:PRK01156 411 LNEINVKLQDIS-------------SKVSSLNQRIRALRENLDELSRNME-MLNGQSVCPVCGTtlgEEKSNHIINHYNE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7569 IQAKSRAKQDMLEdglREAQGFTGELQDILAKINDIEGQLI-ISKPVGGLPETAKEQLEKFMDVYAEL-------EKLEP 7640
Cdd:PRK01156 477 KKSRLEEKIREIE---IEVKDIDEKIVDLKKRKEYLESEEInKSINEYNKIESARADLEDIKIKINELkdkhdkyEEIKN 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7641 QVQSLNVmgEKLGGKSKgpalANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEG----MATNFHGELNKFISWLTDTEKT 7716
Cdd:PRK01156 554 RYKSLKL--EDLDSKRT----SWLNALAVISLIDIETNRSRSNEIKKQLNDLESrlqeIEIGFPDDKSYIDKSIREIENE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7717 LNNLQPVSRLVERVTSQIEDHR----DLQKDISK-------HREAMVALEKMGTHLKYFSQKQDVVLI-----KNLLSSI 7780
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRgkidNYKKQIAEidsiipdLKEITSRINDIEDNLKKSRKALDDAKAnrarlESTIEIL 707
|
650 660 670
....*....|....*....|....*....|
gi 1397727998 7781 QHRWEKIVSRSAERTRHLERGYKEAKQFND 7810
Cdd:PRK01156 708 RTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6731-7320 |
1.51e-04 |
|
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: 48.95 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6731 LDAANKRftaLEPH---SPDAEGIEHLIQELKK-----------LQKEVNEHEPAMKQLATAGKKLQDYCKG-EDVIMIQ 6795
Cdd:pfam05483 204 VQAENAR---LEMHfklKEDHEKIQHLEEEYKKeindkekqvslLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6796 lkiDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFLSWASKV------EPELRALELG---------VPDEETN 6860
Cdd:pfam05483 281 ---DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTicqlteEKEAQMEELNkakaahsfvVTEFEAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6861 IEELANQLTEEMQPL------LDIINSE----GAELAEVAPGDAGLRVE-----DIINRDNKRFDNlRDQIEKRAQKVQL 6925
Cdd:pfam05483 358 TCSLEELLRTEQQRLeknedqLKIITMElqkkSSELEEMTKFKNNKEVEleelkKILAEDEKLLDE-KKQFEKIAEELKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6926 ARQrssevvnELGDLvdwfvdadsrLQNQQPIASDLDLL--------QQQLAEQKVMNEEINNQKVKARDTLSASKKLLs 6997
Cdd:pfam05483 437 KEQ-------ELIFL----------LQAREKEIHDLEIQltaiktseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6998 dsaMEDNSAIRNKMD---ELKQWVDTVSGSANERQSLLEQavpfARHFHEAHTELvvwLDDVEPVLSELdvlsvdadQVK 7074
Cdd:pfam05483 499 ---LENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQ----IENLEEKEMNL---RDELESVREEF--------IQK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7075 KQQEKAKVLKQEVADRKPIVDRLNKtgtalvamcgskgaeqvQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDK 7154
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKK-----------------EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7155 lenmldtLTVTAEQVRSAEpisAQPDKLREQIEENK-AMEEDLEMRHNALESVKNAAEELLrqagdeqdEAVKDVRQKLE 7233
Cdd:pfam05483 624 -------GSAENKQLNAYE---IKVNKLELELASAKqKFEEIIDNYQKEIEDKKISEEKLL--------EEVEKAKAIAD 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7234 ELTKLYKDIQERGrgrQRALEETLAVAEKF---WDELHALNSS---LKDLQEALSSVDQPALEPEaIREQQEELEALKED 7307
Cdd:pfam05483 686 EAVKLQKEIDKRC---QHKIAEMVALMEKHkhqYDKIIEERDSelgLYKNKEQEQSSAKAALEIE-LSNIKAELLSLKKQ 761
|
650
....*....|...
gi 1397727998 7308 IEASQADFEEVQQ 7320
Cdd:pfam05483 762 LEIEKEEKEKLKM 774
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
7111-7392 |
1.61e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7111 KGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMldtltvTAEQVRSAEPISAQPDKLREQIEENK 7190
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK------YKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7191 A----MEEDLEM-------RHNALESVKNAAEELLRQAGDEQDEAvKDVRQKLE----ELTKLYKDIQE-RGRGRQRAle 7254
Cdd:pfam07888 129 ArireLEEDIKTltqrvleRETELERMKERAKKAGAQRKEEEAER-KQLQAKLQqteeELRSLSKEFQElRNSLAQRD-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7255 etlavaekfwDELHALNSSLKDLQEALSSVDQPALEPEAIREQ----QEELEALKEDIEASQADFEEVQQTGDTLLGMVG 7330
Cdd:pfam07888 206 ----------TQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslQERLNASERKVEGLGEELSSMAAQRDRTQAELH 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 7331 TTEQPEVQKNVDDAGASLAAISDQySKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSE 7392
Cdd:pfam07888 276 QARLQAAQLTLQLADASLALREGR-ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7227-7376 |
1.98e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7227 DVRQKLEELTKlykdiqergrgRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEAL-- 7304
Cdd:COG4913 607 DNRAKLAALEA-----------ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELea 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397727998 7305 -KEDIEASQADFEEVQQtgdtllgmvgttEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQL 7376
Cdd:COG4913 676 eLERLDASSDDLAALEE------------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6525-6602 |
1.99e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 44.24 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727998 6525 GGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQALIKTAVAGSNTtgLETDLESLAERWAGLVEKVAEHEKNLD 6602
Cdd:smart00150 27 GKDLESVEALLKKHEAF-EAELEAHEERVEALNELGEQLIEEGHPDAEE--IEERLEELNERWEELKELAEERRQKLE 101
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
6663-7250 |
2.32e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6663 MKAVQDSGNQLITGLDpaerkHIESELQQLNSRWEALTKRVVDRTA----ILEEVQGLAGEFQDVLDPLTTwLDAANKRF 6738
Cdd:PRK01156 171 LKDVIDMLRAEISNID-----YLEEKLKSSNLELENIKKQIADDEKshsiTLKEIERLSIEYNNAMDDYNN-LKSALNEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6739 TALEphspdaEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQD------YCKGEDVI-MIQLKIDGVQKQngELRSH 6811
Cdd:PRK01156 245 SSLE------DMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvYKNRNYINdYFKYKNDIENKK--QILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6812 IEDCLEQMEEALPLAKHFQEAHAEFLSWASKVEP------ELRALELGVPDEETNIEELANQLTEEM--QPLLDIINSEG 6883
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSknIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6884 AELAEVAPGDAGLRVEDIiNRD-----------NKRFDNLRDQIEKRAQKVQLARQRSSEVV--NELGD-----LVDWFV 6945
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEI-NVKlqdisskvsslNQRIRALRENLDELSRNMEMLNGQSVCPVcgTTLGEeksnhIINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6946 DADSRLQNQ-QPIASDLDLLQQQLAEQKVMNEEINNQKVKardTLSASKKLLSdSAMEDNSAIRNKMDELKQWVDTVSGS 7024
Cdd:PRK01156 476 EKKSRLEEKiREIEIEVKDIDEKIVDLKKRKEYLESEEIN---KSINEYNKIE-SARADLEDIKIKINELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7025 ANERQSLleqavpfarHFHEAHTELVVWLDdvepVLSELDVLSVDADQVKKQQEKAKVlkqevadrKPIVDRLNKTGTal 7104
Cdd:PRK01156 552 KNRYKSL---------KLEDLDSKRTSWLN----ALAVISLIDIETNRSRSNEIKKQL--------NDLESRLQEIEI-- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7105 vamcgskGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDklre 7184
Cdd:PRK01156 609 -------GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN---- 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7185 QIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQ 7250
Cdd:PRK01156 678 DIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7180-7412 |
2.35e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7180 DKLREQIEENKAMEEDLEmrhNALESVKnaAEELLRQAGDEQDEAVKDVR--QKLEELTKLYKDIQERG--RGRQRALEE 7255
Cdd:COG4913 228 DALVEHFDDLERAHEALE---DAREQIE--LLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLEllEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7256 TLAVAEkfwDELHALNSSLKDLQEALSsvdqpALEpEAIREQQ-EELEALKEDIEASQADFEEVQQTGDTLlgmvgtteq 7334
Cdd:COG4913 303 ELARLE---AELERLEARLDALREELD-----ELE-AQIRGNGgDRLEQLEREIERLERELEERERRRARL--------- 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727998 7335 pevQKNVDDAGASLAAISDqyskrsqELESALAQAVHFQDQLMKLLVWLQEAEDE-FSEFEPVASEFETIKKQWDELKN 7412
Cdd:COG4913 365 ---EALLAALGLPLPASAE-------EFAALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLER 433
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6719-6814 |
2.47e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.86 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6719 EFQDVLDPLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyCKGEDVIMIQLKI 6798
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90
....*....|....*.
gi 1397727998 6799 DGVQKQNGELRSHIED 6814
Cdd:smart00150 80 EELNERWEELKELAEE 95
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
5696-6392 |
2.48e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5696 DDLSEVQQQLL---DITQRYEIVGERLADRQQELQLMLTSIrtfmQDMQDILQWLDL--KDHETDSAQPLPTNEK---DA 5767
Cdd:TIGR00606 224 DQITSKEAQLEssrEIVKSYENELDPLKNRLKEIEHNLSKI----MKLDNEIKALKSrkKQMEKDNSELELKMEKvfqGT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5768 KKRLKEHEVFH-REILSKEGLVEDIRKKAQDLLKTRHGVPGE----EMLQQQLQELDDKWH------GLRALSEQQRKGL 5836
Cdd:TIGR00606 300 DEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEktelLVEQGRLQLQADRHQehirarDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5837 EDMVSDLRDMREHEQQLTLwlaQKDRMLDVLGPVAMEPNMLASQM----EQVKVLREELSAQEPTYDH---FLNCAHGIL 5909
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTL---VIERQEDEAKTAAQLCADLQSKErlkqEQADEIRDEKKGLGRTIELkkeILEKKQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5910 ERCGDKSQDGIAVSRRLDTVSKAWNKLQSRLNERSKNlSSVEGISVEFASLTRGLADWLSDFSdkldgqgKVSSQPDKQH 5989
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN-SLTETLKKEVKSLQNEKADLDRKLR-------KLDQEMEQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5990 KQLQELKQLESELIVQQPRLARARDL----CRQLCDKAKDASTKTDLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAE 6065
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKMDKDEQIRKIksrhSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6066 KFEADCKELLTWISEAANNLQE---SEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEkgdKLVKESSPTTEVrai 6142
Cdd:TIGR00606 609 HINNELESKEEQLSSYEDKLFDvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFIT---QLTDENQSCCPV--- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6143 ADKVGELQGEWtrlqQEVTVQDSRLTMAGSHAQQFTERLDKmamwlQMTEEKLEKMKPEDVDQNTVVHKLKELQGVQNEM 6222
Cdd:TIGR00606 683 CQRVFQTEAEL----QEFISDLQSKLRLAPDKLKSTESELK-----KKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6223 MKKSHDRERLNS---EGTSLVECVDSGKEAIK---QQVAVIN---ERWDAVNKALSERASHLE--DLGQRLGEVQDSLAE 6291
Cdd:TIGR00606 754 QKVNRDIQRLKNdieEQETLLGTIMPEEESAKvclTDVTIMErfqMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6292 ATSALNKWENKLAVHNSLglsakdpkhinrIKDLLEDTGWLASQLNNTETMLNSIEVDGGETSNLRDELNKLRGQHQTLQ 6371
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKL------------IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
730 740
....*....|....*....|.
gi 1397727998 6372 GELSELVAEMETGAQIVEQFQ 6392
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQ 922
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
5718-6297 |
2.86e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5718 RLADRQQELQLMLTSI------------------RTFMQDMQDILQWLdlkDHETDSAQPLPTNEKDAKKRLKEHEvfhR 5779
Cdd:pfam01576 65 RLAARKQELEEILHELesrleeeeersqqlqnekKKMQQHIQDLEEQL---DEEEAARQKLQLEKVTTEAKIKKLE---E 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5780 EILskegLVEDIRKKaqdLLKTRHGVpgEEMLQQ---QLQELDDKWHGLRALSEQQrkglEDMVSDLRDMREHEQQLTLW 5856
Cdd:pfam01576 139 DIL----LLEDQNSK---LSKERKLL--EERISEftsNLAEEEEKAKSLSKLKNKH----EAMISDLEERLKKEEKGRQE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5857 LAQKDRMLDVlgpvamEPNMLASQMEQVKVLREELSAQeptydhflncahgiLERCGDKSQDGIAvsrRLDTVSKAWNKL 5936
Cdd:pfam01576 206 LEKAKRKLEG------ESTDLQEQIAELQAQIAELRAQ--------------LAKKEEELQAALA---RLEEETAQKNNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5937 QSRLNErsknlssvegisvefasltrgLADWLSDFSDKLDGQGKVSSQPDKQHKQL-QELKQLESEL--------IVQQP 6007
Cdd:pfam01576 263 LKKIRE---------------------LEAQISELQEDLESERAARNKAEKQRRDLgEELEALKTELedtldttaAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6008 RLARARDLcrQLCDKAKDASTKT------DLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEA 6081
Cdd:pfam01576 322 RSKREQEV--TELKKALEEETRSheaqlqEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6082 AnnlQESeplssdldilrEQMRQNRTLQ-QELSLKEPEI-RQLLEKGDKLVKEsspTTEVRAIADKVGELQGEWTRLQQE 6159
Cdd:pfam01576 400 K---QDS-----------EHKRKKLEGQlQELQARLSESeRQRAELAEKLSKL---QSELESVSSLLNEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6160 VTVQDSRLTMAGSHAQQFTERLDKMAMWLQMTEEK----LEKMKPEDVDQNTVVHKLKELQGVQNEMMKKShdrerlnSE 6235
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDErnslQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-------EE 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 6236 GTSLVECVDSGKEAIKQQVavinerwDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALN 6297
Cdd:pfam01576 536 DAGTLEALEEGKKRLQREL-------EALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5993-6835 |
2.92e-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: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5993 QELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRskltaLEKDMNDTTRKLEICKAAVEEASQQAEKFEADCK 6072
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6073 ELLTWISEAANNLQESEPLSSDLDILREQ-MRQNRTLQQELSLKEPEIRQLLEKGDKLVKE-SSPTTEVRAIADKVGELQ 6150
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDElKDYREKLEKLKREINELK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6151 GEWTRLQQEVTVQDSRLT-----MAGSHAQ--QFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKLK-ELQGVQNEM 6222
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlnaaIAGIEAKinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeEYDRVEKEL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6223 MKKSHDRERLNSEGTSLVECVDSGKEAikqqVAVINERWDAVNKALSERASHLED--------LGQRLGEV---QDSLAE 6291
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAV----EEVLKASIQGVHGTVAQLGSVGERyataievaAGNRLNNVvveDDAVAK 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6292 ATSALNKWE----------NKLAV-HNSLGLSAK-------------DPKHINRIKDLLEDTGwlasqlnntetMLNSIE 6347
Cdd:TIGR02169 562 EAIELLKRRkagratflplNKMRDeRRDLSILSEdgvigfavdlvefDPKYEPAFKYVFGDTL-----------VVEDIE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6348 VDggetsnlRDELNKLRgqHQTLQGELSElvaemETGAqiveqfqgllkIVGGqFLELESELGSKTPVSRDDAELGSQLA 6427
Cdd:TIGR02169 631 AA-------RRLMGKYR--MVTLEGELFE-----KSGA-----------MTGG-SRAPRGGILFSRSEPAELQRLRERLE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6428 DMKDFLTRLGEKVETLKDLEQQASSLcnagyVSDPE----LLKSQVEALSNQHASLTERATQRQSDvvanqhsIQHLTQA 6503
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQE-----LSDASrkigEIEKEIEQLEQEEEKLKERLEELEED-------LSSLEQE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6504 LNLVWGDIDKASSTLDAMgpaggnvttvkalQEELkgfvkstmEPLQKQFESvsrqgqalIKTAVAGSNTTGLETDLESL 6583
Cdd:TIGR02169 753 IENVKSELKELEARIEEL-------------EEDL--------HKLEEALND--------LEARLSHSRIPEIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6584 AERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQklvqkmvtdrtpsM 6663
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------------L 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6664 KAVQDSGNQLItgldpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEfqdvldpLTTWLDAANKRFTALEP 6743
Cdd:TIGR02169 871 EELEAALRDLE-----SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-------LKAKLEALEEELSEIED 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6744 HSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAG-KKLQDYckgEDVIM----IQLKIDGVQKQNGELRSHIEDCLEQ 6818
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNmLAIQEY---EEVLKrldeLKEKRAKLEEERKAILERIEEYEKK 1015
|
890 900
....*....|....*....|..
gi 1397727998 6819 -----MEEALPLAKHFQEAHAE 6835
Cdd:TIGR02169 1016 krevfMEAFEAINENFNEIFAE 1037
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
7172-7412 |
3.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7172 AEPISAQPDKLREQIEENKAMEEDLEMRHNALESV------------KNAAEELLRQAGDEQDEAVKDVRQKLEELTKLY 7239
Cdd:PRK04863 788 IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafeadPEAELRQLNRRRVELERALADHESQEQQQRSQL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7240 KDIQERGRGRQRALEE-TLAVAEKFWDELHALNSSLKDLQEALSSVDQ-----PALEPEA--IREQQEELEALKEDIEAS 7311
Cdd:PRK04863 868 EQAKEGLSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKRFVQQhgnalAQLEPIVsvLQSDPEQFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7312 QADFEEVQQTGDTLLGMVgtteQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQlmkllvwLQEAEDEFS 7391
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVV----QRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ-------LRQAQAQLA 1016
|
250 260
....*....|....*....|....*
gi 1397727998 7392 EFEPV----ASEFETIKKQWDELKN 7412
Cdd:PRK04863 1017 QYNQVlaslKSSYDAKRQMLQELKQ 1041
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
8368-8394 |
3.52e-04 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 41.21 E-value: 3.52e-04
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6752-7295 |
3.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6752 EHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgedvimIQLKIDGVQKQNGELRSHIEDcLEQMEEALPLAKHFQE 6831
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE---------LEEELEELEAELEELREELEK-LEKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6832 AHAEFlswaSKVEPELRALElgvpDEETNIEELANQLTEemqpLLDIINSEGAELAEvAPGDAGLRVEDIINRDNKRFDN 6911
Cdd:COG4717 137 LEAEL----AELPERLEELE----ERLEELRELEEELEE----LEAELAELQEELEE-LLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6912 LRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDAD--SRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTL 6989
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6990 SASKKLLSDSAMEdNSAIRNKMDELKQWVDTVSGSANERQSLLEQavpfarhfheahtelvVWLDDVEPVlSELDVLSVD 7069
Cdd:COG4717 284 GLLALLFLLLARE-KASLGKEAEELQALPALEELEEEELEELLAA----------------LGLPPDLSP-EELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7070 ADQVKKQQEKAKVLKQEVAdrkpiVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRmdnvrtkvrdrsnsiDQAMQQSA 7149
Cdd:COG4717 346 IEELQELLREAEELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQAEEY---------------QELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7150 EFTDKLENMLDTLTVTAEQvrsaepisAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAgdEQDEAVKDVR 7229
Cdd:COG4717 406 ELEEQLEELLGELEELLEA--------LDEEELEEELEELEEELEELEEELEELREELAELEAELEQL--EEDGELAELL 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7230 QKLEELtklykdiqergrgrqralEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIR 7295
Cdd:COG4717 476 QELEEL------------------KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
189-260 |
4.03e-04 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 42.67 E-value: 4.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727998 189 RTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLID-----FRQARSNSNKQ-NLELAFTVAEKEFGVTRL-LDPEDV 260
Cdd:pfam11971 3 SQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDledicLKESMSLADSLyNIQLLQEFCQRHLGNRCChLTLEDL 81
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
6785-7436 |
4.16e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6785 YCKGEDVI-MIQLKIDGVQKQNGELRSHIEDcLEQMEEALplakhfqeahAEFLSWASKVEPELRALElgvpdEETNIEE 6863
Cdd:PRK01156 168 YDKLKDVIdMLRAEISNIDYLEEKLKSSNLE-LENIKKQI----------ADDEKSHSITLKEIERLS-----IEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6864 ----LANQLTEEMQPLLDIINSEGAELAEVapgDAGLRVEDIINRDNKRFDNLRDQIEKraQKVQLARQRSSEVVNELGD 6939
Cdd:PRK01156 232 ddynNLKSALNELSSLEDMKNRYESEIKTA---ESDLSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINDYFKYKND 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6940 LVDW---FVDADSRLQNQQPIASDLDLLQQ---QLAEQKVMNEEINNQKVKardtlsaskklLSDSAMEDNSAIRNkMDE 7013
Cdd:PRK01156 307 IENKkqiLSNIDAEINKYHAIIKKLSVLQKdynDYIKKKSRYDDLNNQILE-----------LEGYEMDYNSYLKS-IES 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7014 LKQWVDtvsgsanerqsllEQAVPFARHFHEAHTELVVWLDDVEPVLSELDVLSVDADQVKKQ----QEKAKVLKQEVAD 7089
Cdd:PRK01156 375 LKKKIE-------------EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKvsslNQRIRALRENLDE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7090 RKPIVDRLNktGTALVAMCGSK-GAEQVQSMLDDDNRRMDNVRTKVRDRSN---SIDQAMQQSAEFTDKLE--------- 7156
Cdd:PRK01156 442 LSRNMEMLN--GQSVCPVCGTTlGEEKSNHIINHYNEKKSRLEEKIREIEIevkDIDEKIVDLKKRKEYLEseeinksin 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7157 --NMLDTLTVTAEQVRSAEP-ISAQPDKLREQIEENKAME-EDLEMRH----NALESVKNAAEELLRQAGDEQDEAVKDV 7228
Cdd:PRK01156 520 eyNKIESARADLEDIKIKINeLKDKHDKYEEIKNRYKSLKlEDLDSKRtswlNALAVISLIDIETNRSRSNEIKKQLNDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7229 RQKLEELTKLYKDIQERGRGRQRALEetlavaekfwDELHALNSSLKDLQEalssvdqpalEPEAIREQQEELEALKEDI 7308
Cdd:PRK01156 600 ESRLQEIEIGFPDDKSYIDKSIREIE----------NEANNLNNKYNEIQE----------NKILIEKLRGKIDNYKKQI 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7309 easqadfeevqqtgdtllgmvgtTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAED 7388
Cdd:PRK01156 660 -----------------------AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSD 716
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 7389 EFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEI---ESLNQHVTELTK 7436
Cdd:PRK01156 717 RINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAmirKSASQAMTSLTR 767
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7221-7457 |
4.21e-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: 47.07 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7221 QDEAVKDVRQKLEELtklykdiQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQpalepeAIREQQEE 7300
Cdd:COG4942 18 QADAAAEAEAELEQL-------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ------ELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7301 LEALKEDIEASQADFEEVQQTGDTLLG---MVGTTEQPEV---QKNVDDAGASLAAIS----------DQYSKRSQELES 7364
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRalyRLGRQPPLALllsPEDFLDAVRRLQYLKylaparreqaEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7365 ALAQAVHFQDQLMKLLVWLQEAEDEFSEFEpvASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSSTPEQAS 7444
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|...
gi 1397727998 7445 VLREPMTQLNIRW 7457
Cdd:COG4942 243 TPAAGFAALKGKL 255
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
8368-8394 |
4.57e-04 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 40.85 E-value: 4.57e-04
10 20
....*....|....*....|....*..
gi 1397727998 8368 EMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLK 27
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
5814-6504 |
5.08e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5814 QLQELDDKWHGLRALSEQQRKGLEDMVSDLRD--------MREHEQQLtLWLAQKDRmldvlgpvamepnmLASQMEQVK 5885
Cdd:PRK10246 199 ELEKLQAQASGVALLTPEQVQSLTASLQVLTDeekqlltaQQQQQQSL-NWLTRLDE--------------LQQEASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5886 ----VLREELSAQEPTYDHfLNCAHG------ILERCGDKSQDGIAVSRRLDTVSKawnKLQSRLNERSKNLSSVEGISV 5955
Cdd:PRK10246 264 qalqQALAAEEKAQPQLAA-LSLAQParqlrpHWERIQEQSAALAHTRQQIEEVNT---RLQSTMALRARIRHHAAKQSA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5956 EFASLTRGLADWLSD------FSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRL-ARARDLCRQLCDKAKDAST 6028
Cdd:PRK10246 340 ELQAQQQSLNTWLAEhdrfrqWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6029 KTD-LRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQ------ESEPLSSDLDILREQ 6101
Cdd:PRK10246 420 EQRpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAdvkticEQEARIKDLEAQRAQ 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6102 MRQNRTLQQELSLKEPEIR--QLLEKGDKLVKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTE 6179
Cdd:PRK10246 500 LQAGQPCPLCGSTSHPAVEayQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQ 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6180 RLDKMAMWLQMTEEKLEKMKP---EDVDQNTVVHKLKELQGVQNEMmkkshdrerlnsegtslvecvdsgkEAIKQQVAV 6256
Cdd:PRK10246 580 QWQAVCASLNITLQPQDDIQPwldAQEEHERQLRLLSQRHELQGQI-------------------------AAHNQQIIQ 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6257 INERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNSLglsakdPKHINRIKDLLEdtgwLASQL 6336
Cdd:PRK10246 635 YQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTAL------QNRIQQLTPLLE----TLPQS 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6337 NNTETMLNSIEVDggetsNLR---DELNKLRGQHQTLQGELSElvaEMETGAQIVEQFQGLLKivggqfleleselgskt 6413
Cdd:PRK10246 705 DDLPHSEETVALD-----NWRqvhEQCLSLHSQLQTLQQQDVL---EAQRLQKAQAQFDTALQ----------------- 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6414 pvsrddaelGSQLADMKDFLTRLGEKvETLKDLEQQASSLcnagyvsdpELLKSQVEALSNQHASLTERATQRQSDVVAN 6493
Cdd:PRK10246 760 ---------ASVFDDQQAFLAALLDE-ETLTQLEQLKQNL---------ENQRQQAQTLVTQTAQALAQHQQHRPDGLDL 820
|
730
....*....|.
gi 1397727998 6494 QHSIQHLTQAL 6504
Cdd:PRK10246 821 TVTVEQIQQEL 831
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6751-7241 |
5.28e-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: 47.32 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6751 IEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgeDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEA-------- 6822
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ-----EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeleqnn 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6823 ---LPLAKHFQEAHAEFLS--------WASKVEPELRalelgvpDEETNIEELANQLTEEMQplldIINSEGAELAEvap 6891
Cdd:TIGR04523 281 kkiKELEKQLNQLKSEISDlnnqkeqdWNKELKSELK-------NQEKKLEEIQNQISQNNK----IISQLNEQISQ--- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6892 gdagLRVEdiinRDNKRFDN--LRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQPIASDLDLLQQQLA 6969
Cdd:TIGR04523 347 ----LKKE----LTNSESENseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6970 EQK-VMNEEINN---QKVKARDTLSASKKLLSDSAMEDNSaIRNKMDELKQWVDTVSGSANERQSLLEQavpfarhfhea 7045
Cdd:TIGR04523 419 QEKeLLEKEIERlkeTIIKNNSEIKDLTNQDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQNLEQ----------- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7046 hteLVVWLDDVEPVLSELDvlsvdaDQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALvamcgskgaEQVQSMLDDDNR 7125
Cdd:TIGR04523 487 ---KQKELKSKEKELKKLN------EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK---------ESKISDLEDELN 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7126 RMDNVRTK--VRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSA--------EPISAQPDKLREQIEENKAMEED 7195
Cdd:TIGR04523 549 KDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEkkdlikeiEEKEKKISSLEKELEKAKKENEK 628
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7196 LEMRHNALESVKNAAEELLRQAGDEQDEAV----------KDVRQKLEELTKLYKD 7241
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRnkwpeiikkiKESKTKIDDIIELMKD 684
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5843-5947 |
5.38e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5843 LRDMREHEQqltlWLAQKDRMLDVLgPVAMEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDgiaV 5922
Cdd:smart00150 4 LRDADELEA----WLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE---I 75
|
90 100
....*....|....*....|....*
gi 1397727998 5923 SRRLDTVSKAWNKLQSRLNERSKNL 5947
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKL 100
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6434-7034 |
6.06e-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: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6434 TRLGEKVETLKDLEQQASSLcNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVvanQHSIQHLTQALNLVWGDIDK 6513
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHL-HFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW---KEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6514 ASSTLDAMGPAGG-----NVTTVKALQEELKGFvKSTMEPLQKQFE-------SVSRQGQALIKTAVAGSNT--TGLETD 6579
Cdd:pfam12128 320 DRSELEALEDQHGafldaDIETAAADQEQLPSW-QSELENLEERLKaltgkhqDVTAKYNRRRSKIKEQNNRdiAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6580 LESLAERWAGLVEKVAEHEKNLDSALlrtgkfQDAMASLLDWLAETEELVAmQKAPSPEQRVVRAQLQEQKLVQKMVTD- 6658
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLK-SRLGELKLRLNQATATPELLLQLENFDe 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6659 RTPSMKAVQDSGNqlitgldpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDP--------LTT- 6729
Cdd:pfam12128 472 RIERAREEQEAAN--------AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhfLRKe 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6730 ---WLDAANKRF-------TALEPHSPDAEG---------------IEH-----LIQELKK--------LQKEVNEHEPA 6771
Cdd:pfam12128 544 apdWEQSIGKVIspellhrTDLDPEVWDGSVggelnlygvkldlkrIDVpewaaSEEELRErldkaeeaLQSAREKQAAA 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6772 MKQLATAGKKLQDYCKGEDVIMIQLK--IDGVQKQNGELRSHIEDCLEQMEEalplakHFQEAHAEFlswaSKVEPELRA 6849
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALKnaRLDLRRLFDEKQSEKDKKNKALAE------RKDSANERL----NSLEAQLKQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6850 LELGVPDEETNIEELANQLTEEMQP-LLDIINSEGAELAEVAPGDAGLRVE-----DIINRDNKR-----------FDNL 6912
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAyWQVVEGALDAQLALLKAAIAARRSGakaelKALETWYKRdlaslgvdpdvIAKL 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6913 RDQIEKRAQKVQLARQRSSEVvnelgdlVDWFVDADSRLQNQQP--------IASDLDLLQQQLAEQKVMNEEINNQKVK 6984
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEV-------LRYFDWYQETWLQRRPrlatqlsnIERAISELQQQLARLIADTKLRRAKLEM 846
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1397727998 6985 ARDTLSASKKLLSDSAMEDNSAIRnKMDELK--QWVDTVSGSANERQSLLEQ 7034
Cdd:pfam12128 847 ERKASEKQQVRLSENLRGLRCEMS-KLATLKedANSEQAQGSIGERLAQLED 897
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
7057-7301 |
6.60e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7057 EPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAM-----------------CGSKGAEQ---- 7115
Cdd:pfam05622 228 ERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAeireklirlqhenkmlrLGQEGSYRerlt 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7116 -VQSMLDDDNRRMDNVRTKVRdrsnsidQAMQQSAEFTDKLENMLDTLTvtaEQVRSAEPISAQPDKLREQIEENKAMEE 7194
Cdd:pfam05622 308 eLQQLLEDANRRKNELETQNR-------LANQRILELQQQVEELQKALQ---EQGSKAEDSSLLKQKLEEHLEKLHEAQS 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7195 DLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwDELHALNSSL 7274
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASP--PEIQALKNQL 455
|
250 260
....*....|....*....|....*..
gi 1397727998 7275 KDLQEALSSVDQPALEPEAIREQQEEL 7301
Cdd:pfam05622 456 LEKDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
8346-8394 |
7.12e-04 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 7.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1397727998 8346 GRVTRKEFIEGI--ISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 8394
Cdd:pfam13499 17 GYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5717-6300 |
7.36e-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: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5717 ERLADRQQELQLMLTSIRTFMQDMQDILQW---------LDLKDHETDSAQPLpTNEKDAKKRLKEHEVFHREILS---K 5784
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKynrrrskikEQNNRDIAGIKDKL-AKIREARDRQLAVAEDDLQALEselR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5785 EGLVEDIR--KKAQDLLKTRHG--------VPGEEMLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMReheqqlt 5854
Cdd:pfam12128 426 EQLEAGKLefNEEEYRLKSRLGelklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR------- 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5855 lwlAQKDRMLDVLGPVAMEPNMLASQMEQVKvlrEELSAQEPTYDHFLN-------------CAHGILERC--------- 5912
Cdd:pfam12128 499 ---KRRDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRkeapdweqsigkvISPELLHRTdldpevwdg 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5913 ---GDKSQDGI-----------------AVSRRLDTVSKAWNKLQSRLNERSKNLSSvegISVEFASLTRGLADWLSDFS 5972
Cdd:pfam12128 573 svgGELNLYGVkldlkridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQ---ANGELEKASREETFARTALK 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5973 DKLDGQGKVS----SQPDKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDTTR 6048
Cdd:pfam12128 650 NARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6049 KLEICKAAVEEASQQAEkfeADCKELLTWiseaanNLQESEPLSSDLDILREQMRQNRTLQQELS---LKEPEIRQ---- 6121
Cdd:pfam12128 730 QLALLKAAIAARRSGAK---AELKALETW------YKRDLASLGVDPDVIAKLKREIRTLERKIEriaVRRQEVLRyfdw 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6122 -----LLEKgDKLVkessptTEVRAIADKVGELQGEWTRLQQEVTVQDSRLtMAGSHAQQFTE-RLDKMAMWLQMTEEKL 6195
Cdd:pfam12128 801 yqetwLQRR-PRLA------TQLSNIERAISELQQQLARLIADTKLRRAKL-EMERKASEKQQvRLSENLRGLRCEMSKL 872
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6196 EKMKpEDVDQNTVVHKLKELQGvQNEMMKKSHDRErlnsegtslvecvdsgKEAIKQQVavinERWDAVNKALSerASHL 6275
Cdd:pfam12128 873 ATLK-EDANSEQAQGSIGERLA-QLEDLKLKRDYL----------------SESVKKYV----EHFKNVIADHS--GSGL 928
|
650 660
....*....|....*....|....*.
gi 1397727998 6276 EDLGQRLGEVQDSL-AEATSALNKWE 6300
Cdd:pfam12128 929 AETWESLREEDHYQnDKGIRLLDYRK 954
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
6109-7310 |
8.33e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6109 QQELSLKEPEIRQLLEKGDKLvkesspTTEVRAIADKVGELQGEWTRLQQEVTVQdsrlTMAGSHAQQFTERLDKMAMWL 6188
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKA------ESELKELEKKHQQLCEEKNALQEQLQAE----TELCAEAEEMRARLAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6189 QMTEEKLEKMKPEDVDQNtvvhklkelQGVQNEmmkkshdRERLNSEGTSLVECVDSgKEAIKQQVAVINERWDAVNKAL 6268
Cdd:pfam01576 74 EEILHELESRLEEEEERS---------QQLQNE-------KKKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKIKKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6269 SERASHLEDLGQRLGE----VQDSLAEATSALNKWENKLavhnslglsakdpKHINRIKdlledtgwlasqlNNTETMLN 6344
Cdd:pfam01576 137 EEDILLLEDQNSKLSKerklLEERISEFTSNLAEEEEKA-------------KSLSKLK-------------NKHEAMIS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6345 SIEVDGGETSNLRDELNKLRGQHQTLQGELSELVAEMEtgAQIVEQFQGLLKI---VGGQFLELESELGSKTPVSRDDAE 6421
Cdd:pfam01576 191 DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ--AQIAELRAQLAKKeeeLQAALARLEEETAQKNNALKKIRE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6422 LGSQLADMKDFLTR---LGEKVETLK-DLEQQAsslcnagyvsdpELLKSQVEALSNQHASLTERATQRQSDVVANQHSI 6497
Cdd:pfam01576 269 LEAQISELQEDLESeraARNKAEKQRrDLGEEL------------EALKTELEDTLDTTAAQQELRSKREQEVTELKKAL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6498 QHLTQALNLVWGDIDKASSTldamgpaggnvtTVKALQEELKGF--VKSTMEPLQKQFESVSRQGQALIKTAVAGSNTTg 6575
Cdd:pfam01576 337 EEETRSHEAQLQEMRQKHTQ------------ALEELTEQLEQAkrNKANLEKAKQALESENAELQAELRTLQQAKQDS- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6576 lETDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETE-ELVAMQKAPSPeqrvVRAQLQE-QKLVQ 6653
Cdd:pfam01576 404 -EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgKNIKLSKDVSS----LESQLQDtQELLQ 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6654 KMVTDR---TPSMKAVQDSGNQLITGLDPAE--RKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLT 6728
Cdd:pfam01576 479 EETRQKlnlSTRLRQLEDERNSLQEQLEEEEeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6729 TWLDAANKRFTALEphspdaEGIEHLIQELKKLQKEVNEHepamKQLATAGKKLQdycKGEDVIMIQLKidGVQKQNGEL 6808
Cdd:pfam01576 559 QQLEEKAAAYDKLE------KTKNRLQQELDDLLVDLDHQ----RQLVSNLEKKQ---KKFDQMLAEEK--AISARYAEE 623
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6809 RSHIE-DCLEQMEEALPLAKHFQEA--HAEFLSWASK-VEPELRALELGVPDEETNIEEL------ANQLTEEMQPLLDI 6878
Cdd:pfam01576 624 RDRAEaEAREKETRALSLARALEEAleAKEELERTNKqLRAEMEDLVSSKDDVGKNVHELerskraLEQQVEEMKTQLEE 703
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6879 INSE--GAElaevapgDAGLRVEdiinrdnkrfdnlrdqIEKRAQKVQLARQRSSEvvNELGDlvdwfvdaDSRLQnqqp 6956
Cdd:pfam01576 704 LEDElqATE-------DAKLRLE----------------VNMQALKAQFERDLQAR--DEQGE--------EKRRQ---- 746
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6957 iasdldlLQQQLAEQKVMNEEINNQKVKArdtLSASKKL---LSDSAMEDNSAIRNKMDELKQwVDTVSGSANERQSLLE 7033
Cdd:pfam01576 747 -------LVKQVRELEAELEDERKQRAQA---VAAKKKLeldLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQRELE 815
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7034 QAvpfarhfHEAHTELVVWLDDVEPVLSELDvlsvdADQVKKQQEKA---KVLKQEVADRKPIVDRLNKtgtalvamcGS 7110
Cdd:pfam01576 816 EA-------RASRDEILAQSKESEKKLKNLE-----AELLQLQEDLAaseRARRQAQQERDELADEIAS---------GA 874
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7111 KGaeqvQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAepiSAQPDKLREQIE-EN 7189
Cdd:pfam01576 875 SG----KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERST---SQKSESARQQLErQN 947
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7190 K-------AMEEDLEMRHN----ALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRgrqraleetla 7258
Cdd:pfam01576 948 KelkaklqEMEGTVKSKFKssiaALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERR----------- 1016
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|...
gi 1397727998 7259 VAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQ-QEELEALKEDIEA 7310
Cdd:pfam01576 1017 HADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKlQRELDDATESNES 1069
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6173-6277 |
8.37e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 42.69 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6173 HAQQFTERLDKMAMWLQMTEEKLEKM-KPEDVDqnTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIK 6251
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEALLSSEdYGKDLE--SVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1397727998 6252 QQVAVINERWDAVNKALSERASHLED 6277
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
7166-7255 |
9.59e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a 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: 42.31 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7166 AEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLrqagDEQDEAVKDVRQKLEELTKLYKDIQER 7245
Cdd:pfam00435 20 KEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI----DEGHYASEEIQERLEELNERWEQLLEL 95
|
90
....*....|
gi 1397727998 7246 GRGRQRALEE 7255
Cdd:pfam00435 96 AAERKQKLEE 105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7141-7839 |
1.04e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7141 IDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDE 7220
Cdd:TIGR00606 212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7221 QDEAVKDVRqklEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNsslKDLQEALSSVDQPALEPEAIREQ--- 7297
Cdd:TIGR00606 292 MEKVFQGTD---EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN---QEKTELLVEQGRLQLQADRHQEHira 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7298 ----------QEELEALKED--IEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELE-- 7363
Cdd:TIGR00606 366 rdsliqslatRLELDGFERGpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIElk 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7364 ---------------SALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASeFETIKKQWDELKNFKTRVEPK----NVEI 7424
Cdd:TIGR00606 446 keilekkqeelkfviKELQQLEGSSDRILELDQELRKAERELSKAEKNSL-TETLKKEVKSLQNEKADLDRKlrklDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7425 ESLNQHVTELTKSStpeqaSVLREPMTQLN-IRWNNlltnigdrQRELQMALLTAGQFDHAhKELKNWMDLVDvtlDEIT 7503
Cdd:TIGR00606 525 EQLNHHTTTRTQME-----MLTKDKMDKDEqIRKIK--------SRHSDELTSLLGYFPNK-KQLEDWLHSKS---KEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7504 PVYGDPKLVEIELAKLRIVQNDITAHQEsvesiSKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQaKSRAKQDMLEDG 7583
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELE-----SKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIE-KSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7584 LREAQGFTGELQDILAKINDIEGQLIISKpvGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLGGKSKGPA--- 7660
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTE--AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQsii 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7661 ------LANLRQNLQHLNQRCDYIRSRACDRKK-------KLEDAEGMATNFhGELNKFISWLTDTEKTLNNL------- 7720
Cdd:TIGR00606 740 dlkekeIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpEEESAKVCLTDV-TIMERFQMELKDVERKIAQQaaklqgs 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7721 ---QPVSRLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyfSQKQDVVLIKNLLSSIQHRWEKIVSRSAERTRH 7797
Cdd:TIGR00606 819 dldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK--SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1397727998 7798 LERGYKEAKQFNDTWKDLITWLIEAEKTLETETSVANEPDKI 7839
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6576-7244 |
1.12e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6576 LETDLESL------AERWAGLVEKVAEHEKNLdsALLRTGKFQDAMASLLDWLAETEELVAMQKApspEQRVVRAQLQEQ 6649
Cdd:COG1196 198 LERQLEPLerqaekAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6650 KLVQKMVTDRTPSMKA----VQDSGNQLITGLDPAE--RKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDV 6723
Cdd:COG1196 273 RLELEELELELEEAQAeeyeLLAELARLEQDIARLEerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6724 LDPLTTWLDAANKRFTALEphspdaEGIEHLIQELKKLQKEVNEhepAMKQLATAGKKLQDyckgedvimIQLKIDGVQK 6803
Cdd:COG1196 353 LEEAEAELAEAEEALLEAE------AELAEAEEELEELAEELLE---ALRAAAELAAQLEE---------LEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6804 QNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFLSWASKVEPELRALELGVPDEETNIEELANQLTEEMQPLLDIINSEG 6883
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6884 AELAEVAPgdaglrvediinrdnkrfDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQN--QQPIASDL 6961
Cdd:COG1196 495 LLLEAEAD------------------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6962 DLLQQQLAEQKvmneeinnQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDElkqwvdtvsgsANERQSLLEQAVPFARH 7041
Cdd:COG1196 557 EVAAAAIEYLK--------AAKAGRATFLPLDKIRARAALAAALARGAIGAA-----------VDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7042 FHEAHTELVVWLDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLD 7121
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7122 DDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHN 7201
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1397727998 7202 ALESVKNAAEEllrqagdEQDEavkdVRQKLEELTKLYKDIQE 7244
Cdd:COG1196 778 ALGPVNLLAIE-------EYEE----LEERYDFLSEQREDLEE 809
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6932-7033 |
1.49e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6932 EVVNELGDLVDWFVDADSRLQnQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAmEDNSAIRNKM 7011
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727998 7012 DELKQWVDTVSGSANERQSLLE 7033
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6682-7392 |
2.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6682 RKHIESELQQLnsrwEALTkRVVDRTAILEEVQGLAGEFQDVLDPLTTWldAANKRFTALEPHspdaegIEHLIQELKKL 6761
Cdd:COG4913 241 HEALEDAREQI----ELLE-PIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAE------LEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6762 QKEVNEHEpamKQLATAGKKLQDYckgEDVImiqLKIDGVQKQngELRSHIEDCLEQMEEALPLAKHFQEAhaeflswas 6841
Cdd:COG4913 308 EAELERLE---ARLDALREELDEL---EAQI---RGNGGDRLE--QLEREIERLERELEERERRRARLEAL--------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6842 kvepeLRALELGVPDEETNIEELANQLTEemqpLLDIINSEGAELAEVApgdAGLRVEdiINRDNKRFDNLRDQI---EK 6918
Cdd:COG4913 368 -----LAALGLPLPASAEEFAALRAEAAA----LLEALEEELEALEEAL---AEAEAA--LRDLRRELRELEAEIaslER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6919 RA----QKVQLARQRSSEVVNE-------LGDLVDwfVDADSR---------LQNQQpiasdLDLL--QQQLA------E 6970
Cdd:COG4913 434 RKsnipARLLALRDALAEALGLdeaelpfVGELIE--VRPEEErwrgaiervLGGFA-----LTLLvpPEHYAaalrwvN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6971 QKVMNEEINNQKVKARDTLSASKKLLSDSamednsaIRNKMD----ELKQW-------------VDTVSGSANERQSLLE 7033
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDS-------LAGKLDfkphPFRAWleaelgrrfdyvcVDSPEELRRHPRAITR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7034 QAVpfARHFHEAHTelvvwLDDVEPVLSELdVLSVDAdqvkkqQEKAKVLKQEVADrkpIVDRLNKTGTALvamcgskga 7113
Cdd:COG4913 580 AGQ--VKGNGTRHE-----KDDRRRIRSRY-VLGFDN------RAKLAALEAELAE---LEEELAEAEERL--------- 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7114 EQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEftDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKAME 7193
Cdd:COG4913 634 EALEAELDALQERREALQRLAEYSWDEIDVASAEREI--AELEAELERLDASSDDLAALE---EQLEELEAELEELEEEL 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7194 EDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKL-EELTKLYKDIQERGRGRQ--RALEETLAVAEKfwdELHAL 7270
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERElrENLEERIDALRA---RLNRA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7271 NSSLKDLQEALSSVDQPAL-----EPEAIREQQEELEALKED-IEASQADFEEV--QQTGDTLLGMVGTTEQP--EVQKN 7340
Cdd:COG4913 786 EEELERAMRAFNREWPAETadldaDLESLPEYLALLDRLEEDgLPEYEERFKELlnENSIEFVADLLSKLRRAirEIKER 865
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727998 7341 VDDAGASLAAIsDQYSKRSQELE---SALAQAVHFQDQLMKLLVWLQEAEDEFSE 7392
Cdd:COG4913 866 IDPLNDSLKRI-PFGPGRYLRLEarpRPDPEVREFRQELRAVTSGASLFDEELSE 919
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
5930-6171 |
2.46e-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: 44.75 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5930 SKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQ-ELKQLESELIVQQPR 6008
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6009 LARARDLCRQLCDKAKDASTKTDLRSKLTAleKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQEs 6088
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6089 eplssdldiLREQMRQNRTLQQELSLKEPEIRQLLEKGDKlvKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLT 6168
Cdd:COG4942 176 ---------LEALLAELEEERAALEALKAERQKLLARLEK--ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 1397727998 6169 MAG 6171
Cdd:COG4942 245 AAG 247
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
4988-5567 |
2.50e-03 |
|
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: 45.34 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 4988 QELMTEQEHLGDLEQILKHDSQMGDEASKVKLQLEAHKSTHEKIQSQQQPILSLVYKaEQLTENYQEELTPEQVTQLTTQ 5067
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK-LQSLCKELDILQREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5068 AS-----LLKATLEKVSKTSERRLSHLTKAADELAKFEEESKKFRTWMGAAFSELTNQEDYLKRFedLKVLGEKHRELAS 5142
Cdd:TIGR00618 417 SAfrdlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5143 DISSHQADHRFMSMAVQKYMEEA-KLYKLEMDSFRADRARPARHSLISMEcvaaDNVKDKLTDLTEEYHDLSNRCNLLGD 5221
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSE----EDVYHQLTSERKQRASLKEQMQEIQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5222 RLADLSGKHRQFNDVAFKLLTWLTDM--EGQLSSVKQDAGLSEPQQLQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTN 5299
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQNITVRLqdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5300 SLSGQAAEQQQVAKLQSTMNDLSVRYSTLTKdinshVTQLQAAVTHSQDITQAMNELVSWMDSAEQVVTTQlpislrRPE 5379
Cdd:TIGR00618 651 LQLTLTQERVREHALSIRVLPKELLASRQLA-----LQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY------DRE 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5380 LNAQLQSFSAVDADVTN----HQSALDAVKALANELVKTCELDIARAVE------QRLTSLDEKFSSLQAKCRQRDRDLE 5449
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAredaLNQSLKELMHQARTVLKARTEAHFNNNEevtaalQTGAELSHLAAEIQFFNRLREEDTH 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5450 EVDSSLREFQEKLEqtnlwvHDGilqlDSKELSKLSSDDMKQQLEKLAREKHNRLRTIQEIQVAAEQLLQDPRTGEGEAV 5529
Cdd:TIGR00618 800 LLKTLEAEIGQEIP------SDE----DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
570 580 590
....*....|....*....|....*....|....*...
gi 1397727998 5530 KnlVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENA 5567
Cdd:TIGR00618 870 K--IIQLSDKLNGINQIKIQFDGDALIKFLHEITLYAN 905
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
7198-7320 |
2.51e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 42.20 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7198 MRHNALESVKNAAEELLRQAGDEQDEAVK---DVRQKLEELTKLYKDIQERgrgRQRALEETLAVAEkfwdelhalnssL 7274
Cdd:COG2882 2 KRSFRLQTLLDLAEKEEDEAARELGQAQQaleQAEEQLEQLEQYREEYEQR---LQQKLQQGLSAAQ------------L 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727998 7275 KDLQEALSSVDQpalepeAIREQQEELEALKEDIEASQADFEEVQQ 7320
Cdd:COG2882 67 RNYQQFIARLDE------AIEQQQQQVAQAEQQVEQARQAWLEARQ 106
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2215-2244 |
2.91e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|
gi 1397727998 2215 SITGIVHPKSGARLTVSQAIQNGILDQEKG 2244
Cdd:smart00250 9 AIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4599-4623 |
2.94e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 2.94e-03
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
7078-7735 |
3.25e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7078 EKAKVLKQ---EVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVR-TKVRDRSNSIDQAMQQSAEFTD 7153
Cdd:COG5022 842 LKAEVLIQkfgRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKlVNLELESEIIELKKSLSSDLIE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7154 KLE---NMLDTLTVTAEQVRSAEPISAQPDKLREQI---EENKAMEEDLEMRHNALESvknaaEELLRQAGDEQDEAVKD 7227
Cdd:COG5022 922 NLEfktELIARLKKLLNNIDLEEGPSIEYVKLPELNklhEVESKLKETSEEYEDLLKK-----STILVREGNKANSELKN 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7228 VRQKLEELTKLYKDIQERGRG---RQRALEEtLAVAEKFWDELHALNSSLKDLQEalssvdQPALEPEAIREQQEELEAL 7304
Cdd:COG5022 997 FKKELAELSKQYGALQESTKQlkeLPVEVAE-LQSASKIISSESTELSILKPLQK------LKGLLLLENNQLQARYKAL 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7305 KEDIEASQADFEEVQQTGDT--LLGMVGTTEQPEVQKNVDDAGASLAAISDQYSK--RSQELESALAQAVHF-QDQLMKL 7379
Cdd:COG5022 1070 KLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKlnLLQEISKFLSQLVNTlEPVFQKL 1149
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7380 LVWLQEAEDEFsefePVASEFETIKKQWdelknFKTrvepkNVEIESLNQHVTELTKSSTPEQASVLREPMTQLNIRWNN 7459
Cdd:COG5022 1150 SVLQLELDGLF----WEANLEALPSPPP-----FAA-----LSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFS 1215
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7460 LLtNIGDRQRELQMALLTAGQFDHAHKELKNWMDLVDVtldeiTPVYGDPKLVEIelakLRIVQNDITAHQESVESISKE 7539
Cdd:COG5022 1216 GW-PRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDT-----PASMSNEKLLSL----LNSIDNLLSSYKLEEEVLPAT 1285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7540 AQRLMTSEGIAQAQGLKTKMEDMEktWENIQAKSRaKQDMLEDGLREAQgftgelqdilakINDIEGQLIISKPVGGLPE 7619
Cdd:COG5022 1286 INSLLQYINVGLFNALRTKASSLR--WKSATEVNY-NSEELDDWCREFE------------ISDVDEELEELIQAVKVLQ 1350
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7620 TAKEQLEKFMDVYAELEKLEP-QVQSLNVMGEKLGGKskgpalANLRQnlQHLNQrcdyIRSRACDRKKKLEDAEgmatn 7698
Cdd:COG5022 1351 LLKDDLNKLDELLDACYSLNPaEIQNLKSRYDPADKE------NNLPK--EILKK----IEALLIKQELQLSLEG----- 1413
|
650 660 670
....*....|....*....|....*....|....*..
gi 1397727998 7699 fHGELNKFISWLTDTEKTLNNLQPVSRLVERVTSQIE 7735
Cdd:COG5022 1414 -KDETEVHLSEIFSEEKSLISLDRNSIYKEEVLSSLS 1449
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
8346-8395 |
3.40e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 41.70 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1397727998 8346 GRVTRKEFIEGIISSKFPTSklEMEKVADIFDKDGDGFINYKEFVAALRP 8395
Cdd:COG5126 84 GKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAVRD 131
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6683-7019 |
3.43e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6683 KHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDplttwldaANKRFTALEPHSPDAEgiEHLIQELKKLQ 6762
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD--------EKKQFEKIAEELKGKE--QELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6763 KEVNEHEpamKQLATAGKKLQDYCKgeDVIMIQLKIDGVQKQNGELRSHIEDCL----EQMEEALPLAKHFQEAHAEFLS 6838
Cdd:pfam05483 450 KEIHDLE---IQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNIELTAHCDKLLlenkELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6839 WASKVEPELRALElGVPDEETNIEELANQLTEEMQPLLDIINS--EGAELAEVAPGDAGLRVEDIINRDNKRFDNLRDQI 6916
Cdd:pfam05483 525 CKKQEERMLKQIE-NLEEKEMNLRDELESVREEFIQKGDEVKCklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6917 EKRAQKVQLARQRSSEVVNElgdlvdwfVDADSRLQNQQPIASDLDLLQQQLAEQKvMNEEINNQKVKARDTLSASKKLL 6996
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLELELASAKQK-FEEIIDNYQKEIEDKKISEEKLL 674
|
330 340
....*....|....*....|...
gi 1397727998 6997 SDsaMEDNSAIRNKMDELKQWVD 7019
Cdd:pfam05483 675 EE--VEKAKAIADEAVKLQKEID 695
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7191-7366 |
3.67e-03 |
|
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: 43.37 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7191 AMEEDLEM------RHNALESVKNAAEELLRQAGDEQDEaVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFW 7264
Cdd:COG1579 1 AMPEDLRAlldlqeLDSELDRLEHRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7265 D---------ELHALNSSLKDLQEALSsvdqpALEpEAIREQQEELEALKEDIEASQADFEEVQQTGDtllgmvgtteqp 7335
Cdd:COG1579 80 EqlgnvrnnkEYEALQKEIESLKRRIS-----DLE-DEILELMERIEELEEELAELEAELAELEAELE------------ 141
|
170 180 190
....*....|....*....|....*....|.
gi 1397727998 7336 EVQKNVDDAGASLAAISDQYSKRSQELESAL 7366
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6201-6770 |
3.83e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6201 EDVDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQ 6280
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6281 -------RLGEVQDSLAEATSALNKWENKLAvhnslGLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEvdgGET 6353
Cdd:COG1196 303 diarleeRRRELEERLEELEEELAELEEELE-----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6354 SNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTpvSRDDAELGSQLADMKDFL 6433
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6434 TRLGEKVETLKDLEQQASSLcnAGYVSDPELLKSQVEALSNQHASLTERATQRQSDvvANQHSIQHLTQALNLVWGDIDK 6513
Cdd:COG1196 453 ELEEEEEALLELLAELLEEA--ALLEAALAELLEELAEAAARLLLLLEAEADYEGF--LEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6514 ASST--------LDAMGPAGGNV-----TTVKALQEELKGFVKSTMEPLQKQFESVSRQGQALIKTAVAGSNTTGLETDL 6580
Cdd:COG1196 529 LIGVeaayeaalEAALAAALQNIvveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6581 ESLAERWAGLVEKVAEHekNLDSALLRTGKFQdAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKMVTDRT 6660
Cdd:COG1196 609 READARYYVLGDTLLGR--TLVAARLEAALRR-AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6661 PSMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDplttwldaankrftA 6740
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE--------------E 751
|
570 580 590
....*....|....*....|....*....|
gi 1397727998 6741 LEPHSPDAEGIEHLIQELKKLQKEVNEHEP 6770
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
7025-7370 |
3.99e-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: 44.56 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7025 ANERQSLLEQAVPFARHfheahtelvvWLDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVadrKPIVDRLNKTGTAL 7104
Cdd:COG3096 277 ANERRELSERALELRRE----------LFGARRQLAEEQYRLVEMARELEELSARESDLEQDY---QAASDHLNLVQTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7105 vamcgsKGAEQVQSMLDDdnrrmdnvrtkVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVrsaepisaqpDKLRE 7184
Cdd:COG3096 344 ------RQQEKIERYQED-----------LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV----------DSLKS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7185 QIEEnkaMEEDLEMRH----------NALE-----------SVKNAAEEL--LRQAGDEQDEAVKDVRQKL--------- 7232
Cdd:COG3096 397 QLAD---YQQALDVQQtraiqyqqavQALEkaralcglpdlTPENAEDYLaaFRAKEQQATEEVLELEQKLsvadaarrq 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7233 -----EELTKLYKDIqERGRGRQRALE------ETLAVAEKfwdeLHALNSSLKDLQEALS--------------SVDQP 7287
Cdd:COG3096 474 fekayELVCKIAGEV-ERSQAWQTAREllrryrSQQALAQR----LQQLRAQLAELEQRLRqqqnaerlleefcqRIGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7288 ALEPEAIREQQEELEALKEDIEASQADFEE----VQQTGDTLLGMVGTTEQPE-VQKNVDDAGASLAAISDQYSKRSQEL 7362
Cdd:COG3096 549 LDAAEELEELLAELEAQLEELEEQAAEAVEqrseLRQQLEQLRARIKELAARApAWLAAQDALERLREQSGEALADSQEV 628
|
....*...
gi 1397727998 7363 ESALAQAV 7370
Cdd:COG3096 629 TAAMQQLL 636
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6719-6821 |
4.46e-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: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6719 EFQDVLDPLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYcKGEDVIMIQLKI 6798
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727998 6799 DGVQKQNGELRSHIEDCLEQMEE 6821
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
6215-6783 |
5.53e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6215 LQGVQNEMMKK--SHDRERLNSEgtslvecvdSGKEAIKQQVAVINERwdavNKALSERASHLEDlgqrlgevQDSLAEA 6292
Cdd:pfam05557 11 LSQLQNEKKQMelEHKRARIELE---------KKASALKRQLDRESDR----NQELQKRIRLLEK--------REAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6293 TSALNKWENKLAVHNSLGLSakdpKHINRIKDLLEDTGWLASQLNN-TETMLNSIEVDGGETSNLRDELNKLRGQHQTLQ 6371
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALN----KKLNEKESQLADAREVISCLKNeLSELRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6372 GELSelvaEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTpvsrDDAELgsqLADMKDFLTRLGEKVETLKDLEQQAS 6451
Cdd:pfam05557 146 AKAS----EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE----QDSEI---VKNSKSELARIPELEKELERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6452 SLCNAgyVSDPELLKSQVEALSNQhaslTERATQRQSDVVANQHSIQHLTQALNlVWGDIDKaSSTLDAMGPAGGNVTTV 6531
Cdd:pfam05557 215 HLNEN--IENKLLLKEEVEDLKRK----LEREEKYREEAATLELEKEKLEQELQ-SWVKLAQ-DTGLNLRSPEDLSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6532 KALQEELK-GFVKSTMEPLQKQFESVSRQGQalIKTAVAGSNTTGLETDLESLAERWAGLVEKV--AEHEKNLDSALLrt 6608
Cdd:pfam05557 287 QLQQREIVlKEENSSLTSSARQLEKARRELE--QELAQYLKKIEDLNKKLKRHKALVRRLQRRVllLTKERDGYRAIL-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6609 GKFQDAMA------SLLDWLAETEELVAMQKAPSPEQRVVRAQLQE----QKLVQKMVTDRTPSMKAVQDSGNQLIT--G 6676
Cdd:pfam05557 363 ESYDKELTmsnyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEelggYKQQAQTLERELQALRQQESLADPSYSkeE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6677 LDPAERK--HIESELQQLNSRWEALTKRVVDR----------TAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTAL-EP 6743
Cdd:pfam05557 443 VDSLRRKleTLELERQRLREQKNELEMELERRclqgdydpkkTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLlKK 522
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1397727998 6744 HSPDAEGIEHL-IQELKKLQKEVNEHEpamKQLATAGKKLQ 6783
Cdd:pfam05557 523 LEDDLEQVLRLpETTSTMNFKEVLDLR---KELESAELKNQ 560
|
|
| ElaB |
COG4575 |
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ... |
7190-7262 |
6.25e-03 |
|
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443632 [Multi-domain] Cd Length: 108 Bit Score: 40.31 E-value: 6.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397727998 7190 KAMEEDLEmrhNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEEltkLYKDIQERGRGRQRALEETLAVAEK 7262
Cdd:COG4575 11 EDSKEDLE---ADLKALVDDLEELLKSTADDAGEKAAELREKAEA---ALDEARERLSEAEDAAVERAREAAD 77
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6033-6328 |
6.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6033 RSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEAdckelltwISEAANNLQESEplSSDLDIlreqmrqnRTLQQEL 6112
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE--------RREALQRLAEYS--WDEIDV--------ASAEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6113 SLKEPEIRQLLEkgdklvkeSSPttEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKmamwLQMTE 6192
Cdd:COG4913 671 AELEAELERLDA--------SSD--DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6193 EKLEKMKPEDVDQNtvvhkLKELqgVQNEMMKKSHD--RERLNSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSE 6270
Cdd:COG4913 737 EAAEDLARLELRAL-----LEER--FAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA 809
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727998 6271 RASHLEDLGQRLGE-VQDSLAEATSALNKWENKLAVHNSLGLSAKDPKHINRIKDLLED 6328
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
6866-7472 |
7.50e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6866 NQLTEEMQPLLDIINSEGAELAEVApgdaglRVEDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFV 6945
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNID------YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6946 DADSRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDtvsgsa 7025
Cdd:PRK01156 236 NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN------ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7026 neRQSLLEQAVPFARHFHEAHtelvvwlddvepvlSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTgtalv 7105
Cdd:PRK01156 310 --KKQILSNIDAEINKYHAII--------------KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY----- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7106 amcgSKGAEQVqsmldddNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRS-AEPISAQPDKLRE 7184
Cdd:PRK01156 369 ----LKSIESL-------KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSkVSSLNQRIRALRE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7185 QIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERgRGRQRALEETLAVAE--- 7261
Cdd:PRK01156 438 NLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK-IVDLKKRKEYLESEEink 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7262 --KFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEAlkEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQK 7339
Cdd:PRK01156 517 siNEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL--EDLDSKRTSWLNALAVISLIDIETNRSRSNEIKK 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7340 NVDDAgaslaaisdqySKRSQELESALAQAVHFQDQLMKllvwlqEAEDEFSEFEPVASEFETIKKQWDEL----KNFKT 7415
Cdd:PRK01156 595 QLNDL-----------ESRLQEIEIGFPDDKSYIDKSIR------EIENEANNLNNKYNEIQENKILIEKLrgkiDNYKK 657
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727998 7416 RV------EPKNVEIES-LNQHVTELTKSSTPEQAS------------VLREPMTQLNIRwnnlltnIGDRQRELQ 7472
Cdd:PRK01156 658 QIaeidsiIPDLKEITSrINDIEDNLKKSRKALDDAkanrarlestieILRTRINELSDR-------INDINETLE 726
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
6899-7394 |
7.83e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6899 EDIINRDNKRFDNLRDQIEKRAQKVQLarQRSSEVVNELGDLVDwfvDADSRLQNqqpIASDLDLLQQQLAEQKVMNEEI 6978
Cdd:pfam06160 55 DDIVTKSLPDIEELLFEAEELNDKYRF--KKAKKALDEIEELLD---DIEEDIKQ---ILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6979 NNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVD-TVSGSANERQSLLEQAvpfarhfHEahtelvvwlddve 7057
Cdd:pfam06160 127 KDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEElTESGDYLEAREVLEKL-------EE------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7058 pvlsELDVLSVDADQVKKQQEKAK-VLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVRtkvrd 7136
Cdd:pfam06160 187 ----ETDALEELMEDIPPLYEELKtELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE----- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7137 rsnsIDQAMQQSAEFTDKLENMLDTLT--VTAEQVrSAEPISAQPDKLREQIEENKAMEEDLE-------MRHNALESVK 7207
Cdd:pfam06160 258 ----LDEAEEALEEIEERIDQLYDLLEkeVDAKKY-VEKNLPEIEDYLEHAEEQNKELKEELErvqqsytLNENELERVR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7208 NAAEELlrqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQ- 7286
Cdd:pfam06160 333 GLEKQL-----EELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLe 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7287 -------------PALePEAIREQ----QEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQpEVQKNVDDAGasLA 7349
Cdd:pfam06160 408 lreikrlveksnlPGL-PESYLDYffdvSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYE-KTEELIDNAT--LA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1397727998 7350 AISDQYSKRSQELESALAQAvhfqdqlmkllvwLQEAEDEFSEFE 7394
Cdd:pfam06160 484 EQLIQYANRYRSSNPEVAEA-------------LTEAELLFRNYD 515
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
7132-7369 |
8.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7132 TKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKA----MEEDLEMRHNALESVK 7207
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAeiaeAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7208 NAA---------EELLRQAGDEQD-----EAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwdelhalnsS 7273
Cdd:COG3883 93 RALyrsggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA----------L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7274 LKDLQEALSSVDQpalepeAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISD 7353
Cdd:COG3883 163 KAELEAAKAELEA------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|....*.
gi 1397727998 7354 QYSKRSQELESALAQA 7369
Cdd:COG3883 237 AAAAAAAASAAGAGAA 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
6964-7453 |
9.40e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 6964 LQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSlLEQAVPFARHFH 7043
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA-RNKAEKQRRDLG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7044 EahtelvvwldDVEPVLSEL-DVLsvdaDQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLD- 7121
Cdd:pfam01576 299 E----------ELEALKTELeDTL----DTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEq 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7122 -DDNRRMDNVRTKVR-----DRSN------SIDQAMQQSAEFTDKLENMLDTLTVTA-EQVRSAEPISAQPDKLREQIEE 7188
Cdd:pfam01576 365 lEQAKRNKANLEKAKqalesENAElqaelrTLQQAKQDSEHKRKKLEGQLQELQARLsESERQRAELAEKLSKLQSELES 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7189 NKAMEEDLEMRhnALESVKNAAeELLRQAGDEQDEAVKDVRQKLEELTKLyKDIQERGRGRQRALEETLAVAEKFWDELH 7268
Cdd:pfam01576 445 VSSLLNEAEGK--NIKLSKDVS-SLESQLQDTQELLQEETRQKLNLSTRL-RQLEDERNSLQEQLEEEEEAKRNVERQLS 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7269 ALNSSLKD----LQEALSSVDqpALEpEAIREQQEELEALKEDIEASQADFEE-------VQQTGDTLLGMVGTTEQ--- 7334
Cdd:pfam01576 521 TLQAQLSDmkkkLEEDAGTLE--ALE-EGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDLDHQRQlvs 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 7335 --PEVQKNVDDAGASLAAISDQYskrSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVAsefETIKKQWDELKN 7412
Cdd:pfam01576 598 nlEKKQKKFDQMLAEEKAISARY---AEERDRAEAEAREKETRALSLARALEEALEAKEELERTN---KQLRAEMEDLVS 671
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1397727998 7413 FKTRVePKNVeieslnqHVTELTKSSTPEQASVLREPMTQL 7453
Cdd:pfam01576 672 SKDDV-GKNV-------HELERSKRALEQQVEEMKTQLEEL 704
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
198-279 |
9.57e-03 |
|
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: 39.59 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 198 KIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLEL-AFTVAE--KEFGVTRLLDPEDVDVPNPDEksILTYV 274
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPEDIVSGNPRL--NLAFV 109
|
....*
gi 1397727998 275 SSLYD 279
Cdd:cd21218 110 ATLFN 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
5337-5581 |
9.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5337 TQLQAAVTHSQDITQAMNELVswmDSAEQVVTtqlpisLRRpeLNAQLQSFSAVDADVTNHQSALDAVKALANELvktce 5416
Cdd:COG4913 225 EAADALVEHFDDLERAHEALE---DAREQIEL------LEP--IRELAERYAAARERLAELEYLRAALRLWFAQR----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5417 ldIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEKleqtnlwvhdgILQLDSKELSKLssddmKQQLEKL 5496
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQL-----EREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727998 5497 AREKHNRLRTIQEIQVAAEQL-LQDPrtGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWL 5575
Cdd:COG4913 351 ERELEERERRRARLEALLAALgLPLP--ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
....*.
gi 1397727998 5576 SQMEAR 5581
Cdd:COG4913 429 ASLERR 434
|
|
| |
