|
Name |
Accession |
Description |
Interval |
E-value |
| EFh_DMD |
cd16246 |
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ... |
1781-1942 |
1.80e-113 |
|
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.
Pssm-ID: 320004 Cd Length: 162 Bit Score: 356.65 E-value: 1.80e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1781 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 1860
Cdd:cd16246 1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1861 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 1940
Cdd:cd16246 81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160
|
..
gi 1677502240 1941 MR 1942
Cdd:cd16246 161 MR 162
|
|
| EF-hand_2 |
pfam09068 |
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ... |
1745-1863 |
9.29e-57 |
|
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.
Pssm-ID: 462668 Cd Length: 123 Bit Score: 192.75 E-value: 9.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1745 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 1822
Cdd:pfam09068 1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1677502240 1823 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 1863
Cdd:pfam09068 81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
|
|
| ZZ_dystrophin |
cd02334 |
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
1967-2015 |
4.11e-30 |
|
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.
Pssm-ID: 239074 Cd Length: 49 Bit Score: 113.99 E-value: 4.11e-30
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677502240 1967 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 2015
Cdd:cd02334 1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
761-976 |
1.64e-23 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 100.98 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 761 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 839
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 840 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 919
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 920 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 976
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1346-1589 |
1.16e-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: 92.51 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1346 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 1425
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1426 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 1505
Cdd:cd00176 72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1506 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 1585
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209
|
....
gi 1677502240 1586 DETL 1589
Cdd:cd00176 210 EEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1128-1344 |
2.22e-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: 91.74 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1128 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 1207
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1208 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 1287
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1288 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 1344
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| ZZ |
pfam00569 |
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1963-2008 |
6.17e-17 |
|
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.
Pssm-ID: 395451 Cd Length: 45 Bit Score: 76.37 E-value: 6.17e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677502240 1963 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 2008
Cdd:pfam00569 1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
|
|
| ZnF_ZZ |
smart00291 |
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1964-2007 |
1.49e-14 |
|
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.
Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 69.39 E-value: 1.49e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677502240 1964 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 2007
Cdd:smart00291 2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
779-1474 |
4.33e-14 |
|
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: 78.56 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 779 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 858
Cdd:TIGR02168 212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 859 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 932
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 933 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 1012
Cdd:TIGR02168 363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1013 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 1090
Cdd:TIGR02168 436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1091 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 1162
Cdd:TIGR02168 515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1163 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 1208
Cdd:TIGR02168 595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1209 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 1283
Cdd:TIGR02168 673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1284 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 1360
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1361 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 1440
Cdd:TIGR02168 833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750
....*....|....*....|....*....|....
gi 1677502240 1441 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 1474
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1590-1696 |
9.13e-12 |
|
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: 63.49 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1590 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 1669
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1677502240 1670 LSTLEDLNTRWKLLQVAVEDRVRQLHE 1696
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
763-863 |
2.93e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 61.96 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 763 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 841
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1677502240 842 GSLNLRWQEVCKQLSDRKKRLE 863
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1591-1701 |
1.07e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 63.62 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1591 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 1670
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
|
90 100 110
....*....|....*....|....*....|.
gi 1677502240 1671 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 1701
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
760-864 |
1.88e-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: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 760 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 837
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1677502240 838 QEKLGSLNLRWQEVCKQLSDRKKRLEE 864
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1131-1232 |
1.98e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 59.65 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1131 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 1210
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1677502240 1211 ERIQNQWDEVQEHLQNRRQQLN 1232
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
436-624 |
8.28e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.92 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 436 LKELEQFNSDIQKLLEPLEAEIQQgvnLKEEDFNKDMNEdNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQTKHN 515
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALL---KKHEALEAELAA-HEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 516 ALKDLrSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQ 588
Cdd:cd00176 90 ELREL-AEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLesveellKKHKELEEELEAHEPRLKSLNEL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1677502240 589 AEGLSEDG---AAMAVEPTQIQLSKRWREIESKFAQFRR 624
Cdd:cd00176 169 AEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
29-594 |
1.26e-09 |
|
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: 64.30 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 29 QETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ--GKEAAQRVLSQIDVAQKK 106
Cdd:TIGR01612 1169 EEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLsyGKNLGKLFLEKIDEEKKK 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 107 LQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKSLSEVKSevemviktgRQIV 186
Cdd:TIGR01612 1238 SEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNISHDDDKD---------HHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 187 QKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAatdmeltkrsavegmpsNLDS 265
Cdd:TIGR01612 1293 SKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-----------------NIYN 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 266 EVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEWLNllleyQKHMETFDQNVD 345
Cdd:TIGR01612 1354 ILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIESTLD-----DKDIDECIKKIK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 346 HITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAiSH 425
Cdd:TIGR01612 1426 ELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDK-SK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 426 RIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQriTDER 498
Cdd:TIGR01612 1497 GCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQK--IKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 499 KREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDR 573
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEKKISSFSIDSQDTELKENGD 1650
|
570 580
....*....|....*....|.
gi 1677502240 574 ELQKKKEELNAVRRQAEGLSE 594
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIED 1671
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1226-1342 |
1.66e-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: 57.33 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1226 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 1305
Cdd:pfam00435 1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1677502240 1306 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 1342
Cdd:pfam00435 69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-620 |
3.94e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 3 ARKLRNLSYKKAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI 78
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 79 -SLEEMKKHNQGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQS 156
Cdd:PTZ00121 1296 kKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 157 QLNhcvnlyKSLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRK 234
Cdd:PTZ00121 1375 EAK------KKADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKK 1445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 235 EMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllns 314
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK------ 1517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 315 nwiAVTSRAEEWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQA 394
Cdd:PTZ00121 1518 ---AEEAKKADEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEA 1586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 395 ANLMANRGDHCRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDM 472
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIK 1662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 473 NEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDI 552
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677502240 553 EKKLASLPEPRDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 620
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
1715-1744 |
4.62e-09 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 53.69 E-value: 4.62e-09
10 20 30
....*....|....*....|....*....|
gi 1677502240 1715 GPWERAISPNKVPYYINHETQTTCWDHPKM 1744
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1348-1457 |
1.02e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 54.64 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1348 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 1427
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
|
90 100 110
....*....|....*....|....*....|
gi 1677502240 1428 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 1457
Cdd:smart00150 72 AEEIEERLEELNERWEELKELAEERRQKLE 101
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
1712-1744 |
1.54e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 52.22 E-value: 1.54e-08
10 20 30
....*....|....*....|....*....|...
gi 1677502240 1712 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 1744
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
533-635 |
1.75e-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: 54.25 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 533 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 610
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
|
90 100
....*....|....*....|....*
gi 1677502240 611 RWREIESKFAQFRRLNFAQIHTVRE 635
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1593-1694 |
2.38e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.87 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1593 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 1672
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
|
90 100
....*....|....*....|..
gi 1677502240 1673 LEDLNTRWKLLQVAVEDRVRQL 1694
Cdd:smart00150 79 LEELNERWEELKELAEERRQKL 100
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
1716-1742 |
5.99e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 50.20 E-value: 5.99e-08
10 20
....*....|....*....|....*..
gi 1677502240 1716 PWERAISPNKVPYYINHETQTTCWDHP 1742
Cdd:pfam00397 4 GWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
335-432 |
7.61e-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: 52.32 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 335 KHMETFDQNVDHITKWIIQADTLLDESEKKK----PQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANrGDHCRKLVE 410
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKdlesVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
|
90 100
....*....|....*....|..
gi 1677502240 411 PQISELNHRFAAISHRIKTGKA 432
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQ 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
123-332 |
2.29e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 53.60 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 123 FEQRLQESKMILDEVKMHLPALETKSVEQEVvQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPkELDERVT 202
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 203 ALKLHYNELGAKVTERKQQLEKCLKLSRKMRkEMNVLTEWLAATDMELTKRSAVEGMPSnLDSEVAWGKATQKEIEKQKV 282
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1677502240 283 HLKSITEVGEAL-KTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLE 332
Cdd:cd00176 161 RLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
353-627 |
9.06e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 353 QADTLLDESEKKKPQQKE--DVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVE--PQISELNHRFAAISHRIK 428
Cdd:COG1340 16 KIEELREEIEELKEKRDElnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKElkEERDELNEKLNELREELD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 429 TGKASIPLKELEQFNSD-IQKLLEPLEAEIQqgvnlkeedfNKDMNEDNEgtvKELLQRGDNLQQRITDERKREEIKIKQ 507
Cdd:COG1340 96 ELRKELAELNKAGGSIDkLRKEIERLEWRQQ----------TEVLSPEEE---KELVEKIKELEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 508 QLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER--KIKEIDRELQKKKEELNAV 585
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqeKADELHEEIIELQKELREL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1677502240 586 RRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNF 627
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTT 284
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
536-618 |
1.24e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 536 YQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDG--AAMAVEPTQI 606
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLesveallKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
|
90
....*....|..
gi 1677502240 607 QLSKRWREIESK 618
Cdd:smart00150 81 ELNERWEELKEL 92
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1133-1437 |
1.43e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1133 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 1205
Cdd:COG1196 232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1206 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 1280
Cdd:COG1196 309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1281 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 1360
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1361 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 1437
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
534-758 |
1.63e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.21 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 534 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 606
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 607 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 684
Cdd:cd00176 81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677502240 685 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 758
Cdd:cd00176 139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1145-1677 |
1.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1145 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRrpqLEELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEH 1223
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1224 LQNRRQQLNEMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALK 1302
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1303 LLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAWLTEAETTANVLQDATRKERLLE 1382
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1383 DSKGVKELMKQWQDLQGEIEAHTDVYhnLDENSQKILRSLEGSDDAV---LLQRRLDNMNFKwselrkkSLNIRSHLEAS 1459
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQNIVVEDDEVAAAAieyLKAAKAGRATFL-------PLDKIRARAAL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1460 SDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEpvimsTLETVRIFLTEQPLEGLEK 1539
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1540 LYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIkgswqpV 1619
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677502240 1620 GDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGiqlsPYNLSTLEDLN 1677
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG----PVNLLAIEEYE 791
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1284 |
2.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 849 QEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI------------PLEPGKEQQLKEKLEQVKLLVEE- 915
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkeelerlkkrltGLTPEKLEKELEELEKAKEEIEEe 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 916 ---LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQDKLENKLKqtnlqwikvsralpEKQGEIEAQIKDL 979
Cdd:PRK03918 407 iskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHRKELLEEYT--------------AELKRIEKELKEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 980 GQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFDVKETEiavqAKQPDVEEILSKGQHLYKEKPATQPV 1055
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1056 KRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtlvtqpvvtkETAISKLEmpsslmlevpalaDFNRAW 1135
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----------EERLKELE-------------PFYNEY 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1136 TELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRRPQLEELITA--------AQNLKNKTSNQEARtiIT 1207
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELRKELEELEKKyseeeyeeLREEYLELSRELAG--LR 679
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1208 DRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVLGQARAKLEswkegpytvdAIQKKITETKQLAK 1284
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KLEKALERVE----------ELREKVKKYKALLK 738
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1345-1447 |
3.29e-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: 45.00 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1345 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 1424
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
|
90 100
....*....|....*....|...
gi 1677502240 1425 SDDAVLLQRRLDNMNFKWSELRK 1447
Cdd:pfam00435 72 HYASEEIQERLEELNERWEQLLE 94
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
152-223 |
2.04e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.70 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677502240 152 EVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKkQTENPKELDERVTALKLHYNELGAKVTERKQQLE 223
Cdd:smart00150 31 ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1142-1256 |
6.62e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1142 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 1220
Cdd:PRK00409 497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
|
90 100 110
....*....|....*....|....*....|....*...
gi 1677502240 1221 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQAR 1256
Cdd:PRK00409 557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR 594
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
816-1012 |
2.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 816 RTLNATGEEIIQQSSKTDASILQEKLGSLNlrwqevcKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIple 895
Cdd:COG3206 152 AVANALAEAYLEQNLELRREEARKALEFLE-------EQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 896 pgkeQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDkLENKLKQTNLQWIKVS----------RAL 965
Cdd:COG3206 222 ----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSarytpnhpdvIAL 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1677502240 966 PEKQGEIEAQIKDlgQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 1012
Cdd:COG3206 297 RAQIAALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EFh_DMD |
cd16246 |
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ... |
1781-1942 |
1.80e-113 |
|
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.
Pssm-ID: 320004 Cd Length: 162 Bit Score: 356.65 E-value: 1.80e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1781 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 1860
Cdd:cd16246 1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1861 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 1940
Cdd:cd16246 81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160
|
..
gi 1677502240 1941 MR 1942
Cdd:cd16246 161 MR 162
|
|
| EFh_DMD_like |
cd16242 |
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ... |
1781-1942 |
8.61e-104 |
|
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.
Pssm-ID: 320000 Cd Length: 163 Bit Score: 329.20 E-value: 8.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1781 SLSAACDALDQHNLK-QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 1859
Cdd:cd16242 1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1860 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 1939
Cdd:cd16242 81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160
|
...
gi 1677502240 1940 WMR 1942
Cdd:cd16242 161 WLK 163
|
|
| EFh_UTRO |
cd16247 |
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ... |
1782-1942 |
2.45e-84 |
|
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs.
Pssm-ID: 320005 Cd Length: 162 Bit Score: 273.31 E-value: 2.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1782 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 1861
Cdd:cd16247 2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1862 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 1941
Cdd:cd16247 82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161
|
.
gi 1677502240 1942 R 1942
Cdd:cd16247 162 R 162
|
|
| EFh_DRP-2 |
cd16248 |
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ... |
1781-1941 |
1.77e-80 |
|
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises only two spectrin repeats (SRs) and a WW domain.
Pssm-ID: 320006 Cd Length: 162 Bit Score: 262.42 E-value: 1.77e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1781 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 1860
Cdd:cd16248 1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1861 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 1940
Cdd:cd16248 81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160
|
.
gi 1677502240 1941 M 1941
Cdd:cd16248 161 M 161
|
|
| EFh_DMD_DYTN_DTN |
cd15901 |
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ... |
1782-1941 |
4.68e-68 |
|
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.
Pssm-ID: 319999 Cd Length: 163 Bit Score: 226.77 E-value: 4.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1782 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 1860
Cdd:cd15901 2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1861 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 1940
Cdd:cd15901 82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161
|
.
gi 1677502240 1941 M 1941
Cdd:cd15901 162 L 162
|
|
| EF-hand_2 |
pfam09068 |
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ... |
1745-1863 |
9.29e-57 |
|
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.
Pssm-ID: 462668 Cd Length: 123 Bit Score: 192.75 E-value: 9.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1745 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 1822
Cdd:pfam09068 1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1677502240 1823 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 1863
Cdd:pfam09068 81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
|
|
| EF-hand_3 |
pfam09069 |
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ... |
1867-1958 |
1.03e-49 |
|
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.
Pssm-ID: 462669 Cd Length: 90 Bit Score: 171.33 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1867 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 1946
Cdd:pfam09069 1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78
|
90
....*....|..
gi 1677502240 1947 SMVWLPVLHRVA 1958
Cdd:pfam09069 79 SLVWLPVLHRLA 90
|
|
| ZZ_dystrophin |
cd02334 |
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
1967-2015 |
4.11e-30 |
|
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.
Pssm-ID: 239074 Cd Length: 49 Bit Score: 113.99 E-value: 4.11e-30
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1677502240 1967 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 2015
Cdd:cd02334 1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
761-976 |
1.64e-23 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 100.98 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 761 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 839
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 840 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 919
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 920 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 976
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| EFh_DAH |
cd16245 |
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ... |
1781-1941 |
1.21e-21 |
|
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.
Pssm-ID: 320003 [Multi-domain] Cd Length: 164 Bit Score: 93.90 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1781 SLSAACDALDQHNLKQND-----QPMDILQIINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 1855
Cdd:cd16245 1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1856 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 1935
Cdd:cd16245 78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157
|
....*.
gi 1677502240 1936 LFLDWM 1941
Cdd:cd16245 158 QFIGWW 163
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1346-1589 |
1.16e-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: 92.51 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1346 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 1425
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1426 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 1505
Cdd:cd00176 72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1506 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 1585
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209
|
....
gi 1677502240 1586 DETL 1589
Cdd:cd00176 210 EEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1128-1344 |
2.22e-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: 91.74 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1128 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 1207
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1208 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 1287
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1288 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 1344
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| EFh_DTN |
cd16244 |
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ... |
1800-1941 |
5.26e-19 |
|
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrobrevins contain one or two syntrophin binding sites (SBSs).
Pssm-ID: 320002 [Multi-domain] Cd Length: 161 Bit Score: 86.14 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1800 PMDILQIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLF 1875
Cdd:cd16244 22 ELSVSRLETLLSSIYyqlnKRLPTTHQ--IDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTLCAGKLVDKLRYIF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677502240 1876 KQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCFQfANNKPEIEAalFLDWM 1941
Cdd:cd16244 100 SQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFP-GQSKVTVND--FLDVM 160
|
|
| ZZ |
pfam00569 |
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1963-2008 |
6.17e-17 |
|
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.
Pssm-ID: 395451 Cd Length: 45 Bit Score: 76.37 E-value: 6.17e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677502240 1963 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 2008
Cdd:pfam00569 1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
|
|
| ZnF_ZZ |
smart00291 |
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1964-2007 |
1.49e-14 |
|
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.
Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 69.39 E-value: 1.49e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677502240 1964 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 2007
Cdd:smart00291 2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
779-1474 |
4.33e-14 |
|
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: 78.56 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 779 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 858
Cdd:TIGR02168 212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 859 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 932
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 933 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 1012
Cdd:TIGR02168 363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1013 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 1090
Cdd:TIGR02168 436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1091 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 1162
Cdd:TIGR02168 515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1163 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 1208
Cdd:TIGR02168 595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1209 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 1283
Cdd:TIGR02168 673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1284 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 1360
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1361 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 1440
Cdd:TIGR02168 833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750
....*....|....*....|....*....|....
gi 1677502240 1441 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 1474
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1240-1459 |
1.60e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 71.71 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1240 QWLEAKEEAEQVLGQARAKLESWkEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSaDDTRKVHMIT 1319
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1320 ENINASWRSIHKRVSEREAALEETHRLLQQFpLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQG 1399
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-------SEDLGKDLESVEELLKKHKELEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1400 EIEAHTDVYHNLDENSQKiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEAS 1459
Cdd:cd00176 154 ELEAHEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
667-864 |
3.07e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 68.24 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 667 LLEVEQLLNAPDLcAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHsKKTAALQSATPVERVKLQEALSQLDFQWEKVNK 746
Cdd:cd00176 16 LSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALN-ELGEQLIEEGHPDAEEIQERLEELNQRWEELRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 747 MYKDRQGRFDRSVEKWRRFHyDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEI 825
Cdd:cd00176 94 LAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLkKHKELEEELEAHEPRLKSLNELAEEL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1677502240 826 IQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEE 864
Cdd:cd00176 173 LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| EFh_DYTN |
cd16243 |
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ... |
1810-1942 |
6.59e-12 |
|
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.
Pssm-ID: 320001 Cd Length: 163 Bit Score: 65.87 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1810 LTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFK----QVASSTGFC 1885
Cdd:cd16243 31 LERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGGSSGSI 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1886 DQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 1942
Cdd:cd16243 110 TRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1462-1698 |
6.93e-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: 67.09 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1462 QWKRLHLSLQELLVWLQLKDDELSRQAPiGGDFPAVQKQNDVHRAFKRELKTKEPVImstletvriflteqplEGLEKLY 1541
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERV----------------EALNELG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1542 QEPRELPPEERAQnvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEAtDELDLKLRQAEVIKGSWQPVGD 1621
Cdd:cd00176 64 EQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677502240 1622 LliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL-STLEDLNTRWKLLQVAVEDRVRQLHEAH 1698
Cdd:cd00176 138 L--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIeEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1590-1696 |
9.13e-12 |
|
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: 63.49 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1590 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 1669
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1677502240 1670 LSTLEDLNTRWKLLQVAVEDRVRQLHE 1696
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
763-863 |
2.93e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 61.96 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 763 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 841
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1677502240 842 GSLNLRWQEVCKQLSDRKKRLE 863
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1591-1701 |
1.07e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 63.62 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1591 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 1670
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
|
90 100 110
....*....|....*....|....*....|.
gi 1677502240 1671 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 1701
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
760-864 |
1.88e-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: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 760 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 837
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1677502240 838 QEKLGSLNLRWQEVCKQLSDRKKRLEE 864
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1131-1232 |
1.98e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 59.65 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1131 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 1210
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1677502240 1211 ERIQNQWDEVQEHLQNRRQQLN 1232
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| EFh_DTNB |
cd16250 |
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ... |
1816-1941 |
4.06e-10 |
|
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs).
Pssm-ID: 320008 Cd Length: 161 Bit Score: 60.81 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1816 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 1895
Cdd:cd16250 42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1677502240 1896 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 1941
Cdd:cd16250 120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160
|
|
| EFh_DTNA |
cd16249 |
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ... |
1810-1923 |
4.79e-10 |
|
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).
Pssm-ID: 320007 Cd Length: 161 Bit Score: 60.30 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1810 LTTIYDRLEQE--HNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQ 1887
Cdd:cd16249 32 LSTIFYQLNKRmpTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVMVY 111
|
90 100 110
....*....|....*....|....*....|....*.
gi 1677502240 1888 RRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCF 1923
Cdd:cd16249 112 GRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 145
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
436-624 |
8.28e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.92 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 436 LKELEQFNSDIQKLLEPLEAEIQQgvnLKEEDFNKDMNEdNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQTKHN 515
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALL---KKHEALEAELAA-HEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 516 ALKDLrSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQ 588
Cdd:cd00176 90 ELREL-AEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLesveellKKHKELEEELEAHEPRLKSLNEL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1677502240 589 AEGLSEDG---AAMAVEPTQIQLSKRWREIESKFAQFRR 624
Cdd:cd00176 169 AEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
29-594 |
1.26e-09 |
|
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: 64.30 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 29 QETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ--GKEAAQRVLSQIDVAQKK 106
Cdd:TIGR01612 1169 EEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLsyGKNLGKLFLEKIDEEKKK 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 107 LQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKSLSEVKSevemviktgRQIV 186
Cdd:TIGR01612 1238 SEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNISHDDDKD---------HHII 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 187 QKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAatdmeltkrsavegmpsNLDS 265
Cdd:TIGR01612 1293 SKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-----------------NIYN 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 266 EVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEWLNllleyQKHMETFDQNVD 345
Cdd:TIGR01612 1354 ILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIESTLD-----DKDIDECIKKIK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 346 HITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAiSH 425
Cdd:TIGR01612 1426 ELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDK-SK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 426 RIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQriTDER 498
Cdd:TIGR01612 1497 GCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQK--IKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 499 KREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDR 573
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEKKISSFSIDSQDTELKENGD 1650
|
570 580
....*....|....*....|.
gi 1677502240 574 ELQKKKEELNAVRRQAEGLSE 594
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIED 1671
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1226-1342 |
1.66e-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: 57.33 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1226 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 1305
Cdd:pfam00435 1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1677502240 1306 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 1342
Cdd:pfam00435 69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
869-974 |
2.63e-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: 56.56 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 869 LSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLE 948
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE---GHYASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1677502240 949 NKLKQTNLQWIKVSRALPEKQGEIEA 974
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-620 |
3.94e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 3 ARKLRNLSYKKAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI 78
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 79 -SLEEMKKHNQGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQS 156
Cdd:PTZ00121 1296 kKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 157 QLNhcvnlyKSLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRK 234
Cdd:PTZ00121 1375 EAK------KKADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKK 1445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 235 EMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllns 314
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK------ 1517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 315 nwiAVTSRAEEWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQA 394
Cdd:PTZ00121 1518 ---AEEAKKADEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEA 1586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 395 ANLMANRGDHCRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDM 472
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIK 1662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 473 NEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDI 552
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677502240 553 EKKLASLPEPRDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 620
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
1715-1744 |
4.62e-09 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 53.69 E-value: 4.62e-09
10 20 30
....*....|....*....|....*....|
gi 1677502240 1715 GPWERAISPNKVPYYINHETQTTCWDHPKM 1744
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1348-1457 |
1.02e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 54.64 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1348 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 1427
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
|
90 100 110
....*....|....*....|....*....|
gi 1677502240 1428 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 1457
Cdd:smart00150 72 AEEIEERLEELNERWEELKELAEERRQKLE 101
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
1712-1744 |
1.54e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 52.22 E-value: 1.54e-08
10 20 30
....*....|....*....|....*....|...
gi 1677502240 1712 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 1744
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
533-635 |
1.75e-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: 54.25 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 533 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 610
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
|
90 100
....*....|....*....|....*
gi 1677502240 611 RWREIESKFAQFRRLNFAQIHTVRE 635
Cdd:pfam00435 81 RLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1593-1694 |
2.38e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.87 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1593 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 1672
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
|
90 100
....*....|....*....|..
gi 1677502240 1673 LEDLNTRWKLLQVAVEDRVRQL 1694
Cdd:smart00150 79 LEELNERWEELKELAEERRQKL 100
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
1716-1742 |
5.99e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 50.20 E-value: 5.99e-08
10 20
....*....|....*....|....*..
gi 1677502240 1716 PWERAISPNKVPYYINHETQTTCWDHP 1742
Cdd:pfam00397 4 GWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
335-432 |
7.61e-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: 52.32 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 335 KHMETFDQNVDHITKWIIQADTLLDESEKKK----PQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANrGDHCRKLVE 410
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKdlesVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
|
90 100
....*....|....*....|..
gi 1677502240 411 PQISELNHRFAAISHRIKTGKA 432
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQ 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
227-332 |
9.90e-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: 51.94 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 227 KLSRKMRKEMNVLTEWLAATDMELTKRSaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVE 306
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1677502240 307 DKLSLLNSNWIAVTSRAEEWLNLLLE 332
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-592 |
1.56e-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: 56.99 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 12 KKAVRRQKLLEQSIQSA----QETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEmkKHN 87
Cdd:TIGR02168 305 QILRERLANLERQLEELeaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE--QLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 88 QGKEAAQRVLSQIDVAQKKLQD-VSMKFRLFQKPANFEQRLQESKMILDEVKMHLPA--LETKSVEQEVVQSQLNHCVNL 164
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERlEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeLEELEEELEELQEELERLEEA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 165 YKSLSEVKSEVEMVIKTGRQIVQKKQT---------ENPKELDERVTALKLHYNELG----------------------- 212
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQArldslerlqENLEGFSEGVKALLKNQSGLSgilgvlselisvdegyeaaieaa 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 213 ------AKVTERKQQLEKC---LKLSRKMRKEMNVLTEW----LAATDMELTKRsaVEGMPSNLDSEVAWGKATQKEIEK 279
Cdd:TIGR02168 543 lggrlqAVVVENLNAAKKAiafLKQNELGRVTFLPLDSIkgteIQGNDREILKN--IEGFLGVAKDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 280 QKVHLKSITEVGEAL--KTVLGKKETLVEDKLSLLNSNWIaVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTL 357
Cdd:TIGR02168 621 LLGGVLVVDDLDNALelAKKLRPGYRIVTLDGDLVRPGGV-ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 358 LDESEKKKpQQKEDVLKRLKAELNDIRPKVDSTRDQAANL---------MANRGDHCRKLVEPQISELNHRFAAISHRIK 428
Cdd:TIGR02168 700 LAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLeaeveqleeRIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 429 TGKAsiplkELEQFNSDIQKLLEPLEAEIQQGVNLKEEdfnkdmnednegtVKELLQRGDNLQQRITDERKReeIKIKQQ 508
Cdd:TIGR02168 779 EAEA-----EIEELEAQIEQLKEELKALREALDELRAE-------------LTLLNEEAANLRERLESLERR--IAATER 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 509 LLQTKHNALKDLRSQRRKKALEISHQWYQY---KRQADDLLKCLDDIEKKLASLPEPRD---------ERKIKEIDRELQ 576
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERASLEEALALLRSELEelseelrelESKRSELRRELE 918
|
650
....*....|....*.
gi 1677502240 577 KKKEELNAVRRQAEGL 592
Cdd:TIGR02168 919 ELREKLAQLELRLEGL 934
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
123-332 |
2.29e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 53.60 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 123 FEQRLQESKMILDEVKMHLPALETKSVEQEVvQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPkELDERVT 202
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 203 ALKLHYNELGAKVTERKQQLEKCLKLSRKMRkEMNVLTEWLAATDMELTKRSAVEGMPSnLDSEVAWGKATQKEIEKQKV 282
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1677502240 283 HLKSITEVGEAL-KTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLE 332
Cdd:cd00176 161 RLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| ZZ |
cd02249 |
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1969-2015 |
2.45e-07 |
|
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.
Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 48.97 E-value: 2.45e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677502240 1969 CNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRvaKGHKMHYPMVEY 2015
Cdd:cd02249 3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1022-1235 |
3.48e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 53.22 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1022 KETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtl 1100
Cdd:cd00176 43 EALEAELAAHEERVEALNELGEQLIEEGHpDAEEIQERLEELNQRWEELRELAEERRQR--------------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1101 vtqpvvtketaisklempsslMLEVPALADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRR 1180
Cdd:cd00176 102 ---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1677502240 1181 PQLEELITAAQNLKNKtSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEML 1235
Cdd:cd00176 160 PRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
721-1562 |
5.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 721 SATPVERVKLQEALSQLDFQWEKVNKMYKDrqgrFDRSVEKWRRFHYDIKIFNQWL----TEAEQFLRKTQIPENWEHAK 796
Cdd:TIGR02169 149 SMSPVERRKIIDEIAGVAEFDRKKEKALEE----LEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 797 YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDAsiLQEKLGSLNLRWQEVCKQLSDR--------KKRLEEQKNI 868
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE--LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 869 LSEFQRDLNEFVLWLEEADNiasiplepgKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLE 948
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEE---------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE---LKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 949 NKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAV 1028
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1029 QAKQPDVEEI---LSK-GQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQP 1104
Cdd:TIGR02169 451 KKQEWKLEQLaadLSKyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1105 VVTKETAISKLEMPSSLMLEVPALADFNRA-------------------WTELTDWLSLLDqvIKSQRVMVGDLEDINEM 1165
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNRLNNVVVEDDAVAkeaiellkrrkagratflpLNKMRDERRDLS--ILSEDGVIGFAVDLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1166 ----------IIKQKATMQDLEQRRPQLEE--LITAAQNL------------------KNKTSNQEARTIITDRIERIQN 1215
Cdd:TIGR02169 609 dpkyepafkyVFGDTLVVEDIEAARRLMGKyrMVTLEGELfeksgamtggsraprggiLFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1216 QWDEVQE---HLQNRRQQLNEMLKDSTQWLEAKE-EAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLR---Q 1288
Cdd:TIGR02169 689 ELSSLQSelrRIENRLDELSQELSDASRKIGEIEkEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1289 WQTNVDVANDLALKLLRDysaddtRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAwltEAEtta 1368
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEA------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--LTLEKEYL---EKE--- 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1369 nvLQDATRKERLLEDSKgvKELMKQWQDLQGEIEAHTDVYhnldENSQKILRSLEGSddAVLLQRRLDNMNFKWSELRKK 1448
Cdd:TIGR02169 835 --IQELQEQRIDLKEQI--KSIEKEIENLNGKKEELEEEL----EELEAALRDLESR--LGDLKKERDELEAQLRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1449 SLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTL----ET 1524
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIqeyeEV 984
|
890 900 910
....*....|....*....|....*....|....*...
gi 1677502240 1525 VRIFLTEQplEGLEKLYQEPRELppEERAQNVTRLLRK 1562
Cdd:TIGR02169 985 LKRLDELK--EKRAKLEEERKAI--LERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
942-1676 |
6.87e-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: 55.06 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 942 EEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ--PNQEGPF 1019
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1020 DVKETEIAVQAKQPD--------VEEILSKGQHLYKEKPATQPVKR-KLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTI 1090
Cdd:TIGR02168 319 EELEAQLEELESKLDelaeelaeLEEKLEELKEELESLEAELEELEaELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1091 GASPTQTVTLVTQPVVTKETAISKLEmpssLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQK 1170
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIE----ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1171 ATMQDLEQRRPQLEELITAAQNLKNKTS-----------NQEARTIITDRIE---RIQNQWD-EVQEHLQNRRQQLneML 1235
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEgfsegvkallkNQSGLSGILGVLSeliSVDEGYEaAIEAALGGRLQAV--VV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1236 KDSTQWLEAKEEAEQ---------VLGQARA------KLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDL- 1299
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQnelgrvtflPLDSIKGteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLd 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1300 -ALKLLRDYSAdDTRKVHMITENINASWRSIHKRVS------EREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQ 1372
Cdd:TIGR02168 633 nALELAKKLRP-GYRIVTLDGDLVRPGGVITGGSAKtnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1373 DATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGsddavlLQRRLDNMNFKWSELRKKSL 1450
Cdd:TIGR02168 712 EELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE------LEERLEEAEEELAEAEAEIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1451 NIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQApiggdFPAVQKQNDVHRAfKRELKTKEPVIMSTLETVrIFLT 1530
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR-----ERLESLERRIAAT-ERRLEDLEEQIEELSEDI-ESLA 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1531 EQplegLEKLYQEPRELPPE-ERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQA 1609
Cdd:TIGR02168 859 AE----IEELEELIEELESElEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677502240 1610 EV-IKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKEnvsHVNDLARQLTTLGiqlsPYNLSTLEDL 1676
Cdd:TIGR02168 935 EVrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELG----PVNLAAIEEY 995
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-594 |
9.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 16 RRQKLLEQSIQSAQETEKSLH-----LIQEsLTFIDKQLAAYIADKVDAAQMPQEAQKIqsdLTSHEISLEEmkkhnqgk 90
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEEKDLHerlngLESE-LAELDEEIERYEEQREQARETRDEADEV---LEEHEERREE-------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 91 eaaqrvlsqIDVAQKKLQDVSMKFR-LFQKPANFEQRLQESKMILDEVKMHLPAL----ETKSVEQEVVQSQLNhcvnly 165
Cdd:PRK02224 253 ---------LETLEAEIEDLRETIAeTEREREELAEEVRDLRERLEELEEERDDLlaeaGLDDADAEAVEARRE------ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 166 kSLSEVKSEVEMVIKTGRQIVQKKQ------TENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVL 239
Cdd:PRK02224 318 -ELEDRDEELRDRLEECRVAAQAHNeeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 240 TEWLAATDMEL----TKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVG---------------EALKTVLGK 300
Cdd:PRK02224 397 RERFGDAPVDLgnaeDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvegsphvETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 301 KETLvEDKLSLLNSNWIAVTSRAEEwLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDEsekkkpqqKEDVLKRLKAEL 380
Cdd:PRK02224 477 VEEL-EAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEE--------KRERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 381 NDIRPKVDSTRDQAANLMaNRGDHCRKlvepQISELNHRFAAISHRIKTgkasipLKELEqfnsDIQKLLEPLEAEIQQg 460
Cdd:PRK02224 547 AELEAEAEEKREAAAEAE-EEAEEARE----EVAELNSKLAELKERIES------LERIR----TLLAAIADAEDEIER- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 461 VNLKEEDFNkDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKaleishqwyqykr 540
Cdd:PRK02224 611 LREKREALA-ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREER------------- 676
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1677502240 541 qaDDLLKCLDDIEKKLASLPEPRDERKikeidrELQKKKEELNAVRRQAEGLSE 594
Cdd:PRK02224 677 --DDLQAEIGAVENELEELEELRERRE------ALENRVEALEALYDEAEELES 722
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
271-428 |
2.33e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.91 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 271 KATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQnVDHITKW 350
Cdd:cd00176 43 EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 351 IIQADTLLDESEK-KKPQQKEDVLKRLKA---ELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHR 426
Cdd:cd00176 122 LEEKEAALASEDLgKDLESVEELLKKHKEleeELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLEL 201
|
..
gi 1677502240 427 IK 428
Cdd:cd00176 202 AE 203
|
|
| ZZ_PCMF_like |
cd02338 |
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ... |
1969-2012 |
3.59e-06 |
|
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.
Pssm-ID: 239078 Cd Length: 49 Bit Score: 45.80 E-value: 3.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1677502240 1969 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 2012
Cdd:cd02338 3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
353-627 |
9.06e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 353 QADTLLDESEKKKPQQKE--DVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVE--PQISELNHRFAAISHRIK 428
Cdd:COG1340 16 KIEELREEIEELKEKRDElnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKElkEERDELNEKLNELREELD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 429 TGKASIPLKELEQFNSD-IQKLLEPLEAEIQqgvnlkeedfNKDMNEDNEgtvKELLQRGDNLQQRITDERKREEIKIKQ 507
Cdd:COG1340 96 ELRKELAELNKAGGSIDkLRKEIERLEWRQQ----------TEVLSPEEE---KELVEKIKELEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 508 QLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER--KIKEIDRELQKKKEELNAV 585
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqeKADELHEEIIELQKELREL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1677502240 586 RRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNF 627
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTT 284
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
76-722 |
1.04e-05 |
|
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: 51.27 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 76 HEISLEEMKKHNQ--GKEAAQRVLS----QIDVAQKKLQDVS-----MKFRLFQKPANFEQRLQESKMILDEVkMHLPAL 144
Cdd:pfam15921 57 YEVELDSPRKIIAypGKEHIERVLEeyshQVKDLQRRLNESNelhekQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 145 ETKSveQEVVQSQLNHCVNLYKSLSEVKSEveMVIKTGRQIVQKKQTENPKE--LDERVTALKLHYNELGAKVTERKQql 222
Cdd:pfam15921 136 ESQS--QEDLRNQLQNTVHELEAAKCLKED--MLEDSNTQIEQLRKMMLSHEgvLQEIRSILVDFEEASGKKIYEHDS-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 223 ekclkLSRKMRKEMNvltewlaatdmeltkrSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSitEVGEALKTVLGKKE 302
Cdd:pfam15921 210 -----MSTMHFRSLG----------------SAISKILRELDTEISYLKGRIFPVEDQLEALKS--ESQNKIELLLQQHQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 303 TLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETF-----DQN------VDHITKWIIQADTLLDESEKKKPQQKED 371
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqarNQNsmymrqLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 372 VLKRL---KAELNDIRpkvdSTRDQAANLMANRGDHCRKLvepqISELNHRFAAISHRIKTGKA--------SIPL---- 436
Cdd:pfam15921 347 LEKQLvlaNSELTEAR----TERDQFSQESGNLDDQLQKL----LADLHKREKELSLEKEQNKRlwdrdtgnSITIdhlr 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 437 KELEQFNSDIQK---LLEPLEAEIqQGVNLKEEDFNKDMNEDNEgTVKELLQRGDNLQQRItdERKREEIKIKQQLLQTK 513
Cdd:pfam15921 419 RELDDRNMEVQRleaLLKAMKSEC-QGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEML--RKVVEELTAKKMTLESS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 514 HNALKDLRS--QRRKKALEISHQWYQYKRQADDL-LKCLDDIEKKLASLPEPRDErkIKEIDRELQKKKEELNAVRRQAE 590
Cdd:pfam15921 495 ERTVSDLTAslQEKERAIEATNAEITKLRSRVDLkLQELQHLKNEGDHLRNVQTE--CEALKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 591 GLSE-------DGAAMAVEPTQIQLSKRWREIESKfaQFRRLNFAQIHTVREetMMVMTEDMPLEISYVPSTYLTEITHV 663
Cdd:pfam15921 573 NMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQ--EFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAV 648
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1677502240 664 SQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNikdSLQQSSGRIDIIHSKKTAALQSA 722
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQLKSA 704
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
536-618 |
1.24e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 536 YQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDG--AAMAVEPTQI 606
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLesveallKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
|
90
....*....|..
gi 1677502240 607 QLSKRWREIESK 618
Cdd:smart00150 81 ELNERWEELKEL 92
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-582 |
1.26e-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: 50.79 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 274 QKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKwiiQ 353
Cdd:TIGR04523 213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK---Q 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 354 ADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANlmanrgdhcrklVEPQISELNHRFAAISHRiktgkas 433
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQ------------NNKIISQLNEQISQLKKE------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 434 ipLKELEQFNSDIQKLLEPLEAEIQQgvNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQriTDERKREEIKIKQQLLQTK 513
Cdd:TIGR04523 351 --LTNSESENSEKQRELEEKQNEIEK--LKKENQSYKQEIKNLESQINDLESKIQNQEK--LNQQKDEQIKKLQQEKELL 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677502240 514 HNALKDLRSQRRKKALEIS---HQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEEL 582
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKdltNQDSVKELIIKNLDNTRESLETQLKVL-----SRSINKIKQNLEQKQKEL 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1133-1437 |
1.43e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1133 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 1205
Cdd:COG1196 232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1206 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 1280
Cdd:COG1196 309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1281 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 1360
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1361 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 1437
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
871-973 |
1.62e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.78 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 871 EFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLENK 950
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1677502240 951 LKQTNLQWIKVSRALPEKQGEIE 973
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
534-758 |
1.63e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.21 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 534 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 606
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 607 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 684
Cdd:cd00176 81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677502240 685 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 758
Cdd:cd00176 139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1145-1677 |
1.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1145 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRrpqLEELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEH 1223
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1224 LQNRRQQLNEMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALK 1302
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1303 LLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAWLTEAETTANVLQDATRKERLLE 1382
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1383 DSKGVKELMKQWQDLQGEIEAHTDVYhnLDENSQKILRSLEGSDDAV---LLQRRLDNMNFKwselrkkSLNIRSHLEAS 1459
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQNIVVEDDEVAAAAieyLKAAKAGRATFL-------PLDKIRARAAL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1460 SDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEpvimsTLETVRIFLTEQPLEGLEK 1539
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1540 LYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIkgswqpV 1619
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1677502240 1620 GDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGiqlsPYNLSTLEDLN 1677
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG----PVNLLAIEEYE 791
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1284 |
2.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 849 QEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI------------PLEPGKEQQLKEKLEQVKLLVEE- 915
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkeelerlkkrltGLTPEKLEKELEELEKAKEEIEEe 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 916 ---LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQDKLENKLKqtnlqwikvsralpEKQGEIEAQIKDL 979
Cdd:PRK03918 407 iskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHRKELLEEYT--------------AELKRIEKELKEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 980 GQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFDVKETEiavqAKQPDVEEILSKGQHLYKEKPATQPV 1055
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1056 KRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtlvtqpvvtkETAISKLEmpsslmlevpalaDFNRAW 1135
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----------EERLKELE-------------PFYNEY 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1136 TELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRRPQLEELITA--------AQNLKNKTSNQEARtiIT 1207
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELRKELEELEKKyseeeyeeLREEYLELSRELAG--LR 679
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502240 1208 DRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVLGQARAKLEswkegpytvdAIQKKITETKQLAK 1284
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KLEKALERVE----------ELREKVKKYKALLK 738
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1131-1233 |
2.87e-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: 45.00 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1131 FNRAWTELTDWLSLLDQVIKSQRvMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 1210
Cdd:pfam00435 6 FFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1677502240 1211 ERIQNQWDEVQEHLQNRRQQLNE 1233
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
1345-1447 |
3.29e-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: 45.00 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1345 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 1424
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
|
90 100
....*....|....*....|...
gi 1677502240 1425 SDDAVLLQRRLDNMNFKWSELRK 1447
Cdd:pfam00435 72 HYASEEIQERLEELNERWEQLLE 94
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
348-1234 |
6.66e-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: 48.50 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 348 TKWIIQADTL----LDESEKKKPQQKE-DVLKRLKAELNDIRPKVDSTRDQAANlmanrGDHCRKLVEPQISELNHRFAA 422
Cdd:TIGR00606 182 TRYIKALETLrqvrQTQGQKVQEHQMElKYLKQYKEKACEIRDQITSKEAQLES-----SREIVKSYENELDPLKNRLKE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 423 ISH-RIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkDMNEDNEGTVKELLQRgdnlqqRITDERKRE 501
Cdd:TIGR00606 257 IEHnLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN-DLYHNHQRTVREKERE------LVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 502 EIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY--KRQADDLLKCLDDIE---------KKLASLPEPRDERKIKE 570
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARdsLIQSLATRLELDGFErgpfserqiKNFHTLVIERQEDEAKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 571 IDRELQKKKEELNAVRRQAEGLSED--GAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDmplE 648
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEkkGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER---E 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 649 ISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDfedlfKQEESLKNIKDSLQQssgrIDIIHSKKTAALQSATPVERV 728
Cdd:TIGR00606 487 LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD-----QEMEQLNHHTTTRTQ----MEMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 729 KLQEALSQL-DFQWEKVnkmykdrqgrfdrsVEKWrrFHYDIKIFNQwlteAEQFLRKTQIPENWEHAKYKWYLKELQDG 807
Cdd:TIGR00606 558 HSDELTSLLgYFPNKKQ--------------LEDW--LHSKSKEINQ----TRDRLAKLNKELASLEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 808 IGQrqtvvrtLNATGEEIIQQSSKTDasiLQEKLGSLNLRWQEVCKQLSdrkkRLEEQKNILSEFQRDLNEfvlwleeaD 887
Cdd:TIGR00606 618 EEQ-------LSSYEDKLFDVCGSQD---EESDLERLKEEIEKSSKQRA----MLAGATAVYSQFITQLTD--------E 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 888 NIASIPL-----EPGKE-QQLKEKLEQVKLLV-EELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIK 960
Cdd:TIGR00606 676 NQSCCPVcqrvfQTEAElQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 961 VSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLL----LWLSPIRNQLEIYNQPNQ----EGPFDVKETEIAVQAKQ 1032
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKlqgsDLDRTVQQVNQEKQEKQ 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1033 PDVEEILSKGQHLYK----EKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIgASPTQTVTLVTQPVVTK 1108
Cdd:TIGR00606 836 HELDTVVSKIELNRKliqdQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPL 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1109 ETAISKLEMPSSLMLEVPALADfNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQK--------ATMQDLEQRR 1180
Cdd:TIGR00606 915 ETFLEKDQQEKEELISSKETSN-KKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKetelntvnAQLEECEKHQ 993
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677502240 1181 PQLEELITAAQNLKNKTSNQEarTIITDRIER--IQNQWDEVQEHLQNRRQQLNEM 1234
Cdd:TIGR00606 994 EKINEDMRLMRQDIDTQKIQE--RWLQDNLTLrkRENELKEVEEELKQHLKEMGQM 1047
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
360-1008 |
8.33e-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: 48.13 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 360 ESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMAnrgdhcrkLVEPQISELNHRFAAISHRIKTGKASipLKEL 439
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA--------ELEEKLEELKEELESLEAELEELEAE--LEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 440 EQFNSDIQKLLEPLEAEiqqgVNLKEEDFNKDMNEdnegtvkelLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKD 519
Cdd:TIGR02168 371 ESRLEELEEQLETLRSK----VAQLELQIASLNNE---------IERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 520 LRSQRRKKaleishqwyqyKRQADDLLKCLDDIEKKLASLPEPRDE-----RKIKEIDRELQKKKEELNAVRRQAEGLSE 594
Cdd:TIGR02168 438 LQAELEEL-----------EEELEELQEELERLEEALEELREELEEaeqalDAAERELAQLQARLDSLERLQENLEGFSE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 595 DGAAMAVEPTQI-----QLSKRWrEIESKFAqfrrlnfAQIHTVREETM-MVMTEDMpleisyvpSTYLTEITHVSQALL 668
Cdd:TIGR02168 507 GVKALLKNQSGLsgilgVLSELI-SVDEGYE-------AAIEAALGGRLqAVVVENL--------NAAKKAIAFLKQNEL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 669 EVEQLLNAPDLcaKDFEDLFKQEESLKNIKDSLQQSSGRIDI---IHSKKTAALQSATPVERvkLQEAL---SQLDFQW- 741
Cdd:TIGR02168 571 GRVTFLPLDSI--KGTEIQGNDREILKNIEGFLGVAKDLVKFdpkLRKALSYLLGGVLVVDD--LDNALelaKKLRPGYr 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 742 ------EKVNKMY-------KDRQGRFDRSVEkwrrfhydIKIFNQWLTEAEQFLRKTQIPenwehakykwyLKELQDGI 808
Cdd:TIGR02168 647 ivtldgDLVRPGGvitggsaKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 809 GQRQTVVRTLNATGEEIIQQSSKtdasiLQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEA-D 887
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISA-----LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 888 NIASIplepgkEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPE 967
Cdd:TIGR02168 783 EIEEL------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1677502240 968 KQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLE 1008
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
321-1083 |
9.04e-05 |
|
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: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 321 SRAEEWLNLLLEYQKHMETFDQNVDHITKwiiQADTLLDESEKKKPQQkeDVLKRL-KAELNDIRPKVDSTRDQAANLMA 399
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQ--ALLKEKrEYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 400 NRGDHCRKL--VEPQISELNHRFAAISHRIKTGKASI-PLKELEQFNsdIQKLLEPLEAEIQQGVnlKEEDFNKDMNEDN 476
Cdd:TIGR02169 245 QLASLEEELekLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLR--VKEKIGELEAEIASLE--RSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 477 EGTVKELLQRGDNLQQRITD--------------------ERKREEIKIKQQL--LQTKHNALKDLRSQRRKKALEISHQ 534
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEElereieeerkrrdklteeyaELKEELEDLRAELeeVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 535 WYQYKRQADDLLKCLDDIEKKLASLPE--PRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQ----- 607
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeeydr 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 608 ----LSKRWREIESKFAQFRRLNFAQIHTVREEtmMVMTEDMPLEISYVPStyLTEITHVSQALLEVEQLLNAPDLCAKD 683
Cdd:TIGR02169 481 vekeLSKLQRELAEAEAQARASEERVRGGRAVE--EVLKASIQGVHGTVAQ--LGSVGERYATAIEVAAGNRLNNVVVED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 684 FEDLFKQEESLKNIKdslqqsSGRIDIIHSKKTAALQSatPVERVKLQEALsqlDFQWEKVnkmykdrqgRFDRSVEKWR 763
Cdd:TIGR02169 557 DAVAKEAIELLKRRK------AGRATFLPLNKMRDERR--DLSILSEDGVI---GFAVDLV---------EFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 764 RFhydikifnqwlteaeqFLRKTQIPENWEHAKY---KWYLKELQDGIGQRQTVVrtlnaTGEEIIQQSSKTDASILQEK 840
Cdd:TIGR02169 617 KY----------------VFGDTLVVEDIEAARRlmgKYRMVTLEGELFEKSGAM-----TGGSRAPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 841 LGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEpgKEQQLKEKLEQVKLLVEELplrq 920
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLKERLEELEEDLSSL---- 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 921 gilkqlnetggpvlvsapispeEQDKLENKLKQTNLQwikvsralpekqGEIEAQIKDLGQLEKKLEDLEEQLNHLLlwL 1000
Cdd:TIGR02169 750 ----------------------EQEIENVKSELKELE------------ARIEELEEDLHKLEEALNDLEARLSHSR--I 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1001 SPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQ----PVKRKLEDLSSEWKAVNRLLQEL 1076
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqikSIEKEIENLNGKKEELEEELEEL 873
|
....*..
gi 1677502240 1077 RAKQPDL 1083
Cdd:TIGR02169 874 EAALRDL 880
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-1261 |
9.53e-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: 47.74 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 480 VKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLAS 558
Cdd:TIGR02168 234 LEELREELEELQEELKEaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 559 LPEPRD--ERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAM-----AVEPTQIQLSKRWREIESKFAQFRR------- 624
Cdd:TIGR02168 314 LERQLEelEAQLEELESKLDELAEELAELEEKLEELKEELESLeaeleELEAELEELESRLEELEEQLETLRSkvaqlel 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 625 -LNFAQIHTVREETMMVMTEDMpleisyvpstylTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQ 703
Cdd:TIGR02168 394 qIASLNNEIERLEARLERLEDR------------RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 704 SSGRIDIIHSKKTAALQSAtpveRVKLQEALSQLDfqwekvnkMYKDRQGRFdrsvekwRRFHYDIKifnQWLTEAEQF- 782
Cdd:TIGR02168 462 ALEELREELEEAEQALDAA----ERELAQLQARLD--------SLERLQENL-------EGFSEGVK---ALLKNQSGLs 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 783 ------LRKTQIPENWEHAKykwyLKELQDGIGQrqTVVRTLNATGEEI--IQQSSKTDASILQEKLgslnLRWQEVCKQ 854
Cdd:TIGR02168 520 gilgvlSELISVDEGYEAAI----EAALGGRLQA--VVVENLNAAKKAIafLKQNELGRVTFLPLDS----IKGTEIQGN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 855 LSDRKKRLEEQKNILSEFQRDLNEFVLWLEE-------ADNIASiplepgKEQQLKEKLEQVKLLVE--ELPLRQGILkq 925
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDN------ALELAKKLRPGYRIVTLdgDLVRPGGVI-- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 926 lneTGGPVlvsapispeeqdklenklkQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRN 1005
Cdd:TIGR02168 662 ---TGGSA-------------------KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1006 QLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQpvkRKLEDLSSEWKAVNRLLQELRAKQPDLAP 1085
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE---ERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1086 GLTTIgasptqtvtlvtqpvvtkETAISKLEMpsslmlevpALADFNRAWTELTDwlslldqviksqrvmvgDLEDINEM 1165
Cdd:TIGR02168 797 ELKAL------------------REALDELRA---------ELTLLNEEAANLRE-----------------RLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1166 IIKQKATMQDLEQRRPQLEELITAAQnlKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAK 1245
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810
....*....|....*.
gi 1677502240 1246 EEAEQVLGQARAKLES 1261
Cdd:TIGR02168 911 SELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
488-1288 |
1.24e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 488 DNLQqRITDERKreEIKIKQQLLQT---KHNALKDLRSQRRKKALEIshqwyqYKRQADDLLKCLDDIEKKLASLpeprd 564
Cdd:TIGR02168 186 ENLD-RLEDILN--ELERQLKSLERqaeKAERYKELKAELRELELAL------LVLRLEELREELEELQEELKEA----- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 565 ERKIKEIDRELQKKKEELNAVRRQaeglsedgaamaveptQIQLSKRWREIESKFAQFRrlnfAQIHTVREETMMVMTED 644
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLE----------------VSELEEEIEELQKELYALA----NEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 645 MPLEISYVpstylteithvsQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQssgRIDIIHSKKTAALQSATP 724
Cdd:TIGR02168 312 ANLERQLE------------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 725 VERV--KLQEALSQLDFQWEKVNK---MYKDRQGRFDRSVEKWRrfhydikifnqwlTEAEQFLRKTQIPEnwehakykw 799
Cdd:TIGR02168 377 LEEQleTLRSKVAQLELQIASLNNeieRLEARLERLEDRRERLQ-------------QEIEELLKKLEEAE--------- 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 800 yLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEvcKQLSDRKKRLEEQKNILSEFQRDLNEF 879
Cdd:TIGR02168 435 -LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL--AQLQARLDSLERLQENLEGFSEGVKAL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 880 VLWLEEADNIA-----SIPLEPGKEQQLKEKLEQV--KLLVEEL-PLRQGILKQLNETGGPVLVSAPISPEEQDKLENKl 951
Cdd:TIGR02168 512 LKNQSGLSGILgvlseLISVDEGYEAAIEAALGGRlqAVVVENLnAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGND- 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 952 kqtnlqwikvsRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIA---- 1027
Cdd:TIGR02168 591 -----------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpgg 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1028 VQAKQPDVEE--ILSKGQHLykeKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPV 1105
Cdd:TIGR02168 660 VITGGSAKTNssILERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1106 VTKETAISKLEMPSSLMLEvpaLADFNRAWTELTDWLSLLDQVIKSQRVMVGDLE-DINEMIIKQKATMQDLEQRRPQLE 1184
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKE---LTELEAEIEELEERLEEAEEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1185 ELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEHLQ-------NRRQQLNEMLKDSTQWLEAKEEAEQVLGQAR 1256
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAaTERRLEDLEEQIEELSEDIEslaaeieELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830
....*....|....*....|....*....|..
gi 1677502240 1257 AKLESWKEgpyTVDAIQKKITETKQLAKDLRQ 1288
Cdd:TIGR02168 894 SELEELSE---ELRELESKRSELRRELEELRE 922
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
853-1288 |
1.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 853 KQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASiplepgKEQQLKEKLEQVKLLVEELPLRQgilkqlnetggp 932
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA------ELEELREELEKLEKLLQLLPLYQ------------ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 933 vlvsapispeEQDKLENKLKQTNLQWikvsRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSP-IRNQLEIYN 1011
Cdd:COG4717 133 ----------ELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1012 QPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPvKRKLEDLSSEWKAVNRLLqELRAKQPDLAPGLTTIG 1091
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1092 ASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADF-NRAWTEL------------TDWLSLLDQVIKSQRVM--- 1155
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeEEELEELlaalglppdlspEELLELLDRIEELQELLrea 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1156 ------------------------VGDLEDINEmIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIE 1211
Cdd:COG4717 357 eeleeelqleeleqeiaallaeagVEDEEELRA-ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1212 RIQNQWDEVQEHLQNRRQQLNE------MLKDSTQWLEAKEEAEQVLGQARAKLESWKegpyTVDAIQKKITETKQLAKD 1285
Cdd:COG4717 436 ELEEELEELEEELEELREELAEleaeleQLEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYRE 511
|
...
gi 1677502240 1286 LRQ 1288
Cdd:COG4717 512 ERL 514
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
152-223 |
2.04e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.70 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677502240 152 EVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKkQTENPKELDERVTALKLHYNELGAKVTERKQQLE 223
Cdd:smart00150 31 ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
|
|
| ZZ_Mind_bomb |
cd02339 |
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ... |
1969-2015 |
2.56e-04 |
|
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.
Pssm-ID: 239079 Cd Length: 45 Bit Score: 40.52 E-value: 2.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1677502240 1969 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRvakgHKMHYPMVEY 2015
Cdd:cd02339 3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1229-1341 |
3.35e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.93 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1229 QQLNEMLKDSTQWLEAKEeaeqvlgqaraKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDyS 1308
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-----------QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-G 68
|
90 100 110
....*....|....*....|....*....|...
gi 1677502240 1309 ADDTRKVHMITENINASWRSIHKRVSEREAALE 1341
Cdd:smart00150 69 HPDAEEIEERLEELNERWEELKELAEERRQKLE 101
|
|
| ZZ_dah |
cd02345 |
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ... |
1969-2014 |
4.09e-04 |
|
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.
Pssm-ID: 239085 Cd Length: 49 Bit Score: 40.27 E-value: 4.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677502240 1969 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVE 2014
Cdd:cd02345 3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
324-590 |
4.86e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 324 EEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDEsekkKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGD 403
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE----KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 404 hcrKLVEPQISELNHRFAAISHRIK-----TGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKE-EDFNKDMNEDN- 476
Cdd:COG5185 308 ---KKATESLEEQLAAAEAEQELEEskretETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELDSFKd 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 477 --EGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKhNALKDLRSQRRKKAleishqwyQYKRQADDLLKCLDDIEK 554
Cdd:COG5185 385 tiESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIE-ELQRQIEQATSSNE--------EVSKLLNELISELNKVMR 455
|
250 260 270
....*....|....*....|....*....|....*.
gi 1677502240 555 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAE 590
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-994 |
5.84e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 4 RKLRNLsYKKAVRRQKLLEQSiqsAQETEKSLHLIQESLTFIDKQLAAYiadKVDAAQMPQEAQKIQSDLTSHEISLEEM 83
Cdd:TIGR02168 200 RQLKSL-ERQAEKAERYKELK---AELRELELALLVLRLEELREELEEL---QEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 84 KKHNQGKEaaqrvlSQIDVAQKKLQDVSMKFrlfqkpanfeQRLQESKMILDEVKMHLPA-LETKSVEQEVVQSQLNHcv 162
Cdd:TIGR02168 273 RLEVSELE------EEIEELQKELYALANEI----------SRLEQQKQILRERLANLERqLEELEAQLEELESKLDE-- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 163 nLYKSLSEVKSEVEMViktgrqivqkkqTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEW 242
Cdd:TIGR02168 335 -LAEELAELEEKLEEL------------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 243 LAATDMELTkrsAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKsITEVGEALKTVLGKKETLVEDKLSL---LNSNWIAV 319
Cdd:TIGR02168 402 IERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAE-LEELEEELEELQEELERLEEALEELreeLEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 320 TSRAEEW------LNLLLEYQKHMETFDQNVDHITKWIIQADTLLD------ESEKKKPQQKEDVLKrlkAELNDIRPKV 387
Cdd:TIGR02168 478 DAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAALG---GRLQAVVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 388 DSTRDQAANLMA-NRGDHCRKLVEPQIS----ELNHRFAAISHRIKTGkasiPLKELEQFNSDIQKLLEPLEAEIqqgvn 462
Cdd:TIGR02168 555 LNAAKKAIAFLKqNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLG----VAKDLVKFDPKLRKALSYLLGGV----- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 463 lkeedfnkdmnednegTVKELLQRGDNLQQRItdeRKREEIKIKQQLLQTKHNALKDLRSQRRKKALEishqwyqYKRQA 542
Cdd:TIGR02168 626 ----------------LVVDDLDNALELAKKL---RPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE-------RRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 543 DDLlkclddiekklaslpeprdERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAamaveptqiQLSKRWREIESKFAQF 622
Cdd:TIGR02168 680 EEL-------------------EEKIEELEEKIAELEKALAELRKELEELEEELE---------QLRKELEELSRQISAL 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 623 R-RLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNapdlcakdfedlfKQEESLKNIKDSL 701
Cdd:TIGR02168 732 RkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-------------ELEAQIEQLKEEL 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 702 QQSSGRIDIIHSKKTAalqsatpvervkLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQ 781
Cdd:TIGR02168 799 KALREALDELRAELTL------------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 782 FLRKTQIP-ENW--EHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtdasiLQEKLGSLNLRWQEVckqlsdr 858
Cdd:TIGR02168 867 LIEELESElEALlnERASLEEALALLRSELEELSEELRELESKRSELRRELEE-----LREKLAQLELRLEGL------- 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 859 KKRLEEQKNILSEFQRDLNEFVLWLEEADniasiplePGKEQQLKEKLEQVKLLVEELplrqgilkqlnetgGPVlvsap 938
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKI--------EDDEEEARRRLKRLENKIKEL--------------GPV----- 987
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677502240 939 ispeeqdklenklkqtNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLN 994
Cdd:TIGR02168 988 ----------------NLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1142-1256 |
6.62e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1142 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 1220
Cdd:PRK00409 497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
|
90 100 110
....*....|....*....|....*....|....*...
gi 1677502240 1221 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQAR 1256
Cdd:PRK00409 557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR 594
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
948-1703 |
1.48e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 948 ENKLKQTNLQWIKVSRALpekqGEIEAQIKDLG-QLEK--KLEDLEEQLNHLLLWLSPIR-----NQLEIYNQPNQEGPF 1019
Cdd:TIGR02168 178 ERKLERTRENLDRLEDIL----NELERQLKSLErQAEKaeRYKELKAELRELELALLVLRleelrEELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1020 DVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQpvkRKLEDLSSEWKAVNRLLQELRAKQPDLapglttigasptqtvt 1099
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQ---KELYALANEISRLEQQKQILRERLANL---------------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1100 lvtqpvvtkETAISKLEMpsslmlevpALADFNRAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQR 1179
Cdd:TIGR02168 315 ---------ERQLEELEA---------QLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1180 RPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLK--DSTQWLEAK---EEAEQVLGQ 1254
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIAS--LNNEIERLEARLERLEDRRERLQQEIEELLKklEEAELKELQaelEELEEELEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1255 ARAKLESWKEGPYTVDA-IQKKITETKQLAKDLRQWQTNVDVANDLaLKLLRDYSADdtrkvhmITENINASWR--SIHK 1331
Cdd:TIGR02168 452 LQEELERLEEALEELREeLEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEG-------VKALLKNQSGlsGILG 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1332 RVSER-------EAALE---------------ETHRLLQQF------------PLDL-----------------EKFLAW 1360
Cdd:TIGR02168 524 VLSELisvdegyEAAIEaalggrlqavvvenlNAAKKAIAFlkqnelgrvtflPLDSikgteiqgndreilkniEGFLGV 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1361 LTEAETT-----------------ANVLQDATRKERLL-------------------------EDSKGVKELMKQWQDLQ 1398
Cdd:TIGR02168 604 AKDLVKFdpklrkalsyllggvlvVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaKTNSSILERRREIEELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1399 GEIEAHTDVYHNLDENSQKILRSL-EGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWL 1477
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1478 QLKDDELsrqapiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLEtvRIFLTEQPLEGLEKLYQEPRE-----LPPEER 1552
Cdd:TIGR02168 764 EELEERL-------------EEAEEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEeaanlRERLES 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1553 AQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLE 1632
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1633 KVKALRGEIAPLKEnvsHVNDLARQLTTLGIQLspynLSTLEDLNTRWKL-LQVAV-------------EDRVRQLHEAH 1698
Cdd:TIGR02168 909 KRSELRRELEELRE---KLAQLELRLEGLEVRI----DNLQERLSEEYSLtLEEAEalenkieddeeeaRRRLKRLENKI 981
|
....*
gi 1677502240 1699 RDFGP 1703
Cdd:TIGR02168 982 KELGP 986
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
20-590 |
1.62e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 20 LLEQSIQSAQETEKSLHLIQESLTF-------IDKQLAAYIADKVDAAQMPQEAQ-KIQSDLTSHEISLEEMKKHNQGKE 91
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVymdlnnnIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 92 -AAQRVLSQIDVAQKKLQDVSmkFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSE 170
Cdd:pfam05483 240 kQVSLLLIQITEKENKMKDLT--FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 171 vksEVEMVIKTGRQIVQKKQTENpKELDERVTALKLHYNELGAKVTerkqQLEKCLKlSRKMRKEMNvlTEWLAATDMEL 250
Cdd:pfam05483 318 ---DLQIATKTICQLTEEKEAQM-EELNKAKAAHSFVVTEFEATTC----SLEELLR-TEQQRLEKN--EDQLKIITMEL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 251 TKRSavegmpSNLDSEVAWGKATQKEIEKqkvhlksitevgeaLKTVLGKKETLVEDKlSLLNSNWIAVTSRAEEWLNLL 330
Cdd:pfam05483 387 QKKS------SELEEMTKFKNNKEVELEE--------------LKKILAEDEKLLDEK-KQFEKIAEELKGKEQELIFLL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 331 LEYQKHMETFDQNVdhitkwiiqadTLLDESEKKKPQQKEDVLKRLKAElndirpKVDSTRDQAanlmanrgdHCRKLve 410
Cdd:pfam05483 446 QAREKEIHDLEIQL-----------TAIKTSEEHYLKEVEDLKTELEKE------KLKNIELTA---------HCDKL-- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 411 pqiselnhrfaAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkdMNEDNEGTVKELLQRGDNL 490
Cdd:pfam05483 498 -----------LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN--LRDELESVREEFIQKGDEV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 491 QQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKE 570
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
570 580
....*....|....*....|
gi 1677502240 571 IDRELQKKKEELNAVRRQAE 590
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIE 664
|
|
| ZZ_NBR1_like |
cd02340 |
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1971-2013 |
1.73e-03 |
|
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.
Pssm-ID: 239080 Cd Length: 43 Bit Score: 38.01 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1677502240 1971 ICKEC--PIIGFRYRSLKHFNYDICQSCffsgrVAKG-HKMHyPMV 2013
Cdd:cd02340 2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-590 |
2.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 54 ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHNQGK--EAAQRVLSQIDVAQ-------KKLQDVSmKFRLFQKPANF 123
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVrKAEELRKAEDARkaEAARKAEEERKAEEarkaedaKKAEAVK-KAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 124 EQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQ--KKQTENPKELDE-- 199
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeaKKKAEEAKKADEak 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 200 -RVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIE 278
Cdd:PTZ00121 1322 kKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 279 KQKVHLKSITEVGEALKTVLGKKETlVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKwiiqADTLL 358
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK 1476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 359 DESEKKKpqqKEDVLKRlKAElnDIRPKVDSTRDQAANLM----ANRGDHCRKLVEPQISElNHRFAAISHRIKTGKASI 434
Cdd:PTZ00121 1477 KKAEEAK---KADEAKK-KAE--EAKKKADEAKKAAEAKKkadeAKKAEEAKKADEAKKAE-EAKKADEAKKAEEKKKAD 1549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 435 PLKELEQFN--SDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQT 512
Cdd:PTZ00121 1550 ELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELKK 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 513 KHNALKDLRSQRRKKALEishqwyqyKRQADDLLKCLDDIEKKLASLP--EPRDERKIKEIDRELQKKKEELNAVRRQAE 590
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEE--------KKKAEELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1176-1701 |
2.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1176 LEQRRPQLEELITAAQNLKNKTSNQEAR-TIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQ 1254
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1255 ARAKLESWKEgpytvdaIQKKITETKQLAKDLRQwqtnvdvaNDLALKLLRDYsADDTRKVHMITENINASWRSIHKRVS 1334
Cdd:PRK03918 254 KRKLEEKIRE-------LEERIEELKKEIEELEE--------KVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1335 EREAALEETHRLLQqfplDLEKflawlteaettanvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDEN 1414
Cdd:PRK03918 318 RLEEEINGIEERIK----ELEE-------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1415 SQkiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELlvwlqlkdDELSRQAPIGGDF 1494
Cdd:PRK03918 375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--------KKAKGKCPVCGRE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1495 PAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGLEKLYQEPRELPPEERaqnvtrlLRKQAEEVNTEWEKL 1574
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE--LRELEKVLKKESELIKLKE-------LAEQLKELEEKLKKY 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1575 NLhsadwqrkidETLERLRELQEATDELDLKLRQAevikgswqpvgdllIDSLQDHLEKVKALRGEIAPLKENvshVNDL 1654
Cdd:PRK03918 516 NL----------EELEKKAEEYEKLKEKLIKLKGE--------------IKSLKKELEKLEELKKKLAELEKK---LDEL 568
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1677502240 1655 ARQLTTLGIQLSPYNLSTLEDLntrwkllqvavEDRVRQLHEAHRDF 1701
Cdd:PRK03918 569 EEELAELLKELEELGFESVEEL-----------EERLKELEPFYNEY 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1208-1423 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1208 DRIERIQNQWD---EVQEHLQNRRQQ---LNEMLKDSTQWLEAKEEAEQvLGQARAKLESWKEGpYTVDAIQKKIT---- 1277
Cdd:COG4913 225 EAADALVEHFDdleRAHEALEDAREQielLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQ-RRLELLEAELEelra 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1278 ETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENInASWRSIHKRVSEREAALEET-HRLLQQFPLDLEK 1356
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI-ERLERELEERERRRARLEALlAALGLPLPASAEE 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677502240 1357 FLAWLTEAETTANVLQDATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLE 1423
Cdd:COG4913 382 FAALRAEAAALLEALEEELEAleEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
816-1012 |
2.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 816 RTLNATGEEIIQQSSKTDASILQEKLGSLNlrwqevcKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIple 895
Cdd:COG3206 152 AVANALAEAYLEQNLELRREEARKALEFLE-------EQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 896 pgkeQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDkLENKLKQTNLQWIKVS----------RAL 965
Cdd:COG3206 222 ----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSarytpnhpdvIAL 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1677502240 966 PEKQGEIEAQIKDlgQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 1012
Cdd:COG3206 297 RAQIAALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1465-1586 |
2.42e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.62 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1465 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 1544
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1677502240 1545 relppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKID 1586
Cdd:smart00150 75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
820-1428 |
4.72e-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: 42.26 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 820 ATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEpgKE 899
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK--KQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 900 QQLKEKLEQVKLLVEELPlrqgILKQLNETGGPVLVSAPISPEEQdklenKLKQTNLQWIKVSRALPEKQGEIEAQIKDL 979
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEA----VLEETQERINRARKAAPLAAHIK-----AVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 980 GQLEKKLEDLEEQLNHLLLWLspiRNQLEIYNQPNQEGPFdvkeTEIAVQAKQpDVEEILSKGQHLYKEKPATQPVKRKL 1059
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHEVATSI----REISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1060 EDLSSEWKAVNRLLQELRAKQPDLAPGLTTIgaSPTQTVTLVTQPVVTKETAISKlempsslmLEVPALADFNRAWTELT 1139
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQ--ELQQRYAELCAAAITCTAQCEK--------LEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1140 DWLSLLDQVIKSQrvmvgdlEDINEMIIKQKATMQdlEQRRP---QLEELITAAQNLKNKTSNqeartiiTDRIERIQNQ 1216
Cdd:TIGR00618 473 QQLQTKEQIHLQE-------TRKKAVVLARLLELQ--EEPCPlcgSCIHPNPARQDIDNPGPL-------TRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1217 WDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEgpytvdaiqkKITETKQLAKDLRQWQTNVDVA 1296
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE----------DIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 1297 NDLALKLLRDYSADDTRKVHMitENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATR 1376
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1677502240 1377 KERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRS----LEGSDDA 1428
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSlgsdLAAREDA 740
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
197-590 |
7.39e-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: 41.88 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 197 LDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKE 276
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 277 IEKQK-------------VHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEewlnlLLEYQKHMETFDQN 343
Cdd:TIGR00618 279 LEETQerinrarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS-----IEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 344 VDHITKWIIQADTLLDESEKKKP---------------QQKEDVLKRLKAELNDIRPKVDsTRDQAANLMANRGDHCRKL 408
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQHTltqhihtlqqqkttlTQKLQSLCKELDILQREQATID-TRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 409 VEPQISELNHRFAAISHRIKTGKASIP--------LKELEQFNSDIQKLLE------PLEAEIQQGVNLKEEDFNKDMNE 474
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIhlqesaqsLKEREQQLQTKEQIHLqetrkkAVVLARLLELQEEPCPLCGSCIH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 475 DNEGTVKELLQRGDN-LQQRITDERKR--EEIKIKQQLLQTKHNALKDLRSQR---RKKALEISHQWYQYKRQADDLLKC 548
Cdd:TIGR00618 513 PNPARQDIDNPGPLTrRMQRGEQTYAQleTSEEDVYHQLTSERKQRASLKEQMqeiQQSFSILTQCDNRSKEDIPNLQNI 592
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1677502240 549 LDDIEKKLASLPEPRDeRKIKEIDRELQKKKEELNAVRRQAE 590
Cdd:TIGR00618 593 TVRLQDLTEKLSEAED-MLACEQHALLRKLQPEQDLQDVRLH 633
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
16-506 |
8.53e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 16 RRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEIS---LEEMKKHNQGKEA 92
Cdd:PRK01156 264 DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIikkLSVLQKDYNDYIK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 93 AQRVLSQIDVAQKKLQDVSMKFRLFQKpaNFEQ----RLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHcvnLYKSL 168
Cdd:PRK01156 344 KKSRYDDLNNQILELEGYEMDYNSYLK--SIESlkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE---INVKL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 169 SEVKSEVEMVIKTGRQIVQKKQ--TENPKEL--------------DERVTALKLHYNELGAKVTERKQQLEKCLKLSRKM 232
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDelSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 233 RKEMNVLTEWLAATDMEltkrsavegmpsNLDSEVAWGKATQKEIEKQKVHLKSITEvgealktvlgkKETLVEDKLSLL 312
Cdd:PRK01156 499 IVDLKKRKEYLESEEIN------------KSINEYNKIESARADLEDIKIKINELKD-----------KHDKYEEIKNRY 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 313 NSNWIA-VTSRAEEWLNLLLEYQK-HMETFDQNVDHITKWIIQADTLLDESEKKKPQQK---EDVLKRLKAELNDIRPKV 387
Cdd:PRK01156 556 KSLKLEdLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyiDKSIREIENEANNLNNKY 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502240 388 DSTRDQAANLMANRGdhcrklvepQISELNHRFAAISHRIKTgkasipLKELEQFNSDIQKLLEPLEAEIQqgvnlkeeD 467
Cdd:PRK01156 636 NEIQENKILIEKLRG---------KIDNYKKQIAEIDSIIPD------LKEITSRINDIEDNLKKSRKALD--------D 692
|
490 500 510
....*....|....*....|....*....|....*....
gi 1677502240 468 FNKDMNEdNEGTVKELLQRGDNLQQRITDERKREEIKIK 506
Cdd:PRK01156 693 AKANRAR-LESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| |
