|
Name |
Accession |
Description |
Interval |
E-value |
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
587-728 |
2.59e-75 |
|
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.
Pssm-ID: 463310 Cd Length: 143 Bit Score: 245.62 E-value: 2.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 587 TIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKN 666
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189185 667 TVTLELHQAHSTDYETIAACQLRFHEILEK-SGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVP 728
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1084-1247 |
1.21e-64 |
|
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.
Pssm-ID: 465655 Cd Length: 166 Bit Score: 216.13 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 1084 PSEEIRIEIIALNL-NDSQITREDTIQRLFIECRFYSLPAE--ETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDIL 1160
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 1161 KAILQRRELPHRSVRFTVVSDPPeDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHA 1240
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 1907189185 1241 LRSVYEQ 1247
Cdd:pfam18111 160 LRAIYSE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-413 |
1.37e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 101 RLGRDVEmeemIEQLQEKVHELERQNEVLKNRLISAKQQLQ---------VQGHRQTSYSRVQARVNTGRRRASASAGSQ 171
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 172 ECPGKGLRFQNVDEAETVQptltkysNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENeiELSLLQLR 251
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEEL-------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 252 EQQATDQRSNIRDNVETIK-----LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCS 326
Cdd:TIGR02168 819 AANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 327 LEKQLHSLQDRINDLEKERELLKEnydklynsafsaaHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQ 406
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELRE-------------KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*..
gi 1907189185 407 NEKLVQE 413
Cdd:TIGR02168 966 DEEEARR 972
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
782-881 |
6.01e-12 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 63.24 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMdldrylkSESLSFYVFDDSDT 861
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 1907189185 862 QENIYMGKVNVPLISLAHDK 881
Cdd:cd00030 74 SKDDFLGEVEIPLSELLDSG 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-473 |
7.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQR--SNIRDNVETIK-LHKQLVE 277
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleQDIARLEERRReLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccslEKQLHSLQDRINDLEKERELLKENYDKLYN 357
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 358 SAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKF 437
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907189185 438 FNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKV 473
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-548 |
1.99e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 123 ERQNEVLKNRliSAKQQLQVQGHRQTSYSRvqaRVNTGRRRASASAGSQECPGKGLR----FQNVDEAETVQPTLTkysn 198
Cdd:pfam15921 397 KEQNKRLWDR--DTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLT---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 199 SLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----------LQLREQQ----ATDQRSNIR 263
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrsrvdLKLQELQhlknEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 264 DNVETIKLhkQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSL-------EKQLHSLQD 336
Cdd:pfam15921 548 TECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFkilkdkkDAKIRELEA 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 337 RINDLEKERELL--------------KENYDKLYNSAFSAAHE------------EQWKLKEQQMKVQIAQLETALKSDL 390
Cdd:pfam15921 626 RVSDLELEKVKLvnagserlravkdiKQERDQLLNEVKTSRNElnslsedyevlkRNFRNKSEEMETTTNKLKMQLKSAQ 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 391 TDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALllikaqKEQKNGDLSFL 470
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL-EEAMTNANKEKHFL------KEEKNKLSQEL 778
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 471 EKVDSKINKdldrSMKELQATHAETVQELEKTRNMLIMQHKINKDYQmEVETVTQKMEnlQQDYELKVEqyvHLLDIR 548
Cdd:pfam15921 779 STVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---HTLDVK 846
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
782-877 |
8.85e-08 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 51.33 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHD--TAIVPSSNDPQFDDHMCFPVPmnmdldrYLKSESLSFYVFDDS 859
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 1907189185 860 DTQENIYMGKVNVPLISL 877
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| C2 |
pfam00168 |
C2 domain; |
782-889 |
1.34e-07 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 50.78 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYV-VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDldrylksESLSFYVFDDSD 860
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 1907189185 861 TQENIYMGKVNVPLISLAHDKCISGIFEL 889
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-413 |
2.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 48 EELEDRFLRLH------DENILLKQHARKQEDKIKRMATKLIRLvndkkrYERVGGGPKRLGRDVEMEEMIEQLQEKVHE 121
Cdd:PRK03918 276 EELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRL------EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 122 LERQNEVLKNRLisakqqlqvqghrqTSYSRVQARVNTGRRRASASAGsqECPGKGLRfqNVDEAETVQPTLTKYsnslL 201
Cdd:PRK03918 350 LEKRLEELEERH--------------ELYEEAKAKKEELERLKKRLTG--LTPEKLEK--ELEELEKAKEEIEEE----I 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 202 EEARGEIRNLENVIQSQRGQIEEL----------------EHLAEILK--------------------TQLKRKENEIEL 245
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteEHRKELLEeytaelkriekelkeieekeRKLRKELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 246 SLLQ----LREQQATDQRSNIRDNVETIKLHKqLVEKSNALSVIEGKFIQLQEKQRTLRIShdalMANGDELNKQLKEQR 321
Cdd:PRK03918 488 VLKKeselIKLKELAEQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 322 LKCCSLEKQLHSLQDRI--------NDLEKERELLKENYDKlYNSAFSAAHEEQWKLKEQQmkvqiaqletALKSDLTDK 393
Cdd:PRK03918 563 KKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNE-YLELKDAEKELEREEKELK----------KLEEELDKA 631
|
410 420
....*....|....*....|
gi 1907189185 394 TEVLDKLKTERDQNEKLVQE 413
Cdd:PRK03918 632 FEELAETEKRLEELRKELEE 651
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-601 |
2.88e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 235 QLKRKENEIELSLLQLREQ---QATDQRSNIRDNVETI-KLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANG 310
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgiLIAALSEQLRKALFELdKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 311 DELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLynsafsaaheeqwKLKEQQMKVQIAQLETALKSDL 390
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL-------------EQQRKQLEAQIAELQSEIAERE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 391 TDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSfL 470
Cdd:COG4372 150 EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL-E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 471 EKVDSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAA 550
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907189185 551 RIQKLEAQLKdiaYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHI 601
Cdd:COG4372 309 LIGALEDALL---AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVL 356
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
312-588 |
1.09e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 312 ELNKQLKEQRLKCCSLEKQLHSLQDRINDLEK----ERELLKENYDKLYNSAfsaaheeqwklkeQQMKVQIAQLETALK 387
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEA-------------KTIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 388 ---SDLTDKTEVLDKLKTER-------DQNEKLV-------------QENRDLQLQCLQQKQRLHELQSRLKFFN----- 439
Cdd:PHA02562 245 nlvMDIEDPSAALNKLNTAAakikskiEQFQKVIkmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDtaide 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 440 -QESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiNKDLDRSMKELQATHAETVQELEKTRNMLImqhKINKDYQm 518
Cdd:PHA02562 325 lEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELD---KIVKTKS- 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189185 519 evETVTQKME-----NLQQDYELKveqyvhlldiraARIQKleaqlKDIAYGTKQYKFKPEIMPDDSV----DEFDETI 588
Cdd:PHA02562 397 --ELVKEKYHrgivtDLLKDSGIK------------ASIIK-----KYIPYFNKQINHYLQIMEADYNftldEEFNETI 456
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
327-521 |
3.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 327 LEKQLHSLQDRINDLEKERELLKENYDKLYNSAFSAahEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQ 406
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRD--REQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 407 NEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQ-------ESDINADDLSEALLLIK---AQKEQKNGDLSFLEKVDSK 476
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKeeeAERKQLQAKLQQTEEELRS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907189185 477 INKDLdRSMKELQATHAETVQELEKTRNMLimQHKINKDYQMEVE 521
Cdd:pfam07888 190 LSKEF-QELRNSLAQRDTQVLQLQDTITTL--TQKLTTAHRKEAE 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-563 |
5.61e-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: 41.20 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 328 EKQLHSLQ---DRINDLEKErelLKENYDKLYNSAFSA--AHEEQWKLKEQQMKVQIAQLETA------LKSDLTDKTEV 396
Cdd:TIGR02168 178 ERKLERTRenlDRLEDILNE---LERQLKSLERQAEKAerYKELKAELRELELALLVLRLEELreeleeLQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 397 LDKLKTERDQNEKLVQENRDLQLQCLQQKqrlHELQSRLKFFNQEsdinADDLSEALLLIKAQKEQKNGDLS----FLEK 472
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEI---EELQKELYALANE----ISRLEQQKQILRERLANLERQLEeleaQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 473 VDSKINKDLDRS------MKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKveqyvhlld 546
Cdd:TIGR02168 328 LESKLDELAEELaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL--------- 398
|
250
....*....|....*..
gi 1907189185 547 irAARIQKLEAQLKDIA 563
Cdd:TIGR02168 399 --NNEIERLEARLERLE 413
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
587-728 |
2.59e-75 |
|
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.
Pssm-ID: 463310 Cd Length: 143 Bit Score: 245.62 E-value: 2.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 587 TIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKN 666
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189185 667 TVTLELHQAHSTDYETIAACQLRFHEILEK-SGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVP 728
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1084-1247 |
1.21e-64 |
|
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.
Pssm-ID: 465655 Cd Length: 166 Bit Score: 216.13 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 1084 PSEEIRIEIIALNL-NDSQITREDTIQRLFIECRFYSLPAE--ETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDIL 1160
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 1161 KAILQRRELPHRSVRFTVVSDPPeDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHA 1240
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 1907189185 1241 LRSVYEQ 1247
Cdd:pfam18111 160 LRAIYSE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-413 |
1.37e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 101 RLGRDVEmeemIEQLQEKVHELERQNEVLKNRLISAKQQLQ---------VQGHRQTSYSRVQARVNTGRRRASASAGSQ 171
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 172 ECPGKGLRFQNVDEAETVQptltkysNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENeiELSLLQLR 251
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEEL-------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 252 EQQATDQRSNIRDNVETIK-----LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCS 326
Cdd:TIGR02168 819 AANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 327 LEKQLHSLQDRINDLEKERELLKEnydklynsafsaaHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQ 406
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELRE-------------KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*..
gi 1907189185 407 NEKLVQE 413
Cdd:TIGR02168 966 DEEEARR 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-488 |
2.20e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-------QRLKCCSLEKQLHSLQDRINDLEKERELLKENYD 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 354 KLYNS-----AFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERDQNEKLVQENRDlqlqclqqkqRL 428
Cdd:TIGR02168 856 SLAAEieeleELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELRE----------KL 924
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189185 429 HELQSRLKFFNQESDINADDLSEAL-LLIKAQKEQKNGDLSFLEKVDSKInKDLDRSMKEL 488
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRL-KRLENKIKEL 984
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
782-881 |
6.01e-12 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 63.24 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMdldrylkSESLSFYVFDDSDT 861
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 1907189185 862 QENIYMGKVNVPLISLAHDK 881
Cdd:cd00030 74 SKDDFLGEVEIPLSELLDSG 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-473 |
7.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQR--SNIRDNVETIK-LHKQLVE 277
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleQDIARLEERRReLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccslEKQLHSLQDRINDLEKERELLKENYDKLYN 357
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 358 SAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKF 437
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907189185 438 FNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKV 473
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-563 |
2.73e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLKRKEneIELSLLQLREQQATDQRsnirdnvetikLHKQ 274
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 275 LVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENydk 354
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE--- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 355 lynsafsaahEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSR 434
Cdd:COG1196 325 ----------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 435 LKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKInKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINK 514
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907189185 515 DYQMEVETVTQKMENLQQDYELKVEQYV-HLLDIRAARIQKLEAQLKDIA 563
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEAdYEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-476 |
4.90e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 106 VEMEEMIEQLQEKVHELERQnevlknrlisaKQQLQVQGHRQTSYSRVQARVNTGRRRASAsagsqecpgkgLRFQN-VD 184
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERYKELKAELRELELALLV-----------LRLEElRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 185 EAETVQPTLTKYsNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSN 261
Cdd:TIGR02168 240 ELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 262 IRDNVETIKLHKQLVEKSNALSviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDL 341
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 342 EKERELLK---ENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERD----QNEKLVQEN 414
Cdd:TIGR02168 392 ELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELErleeALEELREEL 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189185 415 RDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALLLIKAQKEQKNGD---LSFLEKVDSK 476
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEG 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-590 |
5.93e-11 |
|
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: 66.97 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 114 QLQEKVHELERQNEVLKNRLISAKQQLQVQghrQTSYSRVQARVNtgrrrasasagsqecpgkglrfQNVDEAETVQPTL 193
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEK---TTEISNTQTQLN----------------------QLKDEQNKIKKQL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 194 TKySNSLLEEARGEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLKRKENEIELSLLQLRE-----QQATDQRSNIR 263
Cdd:TIGR04523 270 SE-KQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 264 D-----NVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDAL---MANGDELNKQlKEQRLKccSLEKQLHSLQ 335
Cdd:TIGR04523 349 KeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQ-KDEQIK--KLQQEKELLE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 336 DRINDLEKERELLKENYDKLYN--SAFSAAHEEQWKLKEQQmKVQIAQLE---TALKSDLTDKTEVLDK----LKTERDQ 406
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESL-ETQLKVLSrsiNKIKQNLEQKQKELKSkekeLKKLNEE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 407 NEKLVQENRDLQLQCLQQKQRLHELQSR-----LKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiNKDL 481
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEkkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----QKSL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 482 DRSMKELQathaETVQELEKTRNMLIMQHKInkdYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRAARIQKLEAQLKD 561
Cdd:TIGR04523 581 KKKQEEKQ----ELIDQKEKEKKDLIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKE 652
|
490 500 510
....*....|....*....|....*....|.
gi 1907189185 562 IAYGTKQYkfKPEIMPD--DSVDEFDETIHL 590
Cdd:TIGR04523 653 TIKEIRNK--WPEIIKKikESKTKIDDIIEL 681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-562 |
6.88e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 197 SNSLLEEARgEIRNLENviqsqrgQIEELEHLAEILKTQLKRKENEielslLQLREQQATDQRSNIRDnvetikLHKQLV 276
Cdd:TIGR02168 669 NSSILERRR-EIEELEE-------KIEELEEKIAELEKALAELRKE-----LEELEEELEQLRKELEE------LSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 277 EKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLy 356
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL- 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 357 NSAFSAAHEE--QWKLKEQQMKVQIAQLETALksdltdkTEVLDKLKTERDQNEKLVQENRDLQLQCLqqkqrlhELQSR 434
Cdd:TIGR02168 809 RAELTLLNEEaaNLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELEELIE-------ELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 435 LKFFNQESdinaDDLSEALLLIKAQKEQKNGDLSFLEKVdskiNKDLDRSMKELQATHAETVQELEKTRNMLI-MQHKIN 513
Cdd:TIGR02168 875 LEALLNER----ASLEEALALLRSELEELSEELRELESK----RSELRRELEELREKLAQLELRLEGLEVRIDnLQERLS 946
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907189185 514 KDYQMEVETVtQKMENLQQDYELKVEQyvhlldiraaRIQKLEAQLKDI 562
Cdd:TIGR02168 947 EEYSLTLEEA-EALENKIEDDEEEARR----------RLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-373 |
1.41e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRfqnvDEA 186
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE----AEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 187 ETVQPTLTKYSNSL------LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQA--TDQ 258
Cdd:TIGR02168 785 EELEAQIEQLKEELkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIEslAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 259 RSNIRDNVEtiKLHKQLVEKSN-------ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQL 331
Cdd:TIGR02168 861 IEELEELIE--ELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907189185 332 HSLQDRINDLEK-ERELLKENYDKLYNSaFSAAHEEQWKLKEQ 373
Cdd:TIGR02168 939 DNLQERLSEEYSlTLEEAEALENKIEDD-EEEARRRLKRLENK 980
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-548 |
1.99e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 123 ERQNEVLKNRliSAKQQLQVQGHRQTSYSRvqaRVNTGRRRASASAGSQECPGKGLR----FQNVDEAETVQPTLTkysn 198
Cdd:pfam15921 397 KEQNKRLWDR--DTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLT---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 199 SLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----------LQLREQQ----ATDQRSNIR 263
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrsrvdLKLQELQhlknEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 264 DNVETIKLhkQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSL-------EKQLHSLQD 336
Cdd:pfam15921 548 TECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFkilkdkkDAKIRELEA 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 337 RINDLEKERELL--------------KENYDKLYNSAFSAAHE------------EQWKLKEQQMKVQIAQLETALKSDL 390
Cdd:pfam15921 626 RVSDLELEKVKLvnagserlravkdiKQERDQLLNEVKTSRNElnslsedyevlkRNFRNKSEEMETTTNKLKMQLKSAQ 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 391 TDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALllikaqKEQKNGDLSFL 470
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL-EEAMTNANKEKHFL------KEEKNKLSQEL 778
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 471 EKVDSKINKdldrSMKELQATHAETVQELEKTRNMLIMQHKINKDYQmEVETVTQKMEnlQQDYELKVEqyvHLLDIR 548
Cdd:pfam15921 779 STVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---HTLDVK 846
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-562 |
2.77e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndkkRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 116 QEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNtgrrraSASAGSQECPGKGLRFQnvDEAETVQ-PTLT 194
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR------SILVDFEEASGKKIYEH--DSMSTMHfRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEEL----EHLAEILKTQLKRK------ENEIELSLLQLREQQATDQRSNIRD 264
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQDRieqlisEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 265 NVETIklhKQLVEKSNA-----LSVIEGKFIQLQEKQRTL-RISHDALMANGDEL---NKQLKEQRL-------KCCSLE 328
Cdd:pfam15921 300 QLEII---QEQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKIEELEKQLvlaNSELTEARTerdqfsqESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 329 KQLHSLQDRINDLEKERELLKENYDKLYN----SAFSAAHEEQwKLKEQQMKVQ-IAQLETALKSDLTDKTE-VLDKLKT 402
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQrLEALLKAMKSECQGQMErQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 403 ERDQNEKLVQENRDLQLQCLQQKQRLHELQSRlKFFNQESDINADDLSEALLLIKAQKEQKNGDLsflekvdSKINKDLD 482
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKERAIEATNAEI-------TKLRSRVD 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 483 RSMKELQ-----ATHAETVQ-ELEKTRNMLIMQHKINKDYQMEVETVTQ-----------------KMENLQQDYELKVE 539
Cdd:pfam15921 528 LKLQELQhlkneGDHLRNVQtECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQ 607
|
570 580
....*....|....*....|...
gi 1907189185 540 QYVHLLDIRAARIQKLEAQLKDI 562
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDL 630
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-588 |
9.78e-09 |
|
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: 59.65 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEELEHlaEILKTQLKRKENEIELSLLQLREQQAT----------DQRSNIRD 264
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQK--NIDKIKNKLLKLELLLSNLKKKIQKNKslesqiselkKQNNQLKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 265 NVEtiKLHKQLVEKSNALSVIEGKFIQLQEKQrtlrishdalmangDELNKQLKEQRL-------KCCSLEKQLHSLQDR 337
Cdd:TIGR04523 233 NIE--KKQQEINEKTTEISNTQTQLNQLKDEQ--------------NKIKKQLSEKQKeleqnnkKIKELEKQLNQLKSE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 338 INDLEKEREllkENYDKLYNSAFSAAHEEQWKLKEQ---------QMKVQIAQLET----------ALKSDLTDKTEVLD 398
Cdd:TIGR04523 297 ISDLNNQKE---QDWNKELKSELKNQEKKLEEIQNQisqnnkiisQLNEQISQLKKeltnsesensEKQRELEEKQNEIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 399 KLKTE----RDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDInaddLSEALLLIKAQKEQKNGDLSFLEKVD 474
Cdd:TIGR04523 374 KLKKEnqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL----LEKEIERLKETIIKNNSEIKDLTNQD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 475 S----KIN-------------KDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQdyelK 537
Cdd:TIGR04523 450 SvkelIIKnldntresletqlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE----K 525
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907189185 538 VEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEImpddsvDEFDETI 588
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI------DEKNKEI 570
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-408 |
1.04e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 101 RLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrf 180
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEE-------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 181 QNVDEAETVQPTLTKYSNSLlEEARGEIRNLENVIQSQRGQIEELEhlaeilktqlkRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEI-ENVKSELKELEARIEELEEDLHKLE-----------EALNDLEARLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 261 NIRDNVETI---------KLHKQLVEKSNALSVIEGK---FIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLE 328
Cdd:TIGR02169 802 KLEEEVSRIearlreieqKLNRLTLEKEYLEKEIQELqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 329 KQLHSLQDRINDLEKERELLKENYDKLYNSAFSAAHE-EQWKLKEQQMKVQIAQLETALKSDLTDKTEVLD--KLKTERD 405
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQ 961
|
...
gi 1907189185 406 QNE 408
Cdd:TIGR02169 962 RVE 964
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-558 |
1.95e-08 |
|
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: 58.88 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSNIRDNVETIKL 271
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKnklEVELNKLEKQKKENKKNIDKFLTEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 272 HKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEK--QLH-SLQDRINDLEKERELL 348
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiQKNkSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 349 KENYDKLyNSAFSAAhEEQWKLKEQQMKvQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQenrdlqlqclqqkqrl 428
Cdd:TIGR04523 231 KDNIEKK-QQEINEK-TTEISNTQTQLN-QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN---------------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 429 hELQSRLKFFNQESDINAD-DLSEALLLIKAQKEQKNGDLSFLEKVDSKIN---KDLDRSMKELQATHAETVQELEKTRN 504
Cdd:TIGR04523 292 -QLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQN 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907189185 505 MLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIraaRIQKLEAQ 558
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDE---QIKKLQQE 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-413 |
4.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 197 SNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLR--EQQATDQRSNIRDNVETI-KLHK 273
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEKEIaELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 274 QLVEKSNALSviegkfIQLQEKQRTLRISHDALMANGDELN---------KQLKEQRlkccslEKQLHSLQDRINDLEKE 344
Cdd:COG4942 98 ELEAQKEELA------ELLRALYRLGRQPPLALLLSPEDFLdavrrlqylKYLAPAR------REQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189185 345 RELLKENYDKLynSAFSAAHEEQwKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQE 413
Cdd:COG4942 166 RAELEAERAEL--EALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
782-877 |
8.85e-08 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 51.33 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHD--TAIVPSSNDPQFDDHMCFPVPmnmdldrYLKSESLSFYVFDDS 859
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 1907189185 860 DTQENIYMGKVNVPLISL 877
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| C2 |
pfam00168 |
C2 domain; |
782-889 |
1.34e-07 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 50.78 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYV-VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDldrylksESLSFYVFDDSD 860
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 1907189185 861 TQENIYMGKVNVPLISLAHDKCISGIFEL 889
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-321 |
2.16e-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: 55.45 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELERQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 126 NEVLKNRLISAKQQLQVQghrQTSYSRVQARVntgrrrASASAGSQECPGKglrfqnVDEAETVQPTLTKYSNSL---LE 202
Cdd:TIGR02168 318 LEELEAQLEELESKLDEL---AEELAELEEKL------EELKEELESLEAE------LEELEAELEELESRLEELeeqLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 203 EARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETI-KLHKQLVEKSNA 281
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeELQEELERLEEA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907189185 282 LSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQR 321
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-563 |
2.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLH-KQLVEKS 279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 280 NALSVIEGKFIQLQEKQRTLRISHDALMAngdelnKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLYNSA 359
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATE------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 360 FSAAHEEQWKLKEQQMKV--QIAQLETALKSDLTDKTEVLDKLKT-----------ERDQNEKLVQENRDLQLQCLQQKQ 426
Cdd:COG4717 237 EAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 427 RLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQkngdLSFLEKVDSKInkDLDRSMKELQATHAETVQELEKTRNML 506
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189185 507 IMQHKINKDYQMEVETVTQKMENLqqDYELKVEQYVHLLDIRAARIQKLEAQLKDIA 563
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-578 |
2.93e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 223 EELEHLAEILKTQLKRKENEIELSLLQLREQQAT---------DQRSNIRDNVETIKLH----KQLVEKSNAL-SVIEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 289 FIQLQEKQRTLRISHDALMANGDELNK--QLKEQRLKCCSLEKQLHSLQdrINDLEKE----RELLKENYDKLYNSafsa 362
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQltEEKEAQMEELNKAKAAHSFV--VTEFEATtcslEELLRTEQQRLEKN---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 363 ahEEQWKLKEQQMKVQIAQLETALKsdLTDKTEV-LDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHE----LQSRLK- 436
Cdd:pfam05483 376 --EDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKKILAEDEKLLDEKKQFEKIAEELKGKEQEliflLQAREKe 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 437 FFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKD-LDRSMKELQATHAETVQELEKTRNMLIMQHKINKD 515
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189185 516 YQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPD 578
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
198-567 |
1.02e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 198 NSLLEEARGEIRNLENViqsQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQ 274
Cdd:pfam02463 197 LQELKLKEQAKKALEYY---QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaqvLKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 275 LVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELlkenydk 354
Cdd:pfam02463 274 NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 355 lynsafsaaheeqWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKlvqENRDLQLQCLQQKQRLHELQSR 434
Cdd:pfam02463 347 -------------LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS---AAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 435 LKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINK-DLDRSMKELQATHAETVQELEKTRNMLIMQHKIN 513
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKqELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907189185 514 KDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTK 567
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-416 |
7.21e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 47 REELEDRFLRLhDENILLKQHARKQEDKIKRMATKLIR---LVNDKKRYErvggGPKRLGRDVEMEEMIEQLQEKVHELE 123
Cdd:TIGR02169 176 LEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREYE----GYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 124 RQNEVLKnRLISAKQQlqvqghrqtSYSRVQARVNTGRRRASASAGsqecpgkglrfqnvDEAETVQPTLtkysnsllEE 203
Cdd:TIGR02169 251 EELEKLT-EEISELEK---------RLEEIEQLLEELNKKIKDLGE--------------EEQLRVKEKI--------GE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA-----TDQRSNIRDNVETIKLHKQLVEK 278
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 279 SNALSVIEGKfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLYNS 358
Cdd:TIGR02169 379 EFAETRDELK--DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 359 AFSAAheeQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRD 416
Cdd:TIGR02169 457 LEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-586 |
8.84e-06 |
|
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: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 34 RTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndKKRYERVGGGPKRLGRDVEME-EMI 112
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA---QAEEYELLAELARLEQDIARLeERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 113 EQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrfqnvDEAETVQPT 192
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALL-----------EAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 193 LTKYSNSL--LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSNIRDNVE 267
Cdd:COG1196 378 EEELEELAeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALaelEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 268 TIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEqrlkccSLEKQLHSLQDRINDLEKEREL 347
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 348 LKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDktEVLDKLKTERdqnekLVQENRDLQLQCLQQKQR 427
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF--LPLDKIRARA-----ALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 428 LHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEkVDSKINKDLDRSMKELQATHAETVQELEKTRNMLI 507
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189185 508 MQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDE 586
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
47-485 |
9.79e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 47 REELEDRFLRLHDENILLKqhARKQEDKiKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEM-EEMIEQLQEKVHELERQ 125
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLK--AMKSECQ-GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMlRKVVEELTAKKMTLESS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 126 NEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRAsasagsQECPGKGLRFQNVD-EAETVQPTLTKySNSLLEEA 204
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL------QHLKNEGDHLRNVQtECEALKLQMAE-KDKVIEIL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 205 RGEIRN---------------------LENVIQSQRGQIEELEHLAEilKTQLKRKENEIELSLLQLRE----------- 252
Cdd:pfam15921 568 RQQIENmtqlvgqhgrtagamqvekaqLEKEINDRRLELQEFKILKD--KKDAKIRELEARVSDLELEKvklvnagserl 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 253 ------QQATDQ--------RSNIRDNVETIK-LHKQLVEKSNALSVIEGKF-IQLQEKQRTLRISHDAL--MANGDE-- 312
Cdd:pfam15921 646 ravkdiKQERDQllnevktsRNELNSLSEDYEvLKRNFRNKSEEMETTTNKLkMQLKSAQSELEQTRNTLksMEGSDGha 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 313 ------LNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLYNSAFSAAHE--------EQWKLKEQQMKVQ 378
Cdd:pfam15921 726 mkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEknkmagelEVLRSQERRLKEK 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 379 IAQLETALKSDLTDKTEVLDKLKTERDQNEKL-VQENRDLQLQCLQQKQRLHELQSRL----KFFNQESDI-----NADD 448
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRQEQESVRLkLQHTLDVKELQGPGYTSNSSMKPRLlqpaSFTRTHSNVpssqsTASF 885
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907189185 449 LSEALLLIKAQKEQKNGDL-SFLEKVDSKINKDLDRSM 485
Cdd:pfam15921 886 LSHHSRKTNALKEDPTRDLkQLLQELRSVINEEPTVQL 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-562 |
1.85e-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: 49.28 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 20 NLFGVGGLQETSTARTVKTRQAVSRVSR--EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGg 97
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 98 gPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKG 177
Cdd:TIGR02168 368 -EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 178 lrfQNVDEAETVQPTLtkysNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENE--------------- 242
Cdd:TIGR02168 447 ---EELEELQEELERL----EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvkallknqsgls 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 243 -------------------IELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQ------------ 291
Cdd:TIGR02168 520 gilgvlselisvdegyeaaIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndreilknieg 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 292 -------------------------------LQEKQRTLR---------------ISHDALMANGD-------------- 311
Cdd:TIGR02168 600 flgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKklrpgyrivtldgdlVRPGGVITGGSaktnssilerrrei 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 312 -ELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKL--------YNSAFSAAHEEQWKLKEQQMKVQIAQL 382
Cdd:TIGR02168 680 eELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrKDLARLEAEVEQLEERIAQLSKELTEL 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 383 E---TALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLK--FFNQESDI-----NADDLSEA 452
Cdd:TIGR02168 760 EaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeAANLRERLeslerRIAATERR 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 453 LLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQA--------------------THAETVQELEKTRNMLIMQH-- 510
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasleealallrseleELSEELRELESKRSELRRELee 919
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 511 --KINKDYQMEVETVTQKMENLQQ----DYELKVEQYVHLLDIRAARIQKLEAQLKDI 562
Cdd:TIGR02168 920 lrEKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-413 |
2.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 48 EELEDRFLRLH------DENILLKQHARKQEDKIKRMATKLIRLvndkkrYERVGGGPKRLGRDVEMEEMIEQLQEKVHE 121
Cdd:PRK03918 276 EELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRL------EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 122 LERQNEVLKNRLisakqqlqvqghrqTSYSRVQARVNTGRRRASASAGsqECPGKGLRfqNVDEAETVQPTLTKYsnslL 201
Cdd:PRK03918 350 LEKRLEELEERH--------------ELYEEAKAKKEELERLKKRLTG--LTPEKLEK--ELEELEKAKEEIEEE----I 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 202 EEARGEIRNLENVIQSQRGQIEEL----------------EHLAEILK--------------------TQLKRKENEIEL 245
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteEHRKELLEeytaelkriekelkeieekeRKLRKELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 246 SLLQ----LREQQATDQRSNIRDNVETIKLHKqLVEKSNALSVIEGKFIQLQEKQRTLRIShdalMANGDELNKQLKEQR 321
Cdd:PRK03918 488 VLKKeselIKLKELAEQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 322 LKCCSLEKQLHSLQDRI--------NDLEKERELLKENYDKlYNSAFSAAHEEQWKLKEQQmkvqiaqletALKSDLTDK 393
Cdd:PRK03918 563 KKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNE-YLELKDAEKELEREEKELK----------KLEEELDKA 631
|
410 420
....*....|....*....|
gi 1907189185 394 TEVLDKLKTERDQNEKLVQE 413
Cdd:PRK03918 632 FEELAETEKRLEELRKELEE 651
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-350 |
4.72e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQR--SNIRDNVETIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189185 276 VEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccsLEKQLHSLQDRINDLEKERELLKE 350
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAA 170
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
192-463 |
4.80e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 192 TLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKL 271
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 272 HKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQrlkccslEKQLHSLQDRINDLEKERELLKEN 351
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 352 YDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHEL 431
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270
....*....|....*....|....*....|..
gi 1907189185 432 QSRLKFFNQESDINADDLSEALLLIKAQKEQK 463
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-561 |
5.62e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSysrvqARVNTGRRRASASAGSQEcpgkglRFQNVDEA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEAR------REELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 187 ETVQPTltkysnslLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQatDQRSNIRDNV 266
Cdd:PRK02224 324 EELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 267 ETiklhkqlveksnalsvIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEqrlkccsLEKQLHSLQDRIndlEKERE 346
Cdd:PRK02224 394 EE----------------LRERFGDAPVDLGNAEDFLEELREERDELREREAE-------LEATLRTARERV---EEAEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 347 LLKENY---------DKLYNSAFSAAHEEQWKLKEQ--QMKVQIAQLETALKS--DLTDKTEVLDKLKTERDQNEKLVQE 413
Cdd:PRK02224 448 LLEAGKcpecgqpveGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 414 NRDLQLQCLQQKQRLHELQsrlkffnQESDINADDLSEAlllikAQKEQKNGDlSFLEKVdskinKDLDRSMKELqathA 493
Cdd:PRK02224 528 RRETIEEKRERAEELRERA-------AELEAEAEEKREA-----AAEAEEEAE-EAREEV-----AELNSKLAEL----K 585
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 494 ETVQELEKTRNMLIMQhkinKDYQMEVETVTQKMENLQQDYELKVEQyvhlLDIRAARIQKLEAQLKD 561
Cdd:PRK02224 586 ERIESLERIRTLLAAI----ADAEDEIERLREKREALAELNDERRER----LAEKRERKRELEAEFDE 645
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
207-323 |
6.92e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLKRKENEIELSLLQLRE--QQATDQRSNIRDNVETIK-----LHKQLVE 277
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907189185 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLK 323
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-559 |
1.94e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 15 KDTGLNLFGVGGLQETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQ--EDKIKRMA------------- 79
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvlEKELKHLRealqqtqqshayl 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 80 TKLIRLVNDKKRYERVGGgpKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISaKQQLQVQGHRQTSYSRVQARVNt 159
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHTELQSKMR- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 160 grRRASASAGSQecpgkGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQrgQIEELEHLAEI--LKTQLK 237
Cdd:TIGR00618 322 --SRAKLLMKRA-----AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLqqQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 238 RKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQLVEKSNALSVIEgKFIQLQEKQRTLRISHDALMANGDELN 314
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaKKQQELQQRYAELCA-AAITCTAQCEKLEKIHLQESAQSLKER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 315 KQLKEQRLKCCSLEKQLHSLQD-RINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDK 393
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLaRLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 394 TEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKV 473
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 474 --DSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKIN---------KDYQMEVETVTQKMENLQQDYELKVEQYV 542
Cdd:TIGR00618 632 lhLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
570 580
....*....|....*....|....*..
gi 1907189185 543 HLLDIR----------AARIQKLEAQL 559
Cdd:TIGR00618 712 HIEEYDrefneienasSSLGSDLAARE 738
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
108-355 |
2.70e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 108 MEEMIEQ-LQEKVHELERQNEVLKNRLISAKQQLQvqghrqtsysRVQARVNTGRRRASASAGSQEcpgKGLRFQNVDEA 186
Cdd:COG3206 158 AEAYLEQnLELRREEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKNGLVDLSEE---AKLLLQQLSEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 187 ETvqpTLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEIlkTQLKRKENEIELSLLQLReQQATDQrsnirdnv 266
Cdd:COG3206 225 ES---QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELS-ARYTPN-------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 267 etiklHKQLVEKSNALSVIEGKF-IQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccSLEKQLHSLQDRINDLEKER 345
Cdd:COG3206 290 -----HPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLE----ARLAELPELEAELRRLEREV 360
|
250
....*....|
gi 1907189185 346 ELLKENYDKL 355
Cdd:COG3206 361 EVARELYESL 370
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
59-416 |
2.74e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.48 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 59 DENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKrlGRDVEMEEMIEQLQEKVHELERQ------------- 125
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK--GKEQELIFLLQAREKEIHDLEIQltaiktseehylk 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 126 ----------NEVLKNRLISA---------KQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGlRFQNVDEA 186
Cdd:pfam05483 472 evedlkteleKEKLKNIELTAhcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK-EMNLRDEL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 187 ETVQPTLTKYSNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIR 263
Cdd:pfam05483 551 ESVREEFIQKGDEVkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 264 DNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALM-------ANGDELNKQLKEQRLKCcslekqlhslQD 336
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakAIADEAVKLQKEIDKRC----------QH 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 337 RINDLEKERELLKENYDKLYNSAFSAAHeeQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRD 416
Cdd:pfam05483 701 KIAEMVALMEKHKHQYDKIIEERDSELG--LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-601 |
2.88e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 235 QLKRKENEIELSLLQLREQ---QATDQRSNIRDNVETI-KLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANG 310
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgiLIAALSEQLRKALFELdKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 311 DELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLynsafsaaheeqwKLKEQQMKVQIAQLETALKSDL 390
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL-------------EQQRKQLEAQIAELQSEIAERE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 391 TDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSfL 470
Cdd:COG4372 150 EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL-E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 471 EKVDSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAA 550
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907189185 551 RIQKLEAQLKdiaYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHI 601
Cdd:COG4372 309 LIGALEDALL---AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVL 356
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
185-415 |
2.93e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 185 EAETVQPTLTKYSNSLL---EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLK-----RKENEIELSLLQLREQQAt 256
Cdd:pfam07888 105 ELSASSEELSEEKDALLaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKkagaqRKEEEAERKQLQAKLQQT- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 257 dqrsnirdNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDAlmangdelnKQLKEQRLKccSLEKQLHSLQD 336
Cdd:pfam07888 184 --------EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT---------AHRKEAENE--ALLEELRSLQE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 337 RINDLEKERELLKENYDKLyNSAFSAAHEE--QWKLKEQQMKVQIAQLETALKSDLT---------------DKtEVLDK 399
Cdd:pfam07888 245 RLNASERKVEGLGEELSSM-AAQRDRTQAElhQARLQAAQLTLQLADASLALREGRArwaqeretlqqsaeaDK-DRIEK 322
|
250
....*....|....*.
gi 1907189185 400 LKTERDQNEKLVQENR 415
Cdd:pfam07888 323 LSAELQRLEERLQEER 338
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
113-503 |
3.40e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 113 EQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQA---RVNTGRRRASA-------------SAGSQECP-- 174
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEApdwEQSIGKVISPEllhrtdldpevwdGSVGGELNly 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 175 GKGLRFQNVDEAETVQPTltkysnsllEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQ 254
Cdd:pfam12128 582 GVKLDLKRIDVPEWAASE---------EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 255 ATDQRSNIRDNVETIKLHKQLVEKsnalsviegkfiqlqekqrtlrishdalmangdelnKQLKEQRLKccSLEKQLHSL 334
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAER------------------------------------KDSANERLN--SLEAQLKQL 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 335 QDRIND-LEKERELLKENydklynsafSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQN------ 407
Cdd:pfam12128 695 DKKHQAwLEEQKEQKREA---------RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDlaslgv 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 408 -----EKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLD 482
Cdd:pfam12128 766 dpdviAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE 845
|
410 420
....*....|....*....|.
gi 1907189185 483 RSMKELQATHAETVQELEKTR 503
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLR 866
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-389 |
5.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 181 QNVDEAETVQPTLTKYSNSLlEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELsllQLREQQATDQRS 260
Cdd:COG3883 27 ELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 261 NIRDNVETIKLHKQLVEKSNALSVIEG----KFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQD 336
Cdd:COG3883 103 SYLDVLLGSESFSDFLDRLSALSKIADadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907189185 337 RINDLEKERELLKENYDKLynSAFSAAHEEQWKLKEQQMKVQIAQLETALKSD 389
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
108-540 |
5.85e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 108 MEEMIEQLQEKVHELERQNEVLKNRLisakQQLQVQGHRQTSYSRVQARvntGRRRASASAGSQECPG--KGLRFQNVDE 185
Cdd:pfam10174 139 LEEMELRIETQKQTLGARDESIKKLL----EMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVllDQKEKENIHL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 186 AETVQ--------PTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEI-------------------------- 231
Cdd:pfam10174 212 REELHrrnqlqpdPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLhtedreeeikqmevykshskfmknki 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 232 --LKTQLKRKENEIELslLQLREQQATDQRSNIRDNVETIKlhKQLVEKSNALSVIEGKF----IQLQEKQRTLrishda 305
Cdd:pfam10174 292 dqLKQELSKKESELLA--LQTKLETLTNQNSDCKQHIEVLK--ESLTAKEQRAAILQTEVdalrLRLEEKESFL------ 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 306 lmangDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLynsafsaahEEQWKLKEQQM---KVQIAQL 382
Cdd:pfam10174 362 -----NKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL---------QEQLRDKDKQLaglKERVKSL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 383 ET----------ALKSDLTDKTEVLDKLKTERDQNEKLVQENRDlqlqclqqkqrlhELQSRLKFFNQESDINADDLSEA 452
Cdd:pfam10174 428 QTdssntdtaltTLEEALSEKERIIERLKEQREREDRERLEELE-------------SLKKENKDLKEKVSALQPELTEK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 453 LLLIKAQKEQKNGDLSFLEKVDSKInkdldrsmKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEtVTQKMENLQQ 532
Cdd:pfam10174 495 ESSLIDLKEHASSLASSGLKKDSKL--------KSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE-INDRIRLLEQ 565
|
....*...
gi 1907189185 533 DYELKVEQ 540
Cdd:pfam10174 566 EVARYKEE 573
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-400 |
8.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 112 IEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGsqecpgkglrfqnVDEAETVQP 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-------------IAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 192 TLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKEneielsllqlREQQATDQRSNIRDNVETIKL 271
Cdd:COG4913 679 RLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE----------EELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 272 HKQLveksnalsviEGKFIQLQEKQRTLRIShDALMANGDELNKQLKEQRLKccsLEKQLHS--------LQDRINDLEK 343
Cdd:COG4913 748 RALL----------EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMRAfnrewpaeTADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 344 ERELLKEnYDKLYNSAFsAAHEEQWK-LKEQQMKVQIAQLETALKSDLTDKTEVLDKL 400
Cdd:COG4913 814 LPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-400 |
8.86e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 221 QIEELEHLAEILKTQLKRKENEIElsllqlreqQATDQRSNIRDNVETIKlhKQLVEKSNALSVIEGKFIQLQEKQRTLR 300
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELA---------ALEARLEAAKTELEDLE--KEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 301 iSHDALMAngdeLNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLynsafsaahEEQWKLKEQQMKVQIA 380
Cdd:COG1579 87 -NNKEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL---------EAELEEKKAELDEELA 152
|
170 180
....*....|....*....|
gi 1907189185 381 QLETALKSDLTDKTEVLDKL 400
Cdd:COG1579 153 ELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-559 |
1.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELERQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 127 EVLKNRLISAKQQLQVQGHRQtsysrvqaRVNTGRRRASASAGSQECPGKGLRFQnVDEAETVQPTLTKYSN-------- 198
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYE--------EYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKklkelekr 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 199 --------SLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLKRKEnEIELSLLQLREQQAT--DQRSNIRDNVET 268
Cdd:PRK03918 354 leeleerhELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 269 IKLHK----------------QLVEKSNA-LSVIEGKFIQLQEKQRTLRishdalmANGDELNKQLKEQR--LKCCSLEK 329
Cdd:PRK03918 431 LKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELAE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 330 QLHSLQDRIN--DLEK------ERELLKENYDKLyNSAFSAAHEEQWKLKEqqMKVQIAQLETALKSDLTDKTEVLDKLK 401
Cdd:PRK03918 504 QLKELEEKLKkyNLEElekkaeEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 402 TE----RDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDiNADDLSEALLLIKAQKEQKNGDLSFLEKV-DSK 476
Cdd:PRK03918 581 ELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKAFEELAETEKRLEELRKELEELEKKySEE 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 477 INKDLDRSMKELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLD 546
Cdd:PRK03918 660 EYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVKKYKALLK 738
|
570
....*....|....
gi 1907189185 547 IRA-ARIQKLEAQL 559
Cdd:PRK03918 739 ERAlSKVGEIASEI 752
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
312-588 |
1.09e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 312 ELNKQLKEQRLKCCSLEKQLHSLQDRINDLEK----ERELLKENYDKLYNSAfsaaheeqwklkeQQMKVQIAQLETALK 387
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEA-------------KTIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 388 ---SDLTDKTEVLDKLKTER-------DQNEKLV-------------QENRDLQLQCLQQKQRLHELQSRLKFFN----- 439
Cdd:PHA02562 245 nlvMDIEDPSAALNKLNTAAakikskiEQFQKVIkmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDtaide 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 440 -QESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiNKDLDRSMKELQATHAETVQELEKTRNMLImqhKINKDYQm 518
Cdd:PHA02562 325 lEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELD---KIVKTKS- 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189185 519 evETVTQKME-----NLQQDYELKveqyvhlldiraARIQKleaqlKDIAYGTKQYKFKPEIMPDDSV----DEFDETI 588
Cdd:PHA02562 397 --ELVKEKYHrgivtDLLKDSGIK------------ASIIK-----KYIPYFNKQINHYLQIMEADYNftldEEFNETI 456
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-355 |
1.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQqatdQRSNIRDNVETIKlhKQLVEKSN 280
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQ----IRGNGGDRLEQLE--REIERLER 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189185 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLkccSLEKQLHSLQDRINDLEKERELLKENYDKL 355
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE---ALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
201-529 |
1.72e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKEN-EIELSLLQLREQQATDQRSNIrdnvetiklhKQLVEKS 279
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKI----------AQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 280 NALSvIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQrlkccslEKQLHSLQDRINDLEKERELLKENYDK---LY 356
Cdd:TIGR00606 816 QGSD-LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-------QEQIQHLKSKTNELKSEKLQIGTNLQRrqqFE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 357 NSAFSAAHEEQWKLKE-QQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQkqrlhelqsRL 435
Cdd:TIGR00606 888 EQLVELSTEVQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGY---------MK 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 436 KFFNQESDINADDlseallliKAQKEQK----NGDLSFLEKVDSKINKDLDRSMKELQATHA---------------ETV 496
Cdd:TIGR00606 959 DIENKIQDGKDDY--------LKQKETElntvNAQLEECEKHQEKINEDMRLMRQDIDTQKIqerwlqdnltlrkreNEL 1030
|
330 340 350
....*....|....*....|....*....|...
gi 1907189185 497 QELEKTRNMLIMQhkINKDYQMEVETVTQKMEN 529
Cdd:TIGR00606 1031 KEVEEELKQHLKE--MGQMQVLQMKQEHQKLEE 1061
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-532 |
1.89e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 49 ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIR-------LVNDKKRYERV-GGGPKRLGRD----VEMEEMIEQLQ 116
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEeeekaksLSKLKNKHEAMiSDLEERLKKEekgrQELEKAKRKLE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 117 EKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVN-TGRRRASASAGSQECPGKGLRFQNVDEAETVQPT-LT 194
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLA---KKEEELQAALARLEeETAQKNNALKKIRELEAQISELQEDLESERAARNkAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 195 KYSNSLLEEARGEIRNLENVIQSQRGQiEELEHLAEILKTQLKR------KENEIELSLLQLREQQATDQrsnIRDNVET 268
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQ-QELRSKREQEVTELKKaleeetRSHEAQLQEMRQKHTQALEE---LTEQLEQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 269 IKLHKQLVEKSNAlsVIEGKFIQLQEKQRTLRIShdalmangdelnKQLKEQRLKccSLEKQLHSLQDRINDLEKERELL 348
Cdd:pfam01576 368 AKRNKANLEKAKQ--ALESENAELQAELRTLQQA------------KQDSEHKRK--KLEGQLQELQARLSESERQRAEL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 349 KENYDKLYNSAFSAAHeeqwKLKEQQMK-VQIAQLETALKSDLTDKTEVLDKlktERDQNEKLVQENRDLQLQCLQ-QKQ 426
Cdd:pfam01576 432 AEKLSKLQSELESVSS----LLNEAEGKnIKLSKDVSSLESQLQDTQELLQE---ETRQKLNLSTRLRQLEDERNSlQEQ 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 427 RLHELQSRLKFFNQESDINAddlseALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQaTHAETVQELEKTRNML 506
Cdd:pfam01576 505 LEEEEEAKRNVERQLSTLQA-----QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE-EKAAAYDKLEKTKNRL 578
|
490 500
....*....|....*....|....*.
gi 1907189185 507 imqhkinkdyQMEVETVTQKMENLQQ 532
Cdd:pfam01576 579 ----------QQELDDLLVDLDHQRQ 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
270-436 |
2.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 270 KLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLK 349
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 350 ENYDKLYNSAFSAAHEEQWKLK----------------EQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERDQNEKLVQE 413
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLlspedfldavrrlqylKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|...
gi 1907189185 414 NRDLQLQCLQQKQRLHELQSRLK 436
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLE 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-501 |
2.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 28 QETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDVE 107
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE---------ELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 108 MEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNT---GRRRASASAGSQECPGKGLRFQNVD 184
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeleELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 185 EAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRD 264
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 265 NVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHD---------------ALMANGDELNKQLKEQRLKCCSLEK 329
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveaayeaaleaALAAALQNIVVEDDEVAAAAIEYLK 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 330 Q----------------------LHSLQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALK 387
Cdd:COG1196 568 AakagratflpldkiraraalaaALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 388 SDLTDKTEV-----------------LDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLS 450
Cdd:COG1196 648 EVTLEGEGGsaggsltggsrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1907189185 451 EALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAETVQELEK 501
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| C2B_RasGAP |
cd08675 |
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ... |
782-889 |
2.63e-03 |
|
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.
Pssm-ID: 176057 [Multi-domain] Cd Length: 137 Bit Score: 39.66 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQ----------SRASYLQPHAYVVYKffdfpdhdTAIVPSSNDPQFDDHMCFPVPMNMDLDRY---LKS 848
Cdd:cd08675 1 LSVRVLECRDLAlksngtcdpfARVTLNYSSKTDTKR--------TKVKKKTNNPRFDEAFYFELTIGFSYEKKsfkVEE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907189185 849 ESLSFY-----VFDDSDTQENIYMGKVNVPLISLAHDKCISGIFEL 889
Cdd:cd08675 73 EDLEKSelrveLWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFL 118
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
327-521 |
3.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 327 LEKQLHSLQDRINDLEKERELLKENYDKLYNSAFSAahEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQ 406
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRD--REQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 407 NEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQ-------ESDINADDLSEALLLIK---AQKEQKNGDLSFLEKVDSK 476
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKeeeAERKQLQAKLQQTEEELRS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907189185 477 INKDLdRSMKELQATHAETVQELEKTRNMLimQHKINKDYQMEVE 521
Cdd:pfam07888 190 LSKEF-QELRNSLAQRDTQVLQLQDTITTL--TQKLTTAHRKEAE 231
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-515 |
3.41e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 65 KQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEV------------LKNR 132
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAkkkaeeakkadeAKKK 1452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 133 LISAK--QQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAETVQPTLTKYSNSL-------LEE 203
Cdd:PTZ00121 1453 AEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeakkAEE 1532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 204 ARG--EIRNLENVIQSQR-GQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLveKSN 280
Cdd:PTZ00121 1533 AKKadEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 281 ALSVIEGKFIQLQE---------KQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKEN 351
Cdd:PTZ00121 1611 EAKKAEEAKIKAEElkkaeeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 352 YDKLYNSAFSAAHEEQWKLKEQQMKVQIAQL-----ETALKSDLTDKTEVLDKLKTERDQNEklvQENRDLQLQCLQQKQ 426
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaeeENKIKAEEAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEE 1767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 427 RLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKvdskiNKDLDRSMKELQATHAETVQELEKTRNML 506
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEG-----GKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
490
....*....|....*
gi 1907189185 507 ------IMQHKINKD 515
Cdd:PTZ00121 1843 leeadaFEKHKFNKN 1857
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-554 |
3.73e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 209 RNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQAtdQRSNIRDNVEtiKLHKQLVEKSNALSVIEGK 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 289 FIQLQEKQRTLRISHDALMAN-GDELNKQLKEQRLKcCSLEKQLHSLQDRINDLEKERELLKENYDKLYNSAFSAAHEEQ 367
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTElEDTLDTTAAQQELR-SKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 368 wklkeQQMKVQIAQLETALKSDLTDKTEVLDKLKTerdqnekLVQENRDLQLQCLQQKQRLHELQSRLkffnQESDINAD 447
Cdd:pfam01576 366 -----EQAKRNKANLEKAKQALESENAELQAELRT-------LQQAKQDSEHKRKKLEGQLQELQARL----SESERQRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 448 DLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQAThaetvQEL--EKTRNMLIMQHKINkdyQMEVETvTQ 525
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQKLNLSTRLR---QLEDER-NS 500
|
330 340 350
....*....|....*....|....*....|.
gi 1907189185 526 KMENLQQDYELK--VEQYVHLLDIRAARIQK 554
Cdd:pfam01576 501 LQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
35-352 |
4.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 35 TVKTRQAVSRVSREELEDRFLRLHDENiLLKQHARKQEDKIKRMAT------KLIRLVNDKKRYerVGGGPKrLGRDVEM 108
Cdd:PRK04863 760 VVKIADRQWRYSRFPEVPLFGRAAREK-RIEQLRAEREELAERYATlsfdvqKLQRLHQAFSRF--IGSHLA-VAFEADP 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 109 EEMIEQLQEKVHELER-------QNEVLKNRLISAKQQLQvQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGL--- 178
Cdd:PRK04863 836 EAELRQLNRRRVELERaladhesQEQQQRSQLEQAKEGLS-ALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRfvq 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 179 RFQN-VDEAETVQPTLT-------------KYSNSLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQ 235
Cdd:PRK04863 915 QHGNaLAQLEPIVSVLQsdpeqfeqlkqdyQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQR 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 236 LKRKENEIELSLLQLREQQATDQRSNirdnvetiKLHKQLVeksnalSVIEGKFIQLQEKQR-----TLRISHDA---LM 307
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYN--------QVLASLK------SSYDAKRQMLQELKQelqdlGVPADSGAeerAR 1059
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907189185 308 ANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENY 352
Cdd:PRK04863 1060 ARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-409 |
4.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILK------TQLKRKENEIELSLLQLREqqatdQRSNIRDNVETIKLH-K 273
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEE-----KIRELEERIEELKKEiE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 274 QLVEKSNALSVIEGKfiqlQEKQRTLRishdALMangDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYD 353
Cdd:PRK03918 277 ELEEKVKELKELKEK----AEEYIKLS----EFY---EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189185 354 KLYNSAFSAAHEEQWKLKEQQMKVQIAQLETaLKSDLTDKTevLDKLKTERDQNEK 409
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGLT--PEKLEKELEELEK 398
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-363 |
4.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLqvqghrqtsySRVQARVNTGRRRasasagsqecpgkglrfqnvdea 186
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRI----------AALARRIRALEQE----------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 187 etvqptltkysnslLEEARGEIRNLENVIQSQRGQIEELEH-LAEILKTQLKRKENEIELSLLQLREQQATDQRS----- 260
Cdd:COG4942 78 --------------LAALEAELAELEKEIAELRAELEAQKEeLAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylky 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 261 ---NIRDNVETIKLHKQLVEKSNAlsviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDR 337
Cdd:COG4942 144 lapARREQAEELRADLAELAALRA---------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
250 260
....*....|....*....|....*.
gi 1907189185 338 INDLEKERELLKENYDKLYNSAFSAA 363
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-504 |
4.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 261 NIRDNVETIK-LHKQLV---EKSNALSVIEG---KFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccSLEKQLHS 333
Cdd:COG4913 229 ALVEHFDDLErAHEALEdarEQIELLEPIRElaeRYAAARERLAELEYLRAALRLWFAQRRLELLEAELE--ELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 334 LQDRINDLEKERELLKENYDKLynsafsaaheeqwklKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERDQneklvqe 413
Cdd:COG4913 307 LEAELERLEARLDALREELDEL---------------EAQIRGNGGDRLE-QLEREIERLERELEERERRRAR------- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 414 nrdlqlqclqqkqrlheLQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHA 493
Cdd:COG4913 364 -----------------LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250
....*....|.
gi 1907189185 494 EtVQELEKTRN 504
Cdd:COG4913 427 E-IASLERRKS 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
328-563 |
5.61e-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: 41.20 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 328 EKQLHSLQ---DRINDLEKErelLKENYDKLYNSAFSA--AHEEQWKLKEQQMKVQIAQLETA------LKSDLTDKTEV 396
Cdd:TIGR02168 178 ERKLERTRenlDRLEDILNE---LERQLKSLERQAEKAerYKELKAELRELELALLVLRLEELreeleeLQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 397 LDKLKTERDQNEKLVQENRDLQLQCLQQKqrlHELQSRLKFFNQEsdinADDLSEALLLIKAQKEQKNGDLS----FLEK 472
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEI---EELQKELYALANE----ISRLEQQKQILRERLANLERQLEeleaQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 473 VDSKINKDLDRS------MKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKveqyvhlld 546
Cdd:TIGR02168 328 LESKLDELAEELaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL--------- 398
|
250
....*....|....*..
gi 1907189185 547 irAARIQKLEAQLKDIA 563
Cdd:TIGR02168 399 --NNEIERLEARLERLE 413
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
229-545 |
6.19e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 229 AEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNV--------ETIKLHKQLVEKSNALSVI----EGKFIQLQEKQ 296
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaEAEEMRARLAARKQELEEIlhelESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 297 RTLRISHDALMANGDELNKQLKE-----QRL---------KCCSLEKQLHSLQDRINDLEKERELLKENYDKLYnsafSA 362
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEeeaarQKLqlekvtteaKIKKLEEDILLLEDQNSKLSKERKLLEERISEFT----SN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 363 AHEEQWKLKeqqmkvQIAQLETALKSDLTDkteVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQES 442
Cdd:pfam01576 168 LAEEEEKAK------SLSKLKNKHEAMISD---LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 443 DINADDLSEALLLIKAQKEQKNGDLsflekvdskinkdldRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVET 522
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNAL---------------KKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA 303
|
330 340
....*....|....*....|....*....
gi 1907189185 523 VTQKME------NLQQDYELKVEQYVHLL 545
Cdd:pfam01576 304 LKTELEdtldttAAQQELRSKREQEVTEL 332
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
207-397 |
6.99e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.12 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIelsllqlreQQATDQRSNIrdnvetiklhKQLVEKSNalsvie 286
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKENRLLKRLQKRQEKAL---------GKYEGTESEL----------PQLIARHN------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 287 gkfiqlqEKQRTLRISHDALMANGDELNKQLKE------------QRLKCCS----------LEKQLHSLQDRINDLEKE 344
Cdd:pfam15619 67 -------EEVRVLRERLRRLQEKERDLERKLKEkeaellrlrdqlKRLEKLSedknlaereeLQKKLEQLEAKLEDKDEK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189185 345 RELLkENYDKLYNSAFSAA-HEEQWKLKEQQMKVQIAQLE-TALKSDLTDKTEVL 397
Cdd:pfam15619 140 IQDL-ERKLELENKSFRRQlAAEKKKHKEAQEEVKILQEEiERLQQKLKEKEREL 193
|
|
| C2B_RasA3 |
cd04010 |
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ... |
782-877 |
7.62e-03 |
|
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA3 contains an N-terminal C2 domain, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.
Pssm-ID: 175977 [Multi-domain] Cd Length: 148 Bit Score: 38.53 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 782 LHVTVKCCTGLQSRASYLQPHAYV--VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDLDRYLK---SESLSFY-- 854
Cdd:cd04010 2 LSVRVIECSDLALKNGTCDPYASVtlIYSNKKQDTKRTKVKKKTNNPQFDEAFYFDVTIDSSPEKKQFempEEDAEKLel 81
|
90 100
....*....|....*....|....*.
gi 1907189185 855 ---VFDDSDTQENIYMGKVNVPLISL 877
Cdd:cd04010 82 rvdLWHASMGGGDVFLGEVRIPLRGL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-361 |
8.58e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 151 SRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAETVQptltKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAE 230
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG----SRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 231 ILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFI--QLQEKQRTLRIS------ 302
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDleELERELERLEREiealgp 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189185 303 --------HDALMANGDELNKQLKEqrlkccsLEKQLHSLQDRINDLEKE-RELLKENYDKLyNSAFS 361
Cdd:COG1196 782 vnllaieeYEELEERYDFLSEQRED-------LEEARETLEEAIEEIDREtRERFLETFDAV-NENFQ 841
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
201-413 |
9.94e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQ---LKRKENEIEL---SLLQLREQQATDQRSNIRDNVETIKLHkq 274
Cdd:PRK04863 839 LRQLNRRRVELERALADHESQEQQQRSQLEQAKEGlsaLNRLLPRLNLladETLADRVEEIREQLDEAEEAKRFVQQH-- 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189185 275 lvekSNALSVIEGKFIQLQEKQRtlriSHDALMANGDELNKQLKEQRLKCCSL----EKQLH-SLQDRINDLEKERELlk 349
Cdd:PRK04863 917 ----GNALAQLEPIVSVLQSDPE----QFEQLKQDYQQAQQTQRDAKQQAFALtevvQRRAHfSYEDAAEMLAKNSDL-- 986
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189185 350 enydklyNSAFSAAHEEqwklKEQQMKVQIAQLETAlKSDLTDKTEVLDKLKTERDQNEKLVQE 413
Cdd:PRK04863 987 -------NEKLRQRLEQ----AEQERTRAREQLRQA-QAQLAQYNQVLASLKSSYDAKRQMLQE 1038
|
|
| |
