|
Name |
Accession |
Description |
Interval |
E-value |
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
992-1155 |
5.48e-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: 214.20 E-value: 5.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 992 PSEEIRIEIIALNL-NDSQITREDTIQRLFIECRFYSLPAE--ETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDIL 1068
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 1069 KAILQRRELPHRSVRFTVVSDPPeDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHA 1148
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 568956785 1149 LRSVYEQ 1155
Cdd:pfam18111 160 LRAIYSE 166
|
|
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
601-727 |
5.98e-62 |
|
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: 207.48 E-value: 5.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 601 TIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKN 680
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568956785 681 TVTLELHQAHSTDYETIAACQLRFHEILEK-SGRIFCTTSLVDHDTAI 727
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEI 128
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-449 |
1.19e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-------QRLKCCSLEKQLHSVrfsERRVEELQDRINDLEK 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAAT---ERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 354 ERELLKENYDKLynSAFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQL 433
Cdd:TIGR02168 853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
250
....*....|....*.
gi 568956785 434 QCLQQKQRLHELQSRL 449
Cdd:TIGR02168 930 RLEGLEVRIDNLQERL 945
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-562 |
1.96e-08 |
|
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: 58.98 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 123 ERQNEVLKNRliSAKQQLQVQGHRQTSYSRvqaRVNTGRRRASASAGSQECPGKGLR----FQNVDEAETVQPTLTkysn 198
Cdd:pfam15921 397 KEQNKRLWDR--DTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLT---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 199 SLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----------LQLREQQ----ATDQRSNIR 263
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrsrvdLKLQELQhlknEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 264 DNVETIKLhkQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLeKQLHSVRfsERRVEE 343
Cdd:pfam15921 548 TECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF-KILKDKK--DAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 344 LQDRINDLEKERELL--------------KENYDKLYNSAFSAAHE------------EQWKLKEQQMKVQIAQLETALK 397
Cdd:pfam15921 623 LEARVSDLELEKVKLvnagserlravkdiKQERDQLLNEVKTSRNElnslsedyevlkRNFRNKSEEMETTTNKLKMQLK 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 398 SDLTDKTEVLDKLKTERGplinQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALllikaqKEQK 477
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEG----SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL-EEAMTNANKEKHFL------KEEK 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 478 NGDLSFLEKVDSKINKdldrSMKELQATHAETVQELEKTRNMLIMQHKINKDYQmEVETVTQKMEnlQQDYELKVEqyvH 557
Cdd:pfam15921 772 NKLSQELSTVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---H 841
|
....*
gi 568956785 558 LLDIR 562
Cdd:pfam15921 842 TLDVK 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-427 |
4.60e-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: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 197 SNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLR--EQQATDQRSNIRDNVETI-KLHK 273
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEKEIaELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 274 QLVEKSNALSviegkfIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccsLEKQLHSVRfsERRVEELQDRINDLEK 353
Cdd:COG4942 98 ELEAQKEELA------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYLAPAR--REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956785 354 ERELLKENYDKLynSAFSAAHEEQwKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQE 427
Cdd:COG4942 165 LRAELEAERAEL--EALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-592 |
4.06e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 223 EELEHLAEILKTQLKRKENEIELSLLQLREQQAT---------DQRSNIRDNVETIKLH----KQLVEKSNAL-SVIEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 289 FIQLQEKQRTLRISHDALMANGDELNK--QLKEQRLKCCSLEKQLHSVrfserRVEELQDRINDLEkerELLKENYDKLY 366
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQltEEKEAQMEELNKAKAAHSF-----VVTEFEATTCSLE---ELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 367 NSafsaahEEQWKLKEQQMKVQIAQLETALKsdLTDKTEV-LDKLKTergpLINQNEKLVQENRDLQLQCLQQKQRLHE- 444
Cdd:pfam05483 374 KN------EDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKK----ILAEDEKLLDEKKQFEKIAEELKGKEQEl 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 445 ---LQSRLK-FFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKD-LDRSMKELQATHAETVQELEKTRNM 519
Cdd:pfam05483 442 iflLQAREKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQED 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956785 520 LIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPD 592
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
715-789 |
1.84e-05 |
|
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: 44.75 E-value: 1.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956785 715 FCTTSLVD---HDTAIVPSSNDPQFDDHMCFPVPMNMdldrylkSESLSFYVFDDSDTQENIYMGKVNVPLISLAHDK 789
Cdd:cd00030 23 YVKVSLGGkqkFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRFSKDDFLGEVEIPLSELLDSG 93
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-413 |
4.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSysrvqARVNTGRRRASASAGSQEcpgkglRFQNVDEA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEAR------REELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 187 ETVQPTltkysnslLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQatDQRSNIRDNV 266
Cdd:PRK02224 324 EELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 267 ETikLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-QRL----KC--C--SLEKQLHSVRFS 337
Cdd:PRK02224 394 EE--LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaEALleagKCpeCgqPVEGSPHVETIE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956785 338 ERR--VEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDlTDKTEVLDKLKTE 413
Cdd:PRK02224 472 EDRerVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERAEELRERAAE 548
|
|
| C2 |
pfam00168 |
C2 domain; |
725-797 |
2.40e-04 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 41.54 E-value: 2.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956785 725 TAIVPSSNDPQFDDHMCFPVPMNMDldrylksESLSFYVFDDSDTQENIYMGKVNVPLISLAHDKCISGIFEL 797
Cdd:pfam00168 39 TKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-576 |
1.20e-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: 42.44 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 368 SAFSAAHEEQWKLKEQ--QMKVQIAQLETALKSDLTDKTEVLDKLKTERGpLINQNEKLVQENRDLQLQCLQQKQrlhEL 445
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELA---EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 446 QSRLKFFNQESDINADDLSEalLLIKAQKEQKNGDLSFLEKVDS--------KINKDLDRSMKELQATHAETVQELEKTR 517
Cdd:COG4942 89 EKEIAELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956785 518 NMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI 576
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
725-785 |
2.39e-03 |
|
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: 38.62 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956785 725 TAIVPSSNDPQFDDHMCFPVPmnmdldrYLKSESLSFYVFDDSDTQENIYMGKVNVPLISL 785
Cdd:smart00239 39 TKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKDRFGRDDFIGQVTIPLSDL 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
68-573 |
2.45e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 68 ARKQEDKIKRMATKLIRLVNDKKRYERVGGgpKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISaKQQLQVQGHRQ 147
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 148 TSYSRVQARVNtgrRRASASAGSQecpgkGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQrgQIEELEH 227
Cdd:TIGR00618 311 RIHTELQSKMR---SRAKLLMKRA-----AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 228 LAEI--LKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQLVEKSNALSVIEgKFIQLQEKQRTLRIS 302
Cdd:TIGR00618 381 IHTLqqQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaKKQQELQQRYAELCA-AAITCTAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 303 HDALMANG-DELNKQL--KEQRLKCCSLEKQLHSVRFSE-----------------------------RRVEELQDRIND 350
Cdd:TIGR00618 460 HLQESAQSlKEREQQLqtKEQIHLQETRKKAVVLARLLElqeepcplcgscihpnparqdidnpgpltRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 351 LEKERELLKENYDKLYNSAFSAAHEEQwklKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRd 430
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQ---EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 431 lqlqclqqkqrLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFlEKVDSKInkdldRSMKELQATHAETV 510
Cdd:TIGR00618 616 -----------ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ-ERVREHA-----LSIRVLPKELLASR 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956785 511 QELEKTrnmliMQHKInkdyqmevETVTQKMENLQQDYELKVEQYVHLLDIR----------AARIQKLEAQL 573
Cdd:TIGR00618 679 QLALQK-----MQSEK--------EQLTYWKEMLAQCQTLLRELETHIEEYDrefneienasSSLGSDLAARE 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-573 |
4.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELERQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 127 EVLKNRLISAKQQLQVQGHRQtSYSRVQARVNTGRRRASASAGS-----QECPGKGLRFQNV-DEAETVQPTLT--KYSN 198
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGieeriKELEEKEERLEELkKKLKELEKRLEelEERH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 199 SLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLKRKEnEIELSLLQLREQQAT--DQRSNIRDNVETIKLHK--- 273
Cdd:PRK03918 362 ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIEELKKAKgkc 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 274 -------------QLVEKSNA-LSVIEGKFIQLQEKQRTLRishdalmANGDELNKQLKEQR--LKCCSLEKQLHSV--R 335
Cdd:PRK03918 439 pvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELAEQLKELeeK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 336 FSERRVEELQDRindlEKERELLKENYDKLyNSAFSAAHEEQWKLKEqqMKVQIAQLETALKSDLTDKTEVLDKLKTERG 415
Cdd:PRK03918 512 LKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAELLKELEELGF 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 416 PLINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDiNADDLSEALLLIKAQKEQKNGDLSFLEKV-DSKINKD 494
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKAFEELAETEKRLEELRKELEELEKKySEEEYEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 495 LDRSMKELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRA- 563
Cdd:PRK03918 664 LREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVKKYKALLKERAl 742
|
570
....*....|
gi 568956785 564 ARIQKLEAQL 573
Cdd:PRK03918 743 SKVGEIASEI 752
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
992-1155 |
5.48e-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: 214.20 E-value: 5.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 992 PSEEIRIEIIALNL-NDSQITREDTIQRLFIECRFYSLPAE--ETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDIL 1068
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 1069 KAILQRRELPHRSVRFTVVSDPPeDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHA 1148
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 568956785 1149 LRSVYEQ 1155
Cdd:pfam18111 160 LRAIYSE 166
|
|
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
601-727 |
5.98e-62 |
|
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: 207.48 E-value: 5.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 601 TIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKN 680
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568956785 681 TVTLELHQAHSTDYETIAACQLRFHEILEK-SGRIFCTTSLVDHDTAI 727
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEI 128
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-449 |
1.19e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-------QRLKCCSLEKQLHSVrfsERRVEELQDRINDLEK 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAAT---ERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 354 ERELLKENYDKLynSAFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQL 433
Cdd:TIGR02168 853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
250
....*....|....*.
gi 568956785 434 QCLQQKQRLHELQSRL 449
Cdd:TIGR02168 930 RLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-414 |
6.48e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 101 RLGRDVEmeemIEQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAgsqecpgkglrf 180
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALR------------ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 181 QNVDEAETVQPTLTKYSNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA-- 255
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLskeLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAel 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 256 TDQRSNIRDNVETIK-LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSV 334
Cdd:TIGR02168 813 TLLNEEAANLRERLEsLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 335 RFserRVEELQDRINDLEKERELLKENYDKLynsafsAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTER 414
Cdd:TIGR02168 893 RS---ELEELSEELRELESKRSELRRELEEL------REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-490 |
8.74e-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: 66.62 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 106 VEMEEMIEQLQEKVHELERQnevlknrlisaKQQLQVQGHRQTSYSRVQARVNTGRRRASAsagsqecpgkgLRFQN-VD 184
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERYKELKAELRELELALLV-----------LRLEElRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 185 EAETVQPTLTKYsNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSN 261
Cdd:TIGR02168 240 ELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 262 IRDNVETIKLHKQLVEKSNALSviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRfseRRV 341
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR---SKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 342 EELQDRINDLEKERELLKENYDKLynsafsAAHEEQWK--LKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERGPLIN 419
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERL------EDRRERLQqeIEELLKKLEEAELK-ELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956785 420 QNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALLLIKAQKEQKNGD---LSFLEKVDSK 490
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEG 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-604 |
2.91e-10 |
|
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: 64.66 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 114 QLQEKVHELERQNEVLKNRLISAKQQLQVQghrQTSYSRVQARVNtgrrrasasagsqecpgkglrfQNVDEAETVQPTL 193
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEK---TTEISNTQTQLN----------------------QLKDEQNKIKKQL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 194 TKySNSLLEEARGEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLKRKENEIELSLLQLRE-----QQATDQRSNIR 263
Cdd:TIGR04523 270 SE-KQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 264 D-----NVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDAL---MANGDELNKQlKEQRLKCCSLEKQLHSVR 335
Cdd:TIGR04523 349 KeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQ-KDEQIKKLQQEKELLEKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 336 FSERRVE--ELQDRINDLEKERELLKENYDKLYNsaFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTE 413
Cdd:TIGR04523 428 IERLKETiiKNNSEIKDLTNQDSVKELIIKNLDN--TRESLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELKKLNEE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 414 RGPLINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKffNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiNK 493
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----QK 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 494 DLDRSMKELQathaETVQELEKTRNMLIMQHKInkdYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRAARIQKLEAQL 573
Cdd:TIGR04523 579 SLKKKQEEKQ----ELIDQKEKEKKDLIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQI 650
|
490 500 510
....*....|....*....|....*....|...
gi 568956785 574 KDIAYGTKQYkfKPEIMPD--DSVDEFDETIHL 604
Cdd:TIGR04523 651 KETIKEIRNK--WPEIIKKikESKTKIDDIIEL 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-562 |
1.96e-08 |
|
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: 58.98 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 123 ERQNEVLKNRliSAKQQLQVQGHRQTSYSRvqaRVNTGRRRASASAGSQECPGKGLR----FQNVDEAETVQPTLTkysn 198
Cdd:pfam15921 397 KEQNKRLWDR--DTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLT---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 199 SLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----------LQLREQQ----ATDQRSNIR 263
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrsrvdLKLQELQhlknEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 264 DNVETIKLhkQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLeKQLHSVRfsERRVEE 343
Cdd:pfam15921 548 TECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF-KILKDKK--DAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 344 LQDRINDLEKERELL--------------KENYDKLYNSAFSAAHE------------EQWKLKEQQMKVQIAQLETALK 397
Cdd:pfam15921 623 LEARVSDLELEKVKLvnagserlravkdiKQERDQLLNEVKTSRNElnslsedyevlkRNFRNKSEEMETTTNKLKMQLK 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 398 SDLTDKTEVLDKLKTERGplinQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALllikaqKEQK 477
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEG----SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL-EEAMTNANKEKHFL------KEEK 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 478 NGDLSFLEKVDSKINKdldrSMKELQATHAETVQELEKTRNMLIMQHKINKDYQmEVETVTQKMEnlQQDYELKVEqyvH 557
Cdd:pfam15921 772 NKLSQELSTVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---H 841
|
....*
gi 568956785 558 LLDIR 562
Cdd:pfam15921 842 TLDVK 846
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-576 |
4.37e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndkkRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 116 QEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNtgrrraSASAGSQECPGKGLRFQnvDEAETVQ-PTLT 194
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR------SILVDFEEASGKKIYEH--DSMSTMHfRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEEL----EHLAEILKTQLKRK------ENEIELSLLQLREQQATDQRSNIRD 264
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQDRieqlisEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 265 NVETIklhKQLVEKSNA-----LSVIEGKFIQLQEKQRTL-RISHDALmangDELNKQ--LKEQRLKCCSLEKQLHSvRF 336
Cdd:pfam15921 300 QLEII---QEQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKI----EELEKQlvLANSELTEARTERDQFS-QE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 337 SERRVEELQDRINDL---EKERELLKENYDKLYN----SAFSAAHEEQwKLKEQQMKVQiaQLETALKsdlTDKTEVLDK 409
Cdd:pfam15921 372 SGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQ--RLEALLK---AMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 410 LKTERGPLINQNEKLVQENR---DLQLQCLQQKQRLHELQSRlKFFNQESDINADDLSEALLLIKAQKEQKNGDLsflek 486
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSltaQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKERAIEATNAEI----- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 487 vdSKINKDLDRSMKELQ-----ATHAETVQ-ELEKTRNMLIMQHKINKDYQMEVETVTQ-----------------KMEN 543
Cdd:pfam15921 520 --TKLRSRVDLKLQELQhlkneGDHLRNVQtECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvekaQLEK 597
|
570 580 590
....*....|....*....|....*....|...
gi 568956785 544 LQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI 576
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-427 |
4.60e-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: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 197 SNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLR--EQQATDQRSNIRDNVETI-KLHK 273
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEKEIaELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 274 QLVEKSNALSviegkfIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccsLEKQLHSVRfsERRVEELQDRINDLEK 353
Cdd:COG4942 98 ELEAQKEELA------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYLAPAR--REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956785 354 ERELLKENYDKLynSAFSAAHEEQwKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQE 427
Cdd:COG4942 165 LRAELEAERAEL--EALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-484 |
7.54e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 101 RLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQEcpgKGLRF 180
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE---QDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 181 QNVDEAETVQptltkysnsLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKrkenEIELSLLQLREQQATDQRS 260
Cdd:COG1196 307 LEERRRELEE---------RLEELEEELAELEEELEELEEELEELEEELEEAEEELE----EAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 261 NIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccslEKQLHsvrfsERR 340
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE----EEEEE-----EAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 341 VEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLInq 420
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL-- 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956785 421 nEKLVQENRDLQLQCLQQKQRlhELQSRLKffnqesDINADDLSEALLLIKAQKEQKNGDLSFL 484
Cdd:COG1196 523 -AGAVAVLIGVEAAYEAALEA--ALAAALQ------NIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
207-602 |
1.83e-07 |
|
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: 55.41 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 207 EIRNLENVIQSQRGQIEELEHLAEILKTqLKRKENEIELSLLQLREQQatdqrSNIRDNVEtiKLHKQLVEKSNALSVIE 286
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISELKKQN-----NQLKDNIE--KKQQEINEKTTEISNTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 287 GKFIQLQEKQrtlrishdalmangDELNKQLKEQRLKCCSLEKQLHSVrfsERRVEELQDRINDLEKEREllkENYDKLY 366
Cdd:TIGR04523 253 TQLNQLKDEQ--------------NKIKKQLSEKQKELEQNNKKIKEL---EKQLNQLKSEISDLNNQKE---QDWNKEL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 367 NSAFSAAHEEQWKLKEQ---------QMKVQIAQLET----------ALKSDLTDKTEVLDKLKTERGPLINQNEKLVQE 427
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQisqnnkiisQLNEQISQLKKeltnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 428 NRDLQLQCLQQKQRLHELQSRLKFFNQESDInaddLSEALLLIKAQKEQKNGDLSFLEKVDS----KIN----------- 492
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKEL----LEKEIERLKETIIKNNSEIKDLTNQDSvkelIIKnldntreslet 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 493 --KDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQdyelKVEQYVHLLDIRAARIQKLE 570
Cdd:TIGR04523 469 qlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE----KIEKLESEKKEKESKISDLE 544
|
410 420 430
....*....|....*....|....*....|..
gi 568956785 571 AQLKDIAYGTKQYKFKPEImpddsvDEFDETI 602
Cdd:TIGR04523 545 DELNKDDFELKKENLEKEI------DEKNKEI 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-582 |
2.14e-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: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELE---HLAEILKtQLKRKENEIELSLLQLREQQATDQRSNIRD-----NVETIKLH 272
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLErqaEKAERYK-ELKAELRELELALLVLRLEELREELEELQEelkeaEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 273 KQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSV----RFSERRVEELQDRI 348
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELeaqlEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 349 NDLEKERELLKENYDklynsAFSAAHEEQWKLKEqqmkvqiaqletALKSDLTDKTEVLDKLKTERgplinqneklvqen 428
Cdd:TIGR02168 340 AELEEKLEELKEELE-----SLEAELEELEAELE------------ELESRLEELEEQLETLRSKV-------------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 429 rdlqlqclqqkqrlHELQsrlkffNQESDINADdlseaLLLIKAQKEQKNGDLSFLEKVDSKINKDLDRS-MKELQATHA 507
Cdd:TIGR02168 389 --------------AQLE------LQIASLNNE-----IERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELE 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956785 508 ETVQELEKTRNMLImqhkinkDYQMEVETVTQKMENLQQDYeLKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQ 582
Cdd:TIGR02168 444 ELEEELEELQEELE-------RLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-577 |
2.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEksn 280
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 281 alsviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccSLEKQLHSVRFSERRVEELQDRINDLEKERELLKE 360
Cdd:COG4717 160 ----------ELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 361 NYDKLYNSAFSAAHEEQWKLKEQQMKV--QIAQLETALKSDLTDKTEVLDKLKTERGPLI-------NQNEKLVQENRDL 431
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLVLGLLAllflllaREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 432 QLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQkngdLSFLEKVDSKInkDLDRSMKELQATHAETVQ 511
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956785 512 ELEKTRNMLIMQHKINKDYQMEVETVTQKMENLqqDYELKVEQYVHLLDIRAARIQKLEAQLKDIA 577
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-358 |
3.74e-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: 54.68 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELERQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 126 NEVLKNRLISAKQQLQVQghrQTSYSRVQARVntgrrrASASAGSQECPGKglrfqnVDEAETVQPTLTKYSNSL---LE 202
Cdd:TIGR02168 318 LEELEAQLEELESKLDEL---AEELAELEEKL------EELKEELESLEAE------LEELEAELEELESRLEELeeqLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 203 EARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDqrsnirdnvetikLHKQLVEKSNAL 282
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE-------------LQAELEELEEEL 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956785 283 SVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQlhsvrfsERRVEELQDRINDLEKERELL 358
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL-------QENLEGFSEGVKALLKNQSGL 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-572 |
4.96e-07 |
|
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: 54.26 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSNIRDNVETIKL 271
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKnklEVELNKLEKQKKENKKNIDKFLTEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 272 HKQLVEKSNalsviegKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSERRVEELQDRINDL 351
Cdd:TIGR04523 151 EKELEKLNN-------KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 352 EKERELLKENYDKLynsafsaaheeqwKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDL 431
Cdd:TIGR04523 224 KKQNNQLKDNIEKK-------------QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 432 QlqclqqkqrlhELQSRLKFFNQESDINAD-DLSEALLLIKAQKEQKNGDLSFLEKVDSKIN---KDLDRSMKELQATHA 507
Cdd:TIGR04523 291 N-----------QLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNeqiSQLKKELTNSESENS 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956785 508 ETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIraaRIQKLEAQ 572
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDE---QIKKLQQE 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-412 |
5.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 101 RLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrf 180
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEE-------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 181 QNVDEAETVQPTLTKYSNSLlEEARGEIRNLENVIQSQRGQIEELEhlaeilktqlkRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEI-ENVKSELKELEARIEELEEDLHKLE-----------EALNDLEARLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 261 nirdnvetiKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVrfsERR 340
Cdd:TIGR02169 802 ---------KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEE 869
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956785 341 VEELQDRINDLEKERELLKENYDKLynsafsAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKT 412
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDEL------EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-574 |
6.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLKRKEneIELSLLQLREQQATDQRsnirdnvetikLHKQ 274
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 275 LVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccsLEKQLHSVRFSERRVEELQDRINDLEKE 354
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 355 RELLKEnydklynsafsaaHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLktergplinqneklvqenrdlqlq 434
Cdd:COG1196 325 LAELEE-------------ELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL------------------------ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 435 clqqkqrlHELQSRLkffnQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRsMKELQATHAETVQELE 514
Cdd:COG1196 368 --------LEAEAEL----AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELE 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 515 KTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLK 574
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-592 |
4.06e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 223 EELEHLAEILKTQLKRKENEIELSLLQLREQQAT---------DQRSNIRDNVETIKLH----KQLVEKSNAL-SVIEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 289 FIQLQEKQRTLRISHDALMANGDELNK--QLKEQRLKCCSLEKQLHSVrfserRVEELQDRINDLEkerELLKENYDKLY 366
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQltEEKEAQMEELNKAKAAHSF-----VVTEFEATTCSLE---ELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 367 NSafsaahEEQWKLKEQQMKVQIAQLETALKsdLTDKTEV-LDKLKTergpLINQNEKLVQENRDLQLQCLQQKQRLHE- 444
Cdd:pfam05483 374 KN------EDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKK----ILAEDEKLLDEKKQFEKIAEELKGKEQEl 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 445 ---LQSRLK-FFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKD-LDRSMKELQATHAETVQELEKTRNM 519
Cdd:pfam05483 442 iflLQAREKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQED 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956785 520 LIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPD 592
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-361 |
8.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQqatdQRSNIRDNVETIKlhKQLVEKSN 280
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQ----IRGNGGDRLEQLE--REIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFS-ERRVEELQDRINDLEKERELLK 359
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
|
..
gi 568956785 360 EN 361
Cdd:COG4913 433 RR 434
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
715-789 |
1.84e-05 |
|
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: 44.75 E-value: 1.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956785 715 FCTTSLVD---HDTAIVPSSNDPQFDDHMCFPVPMNMdldrylkSESLSFYVFDDSDTQENIYMGKVNVPLISLAHDK 789
Cdd:cd00030 23 YVKVSLGGkqkFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRFSKDDFLGEVEIPLSELLDSG 93
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-413 |
4.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSysrvqARVNTGRRRASASAGSQEcpgkglRFQNVDEA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEAR------REELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 187 ETVQPTltkysnslLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQatDQRSNIRDNV 266
Cdd:PRK02224 324 EELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 267 ETikLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-QRL----KC--C--SLEKQLHSVRFS 337
Cdd:PRK02224 394 EE--LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaEALleagKCpeCgqPVEGSPHVETIE 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956785 338 ERR--VEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDlTDKTEVLDKLKTE 413
Cdd:PRK02224 472 EDRerVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERAEELRERAAE 548
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-410 |
7.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 112 IEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGsqecpgkglrfqnVDEAETVQP 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-------------IAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 192 TLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKEneielsllqlREQQATDQRSNIRDNVETIKL 271
Cdd:COG4913 679 RLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE----------EELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 272 HKQLveksnalsviEGKFIQLQEKQRTLRIShDALMANGDELNKQLKEQRLKccsLEKQLHsvRFSERRVEELQDRINDL 351
Cdd:COG4913 748 RALL----------EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMR--AFNREWPAETADLDADL 811
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 352 EKERELLKEnYDKLYNSAFsAAHEEQWK-LKEQQMKVQIAQLETALKSDLTDKTEVLDKL 410
Cdd:COG4913 812 ESLPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
148-405 |
8.39e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 148 TSYSRVQARVNTGRRRASASAGSQecpgkglRFQNVDEAETVqptltkySNSLLEEARGEIRNLE-NVIQSQRGQIEELE 226
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNE-------QQTNSKDGEQL-------SDFQLEDLVGMIQNAEkNILLLNQARLQALE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 227 HLAEIL--KTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHD 304
Cdd:PLN02939 157 DLEKILteKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 305 ALMANGDELNKQLKEqrlkccslekqlhsvrfserrVEELQDRINDLEKERELLKENYDKLyNSAFSAAHEEQWKLKEQQ 384
Cdd:PLN02939 237 LLKDDIQFLKAELIE---------------------VAETEERVFKLEKERSLLDASLREL-ESKFIVAQEDVSKLSPLQ 294
|
250 260
....*....|....*....|...
gi 568956785 385 MKVQIAQLET--ALKSDLTDKTE 405
Cdd:PLN02939 295 YDCWWEKVENlqDLLDRATNQVE 317
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
215-427 |
9.43e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 215 IQSQRGQIEELEHLAEILKTQLKRKENEIElSLLQLREQQATDQRSNIRDNVETIK-LHKQLVEKSNALSVIEGKFIQLQ 293
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIE-EQRKKNGENIARKQNKYDELVEEAKtIKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 294 EKQRTLRISHDALMANGDELNKQLK--EQRLKCCSLEKQLHSvrfSERRVEELQDRINDLEKERELLKENYDKL------ 365
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISE---GPDRITKIKDKLKELQHSLEKLDTAIDELeeimde 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 366 YNSAFSAAHEEQWKL--KEQQMKVQIAQLETA------LKSDLTDKTEVLDKLKTERGPLINQNEKLVQE 427
Cdd:PHA02562 332 FNEQSKKLLELKNKIstNKQSLITLVDKAKKVkaaieeLQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
34-360 |
1.85e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 34 RTVKTRQAVSRVSREELEdRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGggpkrLGRDVEMEEMie 113
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQE-RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA-----MERERELERI-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 114 QLQEKVHELER-QNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAEtvQPT 192
Cdd:pfam17380 354 RQEERKRELERiRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--QEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 193 LTKYSNSLLEEARGeiRNLENVIQSQrgqiEELEHLAEILKTQ-LKRKENEIELSLLQLREQQATDQRSNIRDNvETIKL 271
Cdd:pfam17380 432 ARQREVRRLEEERA--REMERVRLEE----QERQQQVERLRQQeEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 272 HKQLVEKSNALSVIEGkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccsLEKQLhsvrfseRRVEELQDRINDL 351
Cdd:pfam17380 505 KQAMIEEERKRKLLEK---EMEERQKAIYEEERRREAEEERRKQQEMEERRR---IQEQM-------RKATEERSRLEAM 571
|
....*....
gi 568956785 352 EKERELLKE 360
Cdd:pfam17380 572 EREREMMRQ 580
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
207-323 |
1.89e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLKRKENEIELSLLQLRE--QQATDQRSNIRDNVETIK-----LHKQLVE 277
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568956785 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLK 323
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| C2 |
pfam00168 |
C2 domain; |
725-797 |
2.40e-04 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 41.54 E-value: 2.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956785 725 TAIVPSSNDPQFDDHMCFPVPMNMDldrylksESLSFYVFDDSDTQENIYMGKVNVPLISLAHDKCISGIFEL 797
Cdd:pfam00168 39 TKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-424 |
2.78e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 193 LTKYSNS------LLEEARGEIRNLENVIQSQrGQIEELEHLAEILKTQLKRKENEIELSLLQLREqqatdQRSNIRDNV 266
Cdd:PRK03918 157 LDDYENAyknlgeVIKEIKRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELRE-----ELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 267 ETIKLHKQLVEKSN-ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-------------------------- 319
Cdd:PRK03918 231 KELEELKEEIEELEkELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyiklsefyeeyldelr 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 320 ----------QRLKccSLEKQLHSVRFSERRVEELQDRINDLEKERELLKEnYDKLYNSAfSAAHEEQWKLKEQQMKVQI 389
Cdd:PRK03918 311 eiekrlsrleEEIN--GIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEA-KAKKEELERLKKRLTGLTP 386
|
250 260 270
....*....|....*....|....*....|....*...
gi 568956785 390 AQLETALKSDLTDKTEV---LDKLKTERGPLINQNEKL 424
Cdd:PRK03918 387 EKLEKELEELEKAKEEIeeeISKITARIGELKKEIKEL 424
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-360 |
3.77e-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: 43.37 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQR--SNIRDNVETIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 276 VEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEqrlkccsLEKQLhsvrfsERRVEELQDRINDLEKER 355
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE-------KKAEL------DEELAELEAELEELEAER 165
|
....*
gi 568956785 356 ELLKE 360
Cdd:COG1579 166 EELAA 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-397 |
4.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 47 REELEDRFLRLhDENILLKQHARKQEDKIKRMATKLIR---LVNDKKRYErvggGPKRLGRDVEMEEMIEQLQEKVHELE 123
Cdd:TIGR02169 176 LEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREYE----GYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 124 RQNEVLKnRLISAKQQlqvqghrqtSYSRVQARVNTGRRRASASAGsqecpgkglrfqnvDEAETVQPTLtkysnsllEE 203
Cdd:TIGR02169 251 EELEKLT-EEISELEK---------RLEEIEQLLEELNKKIKDLGE--------------EEQLRVKEKI--------GE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA-----TDQRSNIRDNVETIKLHKQLVEK 278
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 279 SNALSVIEGKfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRF----SERRVEELQDRINDLEKE 354
Cdd:TIGR02169 379 EFAETRDELK--DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkineLEEEKEDKALEIKKQEWK 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568956785 355 RELLKENYDKlYNSAFSAAHEEQWKLKEQQMKVQ--IAQLETALK 397
Cdd:TIGR02169 457 LEQLAADLSK-YEQELYDLKEEYDRVEKELSKLQreLAEAEAQAR 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-427 |
4.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 48 EELEDRFLRLH------DENILLKQHARKQEDKIKRMATKLIRLvndkkrYERVGGGPKRLGRDVEMEEMIEQLQEKVHE 121
Cdd:PRK03918 276 EELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRL------EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 122 LERQNEVLKNRLisakqqlqvqghrqTSYSRVQARVNTGRRRASASAGsqECPGKGLRfqNVDEAETVQPTLTKYsnslL 201
Cdd:PRK03918 350 LEKRLEELEERH--------------ELYEEAKAKKEELERLKKRLTG--LTPEKLEK--ELEELEKAKEEIEEE----I 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 202 EEARGEIRNLENVIQSQRGQIEEL----------------EHLAEILK--------------------TQLKRKENEIEL 245
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteEHRKELLEeytaelkriekelkeieekeRKLRKELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 246 SLLQ----LREQQATDQRSNIRDNVETIKLHKqLVEKSNALSVIEGKFIQLQEKQRTLRIShdalMANGDELNKQLKEQR 321
Cdd:PRK03918 488 VLKKeselIKLKELAEQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 322 LKCCSLEKQLHSVrfsERRVEELQ-DRINDLEKERELLKENYDKlYNSAFSAAHEEQWKLKEQQmkvqiaqletALKSDL 400
Cdd:PRK03918 563 KKLDELEEELAEL---LKELEELGfESVEELEERLKELEPFYNE-YLELKDAEKELEREEKELK----------KLEEEL 628
|
410 420
....*....|....*....|....*..
gi 568956785 401 TDKTEVLDKLKTERGPLINQNEKLVQE 427
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-365 |
5.06e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELERQ 125
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAaNLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 126 NEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrfQNVDEAEtvqptltkysnSLLEEAR 205
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE--------EALALLR-----------SELEELS 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQatdqrsniRDNVETIKLHKQLVEKSnaLSVI 285
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY--------SLTLEEAEALENKIEDD--EEEA 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 286 EGKFIQLQEKQRTL-RISHDALmangDELnKQLKEqRLKccSLEKQLHSVrfsERRVEELQDRINDLEKE-RELLKENYD 363
Cdd:TIGR02168 971 RRRLKRLENKIKELgPVNLAAI----EEY-EELKE-RYD--FLTAQKEDL---TEAKETLEEAIEEIDREaRERFKDTFD 1039
|
..
gi 568956785 364 KL 365
Cdd:TIGR02168 1040 QV 1041
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-365 |
5.18e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIR---------NLENVIQSQRGQIEELEhlAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKL 271
Cdd:COG3206 191 LEEAEAALEefrqknglvDLSEEAKLLLQQLSELE--SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 272 HKQLVEKSNALSVIEGKF-------IQLQEKQRTLRISHDALMANG-DELNKQLKEQRLKCCSLEKQLHSVRFSERRVEE 343
Cdd:COG3206 269 RAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180
....*....|....*....|..
gi 568956785 344 LQDRINDLEKERELLKENYDKL 365
Cdd:COG3206 349 LEAELRRLEREVEVARELYESL 370
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-478 |
5.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 63 LLKQHARKQEDKI--KRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQL 140
Cdd:COG4717 46 MLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 141 QVQGHRQTsYSRVQARVNTGRRRAsASAGSQECPGKGLRFQ---NVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQS 217
Cdd:COG4717 126 QLLPLYQE-LEALEAELAELPERL-EELEERLEELRELEEEleeLEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 218 QRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQrsnIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQR 297
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 298 T-----------LRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSE--------------RRVEELQDRINDLE 352
Cdd:COG4717 281 LvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 353 KEREL--LKENYDKLYNSAFSAAHEE-----QWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERgpLINQNEKLV 425
Cdd:COG4717 361 EELQLeeLEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568956785 426 QENRDLQLQCLQQKQRLHELQSRLKffNQESDinaDDLSEALLLIKAQKEQKN 478
Cdd:COG4717 439 EELEELEEELEELREELAELEAELE--QLEED---GELAELLQELEELKAELR 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-576 |
1.20e-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: 42.44 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 368 SAFSAAHEEQWKLKEQ--QMKVQIAQLETALKSDLTDKTEVLDKLKTERGpLINQNEKLVQENRDLQLQCLQQKQrlhEL 445
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELA---EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 446 QSRLKFFNQESDINADDLSEalLLIKAQKEQKNGDLSFLEKVDS--------KINKDLDRSMKELQATHAETVQELEKTR 517
Cdd:COG4942 89 EKEIAELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956785 518 NMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI 576
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-568 |
1.50e-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: 42.85 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 209 RNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQAtdQRSNIRDNVEtiKLHKQLVEKSNALSVIEGK 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 289 FIQLQEKQRTLrishdalmanGDELN--KQLKEQRLKCCSLEKQLHSVRfsERRVEELQDRINDLEKERELLKENYDKLY 366
Cdd:pfam01576 287 RNKAEKQRRDL----------GEELEalKTELEDTLDTTAAQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKH 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 367 NSAFSAAHEEQwklkeQQMKVQIAQLETALKSdltdktevldkLKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHELQ 446
Cdd:pfam01576 355 TQALEELTEQL-----EQAKRNKANLEKAKQA-----------LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 447 SRLkffnQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQAThaetvQEL--EKTRNMLIMQH 524
Cdd:pfam01576 419 ARL----SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQKLNLST 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568956785 525 KINkdyQMEVETvTQKMENLQQDYELK--VEQYVHLLDIRAARIQK 568
Cdd:pfam01576 490 RLR---QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-573 |
2.03e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQnvDEA 186
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH--PNP 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 187 ETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEiELSLLQLReQQATDQRSNIRDNV 266
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCD-NRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 267 ETIK--LHKQLVEKSNALSVIEGKFIQLQEKQRTLRIS-HDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSERRVEE 343
Cdd:TIGR00618 594 VRLQdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 344 LQDRINDLEKERELLKEN--YDK-LYNSAFSAAHEEQWKLKEQQMKVQiaQLETALKSdltdktevldklkteRGPLINQ 420
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQltYWKeMLAQCQTLLRELETHIEEYDREFN--EIENASSS---------------LGSDLAA 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 421 NEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADD-LSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSM 499
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 500 KELQATHAETVQELEKTRNML----IMQHKINKDYQMEVETVTQKMENLQQDYEL-----KVEQY-VHLLDIRAARIQKL 569
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLeeksATLGEITHQLLKYEECSKQLAQLTQEQAKIiqlsdKLNGInQIKIQFDGDALIKF 896
|
....
gi 568956785 570 EAQL 573
Cdd:TIGR00618 897 LHEI 900
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-547 |
2.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 65 KQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNrlisAKQQLQVQG 144
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK----AEEAKKADE 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 145 HRQTSYSRVQARvnTGRRRASASAGSQECPGKGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEE 224
Cdd:PTZ00121 1449 AKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 225 LEHLAEILKTQLKRKENEIELS--LLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRIS 302
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 303 HDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSE----RRVEELQ--DRINDLEKERELLKENYDKLYNSAFSAAHEE 376
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEELKkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 377 QWKLKEQ-----QMKVQIAQLETALKSDLTdKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKf 451
Cdd:PTZ00121 1687 EKKAAEAlkkeaEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK- 1764
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 452 fnQESDINADDLSEALLLIKAQkeqkngdlsfLEKVDSKINKDLDRSMKELQaTHAETVQELEKTRNMLIMQHKINKDYQ 531
Cdd:PTZ00121 1765 --EEEKKAEEIRKEKEAVIEEE----------LDEEDEKRRMEVDKKIKDIF-DNFANIIEGGKEGNLVINDSKEMEDSA 1831
|
490
....*....|....*.
gi 568956785 532 MEVETVTQKMENLQQD 547
Cdd:PTZ00121 1832 IKEVADSKNMQLEEAD 1847
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
725-785 |
2.39e-03 |
|
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: 38.62 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956785 725 TAIVPSSNDPQFDDHMCFPVPmnmdldrYLKSESLSFYVFDDSDTQENIYMGKVNVPLISL 785
Cdd:smart00239 39 TKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKDRFGRDDFIGQVTIPLSDL 92
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
68-573 |
2.45e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 68 ARKQEDKIKRMATKLIRLVNDKKRYERVGGgpKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISaKQQLQVQGHRQ 147
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 148 TSYSRVQARVNtgrRRASASAGSQecpgkGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQrgQIEELEH 227
Cdd:TIGR00618 311 RIHTELQSKMR---SRAKLLMKRA-----AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 228 LAEI--LKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQLVEKSNALSVIEgKFIQLQEKQRTLRIS 302
Cdd:TIGR00618 381 IHTLqqQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaKKQQELQQRYAELCA-AAITCTAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 303 HDALMANG-DELNKQL--KEQRLKCCSLEKQLHSVRFSE-----------------------------RRVEELQDRIND 350
Cdd:TIGR00618 460 HLQESAQSlKEREQQLqtKEQIHLQETRKKAVVLARLLElqeepcplcgscihpnparqdidnpgpltRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 351 LEKERELLKENYDKLYNSAFSAAHEEQwklKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRd 430
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQ---EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 431 lqlqclqqkqrLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFlEKVDSKInkdldRSMKELQATHAETV 510
Cdd:TIGR00618 616 -----------ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ-ERVREHA-----LSIRVLPKELLASR 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956785 511 QELEKTrnmliMQHKInkdyqmevETVTQKMENLQQDYELKVEQYVHLLDIR----------AARIQKLEAQL 573
Cdd:TIGR00618 679 QLALQK-----MQSEK--------EQLTYWKEMLAQCQTLLRELETHIEEYDrefneienasSSLGSDLAARE 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-363 |
3.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQA---RVNTgrRRASASAGSQECPGKGLRFQNV 183
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDleeLIAE--RRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 184 D-EAETVQPTLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKtqlKRKENEIELSLLQLREQQATDQRSNI 262
Cdd:PRK02224 550 EaEAEEKREAAAE-AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA---AIADAEDEIERLREKREALAELNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 263 RDNVETIK-LHKQLVEKSNALSVIEGKfiqlQEKQRTlrishDALMANGDELNKQLKEQRlkcCSLEKQLHSVRFSERRV 341
Cdd:PRK02224 626 RERLAEKReRKRELEAEFDEARIEEAR----EDKERA-----EEYLEQVEEKLDELREER---DDLQAEIGAVENELEEL 693
|
250 260
....*....|....*....|..
gi 568956785 342 EELQDRINDLEKERELLKENYD 363
Cdd:PRK02224 694 EELRERREALENRVEALEALYD 715
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
107-376 |
3.44e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 107 EMEEMIEQLQE--KVH--ELERQNEVLKNRLISAKQqlqvqghrqtsySRVQARVNTGRRRASASAGSQECPGKgLRFQN 182
Cdd:PRK05771 17 YKDEVLEALHElgVVHieDLKEELSNERLRKLRSLL------------TKLSEALDKLRSYLPKLNPLREEKKK-VSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 183 VDEAEtvqptltKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKtqlKRKENEIELSLLQlreqqatdQRSNI 262
Cdd:PRK05771 84 LEELI-------KDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE---PWGNFDLDLSLLL--------GFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 263 RdnVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRtlrishDALMA-----NGDELNKQLKEQRLKccslEKQLHSVRFS 337
Cdd:PRK05771 146 S--VFVGTVPEDKLEELKLESDVENVEYISTDKGY------VYVVVvvlkeLSDEVEEELKKLGFE----RLELEEEGTP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568956785 338 ERRVEELQDRINDLEKERELLKE---NYDKLYNSAFSAAHEE 376
Cdd:PRK05771 214 SELIREIKEELEEIEKERESLLEelkELAKKYLEELLALYEY 255
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
207-407 |
4.79e-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: 39.50 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIelsllqlreQQATDQRSNIrdnvetiklhKQLVEKSNalsvie 286
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKENRLLKRLQKRQEKAL---------GKYEGTESEL----------PQLIARHN------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 287 gkfiqlqEKQRTLRISHDALMANGDELNKQLKE------------QRLKCCSLEKQLHSVRFSERRVEELQDRINDLEKE 354
Cdd:pfam15619 67 -------EEVRVLRERLRRLQEKERDLERKLKEkeaellrlrdqlKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956785 355 RELLkENYDKLYNSAFSAA-HEEQWKLKEQQMKVQIAQLE-TALKSDLTDKTEVL 407
Cdd:pfam15619 140 IQDL-ERKLELENKSFRRQlAAEKKKHKEAQEEVKILQEEiERLQQKLKEKEREL 193
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-573 |
4.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELERQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 127 EVLKNRLISAKQQLQVQGHRQtSYSRVQARVNTGRRRASASAGS-----QECPGKGLRFQNV-DEAETVQPTLT--KYSN 198
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGieeriKELEEKEERLEELkKKLKELEKRLEelEERH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 199 SLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLKRKEnEIELSLLQLREQQAT--DQRSNIRDNVETIKLHK--- 273
Cdd:PRK03918 362 ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIEELKKAKgkc 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 274 -------------QLVEKSNA-LSVIEGKFIQLQEKQRTLRishdalmANGDELNKQLKEQR--LKCCSLEKQLHSV--R 335
Cdd:PRK03918 439 pvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELAEQLKELeeK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 336 FSERRVEELQDRindlEKERELLKENYDKLyNSAFSAAHEEQWKLKEqqMKVQIAQLETALKSDLTDKTEVLDKLKTERG 415
Cdd:PRK03918 512 LKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAELLKELEELGF 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 416 PLINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDiNADDLSEALLLIKAQKEQKNGDLSFLEKV-DSKINKD 494
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKAFEELAETEKRLEELRKELEELEKKySEEEYEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 495 LDRSMKELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRA- 563
Cdd:PRK03918 664 LREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVKKYKALLKERAl 742
|
570
....*....|
gi 568956785 564 ARIQKLEAQL 573
Cdd:PRK03918 743 SKVGEIASEI 752
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-602 |
4.94e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 289 FIQLQEKQRT------LRISHDALMangDELNK-QLKEQRLKCCSLEKQLHSVrfsERRVEELQDRINDLEK----EREL 357
Cdd:PHA02562 144 FMQLSAPARRklvedlLDISVLSEM---DKLNKdKIRELNQQIQTLDMKIDHI---QQQIKTYNKNIEEQRKkngeNIAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 358 LKENYDKLYNSAfsaaheeqwklkeQQMKVQIAQLETALK---SDLTDKTEVLDKLKTERGPLINQNEKL---------- 424
Cdd:PHA02562 218 KQNKYDELVEEA-------------KTIKAEIEELTDELLnlvMDIEDPSAALNKLNTAAAKIKSKIEQFqkvikmyekg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 425 ------VQENRDLQLQCLQQKQRLHELQSRLKFFN------QESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiN 492
Cdd:PHA02562 285 gvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDtaidelEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK----A 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 493 KDLDRSMKELQATHAETVQELEKTRNMLImqhKINKDYQmevETVTQKME-----NLQQDYELKveqyvhlldiraARIQ 567
Cdd:PHA02562 361 KKVKAAIEELQAEFVDNAEELAKLQDELD---KIVKTKS---ELVKEKYHrgivtDLLKDSGIK------------ASII 422
|
330 340 350
....*....|....*....|....*....|....*....
gi 568956785 568 KleaqlKDIAYGTKQYKFKPEIMPDDSV----DEFDETI 602
Cdd:PHA02562 423 K-----KYIPYFNKQINHYLQIMEADYNftldEEFNETI 456
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-410 |
5.98e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 221 QIEELEHLAEILKTQLKRKENEIElsllqlreqQATDQRSNIRDNVETIKlhKQLVEKSNALSVIEGKFIQLQEKQRTLR 300
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELA---------ALEARLEAAKTELEDLE--KEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 301 ishdalmaNGDELNkqlkeqrlkccSLEKQLHSVrfsERRVEELQDRINDLEKERELLKENYDKLynSAFSAAHEEQWKL 380
Cdd:COG1579 87 --------NNKEYE-----------ALQKEIESL---KRRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEE 142
|
170 180 190
....*....|....*....|....*....|
gi 568956785 381 KEQQMKVQIAQLETALKSDLTDKTEVLDKL 410
Cdd:COG1579 143 KKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
192-554 |
7.61e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 192 TLTKYSNSLLEEARGEIRNLEN---VIQSQRGQIEELEHLAEILKtQLKRKENEIELSLL---QLREQQATDQRSNIRDN 265
Cdd:COG5185 212 TGNLGSESTLLEKAKEIINIEEalkGFQDPESELEDLAQTSDKLE-KLVEQNTDLRLEKLgenAESSKRLNENANNLIKQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 266 VETiklHKQLVEKSNALSVIEGKFIQLQE--KQRTLRISHDALMANGDELNKQLKEQRLKCC-SLEKQLHSVR------F 336
Cdd:COG5185 291 FEN---TKEKIAEYTKSIDIKKATESLEEqlAAAEAEQELEESKRETETGIQNLTAEIEQGQeSLTENLEAIKeeieniV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 337 SERRVEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLkEQQMKVQIAQLETaLKSDLTDKTEVLDKLKTERGP 416
Cdd:COG5185 368 GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATL-EDTLKAADRQIEE-LQRQIEQATSSNEEVSKLLNE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 417 LINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINadDLSEALLLIKAQKEQKNGDLSF-LEKVDSKINKDL 495
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELT--QIESRVSTLKATLEKLRAKLERqLEGVRSKLDQVA 523
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956785 496 DRSMKELQATHAETVQELEKTRNMLIMQHKINK--DYQMEVETVTQKMENLQQDYELKVEQ 554
Cdd:COG5185 524 ESLKDFMRARGYAHILALENLIPASELIQASNAktDGQAANLRTAVIDELTQYLSTIESQQ 584
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-414 |
7.65e-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: 40.42 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 108 MEEMIEQLQEKVHE------LERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARvntgrrraSASAGSQECPGKGLRFQ 181
Cdd:TIGR00606 617 KEEQLSSYEDKLFDvcgsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ--------LTDENQSCCPVCQRVFQ 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 182 NVDEAETVQPTLtkysNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQR-- 259
Cdd:TIGR00606 689 TEAELQEFISDL----QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlk 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 260 SNIRDN---VETIKLHKQLVEKSNA-LSVIEGKFIQLQEKQRtlRISHDALMANGDELNKQLKEQRLKccsLEKQLHSVR 335
Cdd:TIGR00606 765 NDIEEQetlLGTIMPEEESAKVCLTdVTIMERFQMELKDVER--KIAQQAAKLQGSDLDRTVQQVNQE---KQEKQHELD 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 336 FSERRVEELQDRINDLEKERELLKENYDKL--------YNSAFSAAHEEQW--KLKE--------QQMKVQIAQLETALK 397
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELkseklqigTNLQRRQQFEEQLveLSTEvqslireiKDAKEQDSPLETFLE 919
|
330
....*....|....*..
gi 568956785 398 SDLTDKTEVLDKLKTER 414
Cdd:TIGR00606 920 KDQQEKEELISSKETSN 936
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-364 |
8.33e-03 |
|
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: 40.19 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 208 IRNLENVIQSQRGQIEELEHLAEILKTQ--------------LKRKENEIElsllQLREQQATDQRSNiRDNVETI-KLH 272
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKERIIE----RLKEQREREDRER-LEELESLkKEN 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 273 KQLVEKSNALSVI----EGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQL---HSVRFSERRVEELQ 345
Cdd:pfam10174 478 KDLKEKVSALQPEltekESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEIN 557
|
170
....*....|....*....
gi 568956785 346 DRINDLEKERELLKENYDK 364
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGK 576
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-405 |
9.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRsNIRDNVETIKLH-KQLVEKS 279
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID----KLQAEIAEAEA-EIEERREELGERaRALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956785 280 NALSVIE--------GKFIqlqekQRTLRIShdALMANGDELNKQLKEQRLKccsLEKQLHSVRFSERRVEELQDRINDL 351
Cdd:COG3883 100 GSVSYLDvllgsesfSDFL-----DRLSALS--KIADADADLLEELKADKAE---LEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956785 352 EKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTE 405
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| |
