#=GF ID   pRN1_helical
#=GF AC   PF13010.10
#=GF DE   Primase helical domain
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF SE   Jackhmmer:Q54324.1
#=GF GA   27.00 27.00;
#=GF TC   28.70 68.10;
#=GF NC   22.40 20.30;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF RN   [1]
#=GF RM   20511586
#=GF RT   The archaeo-eukaryotic primase of plasmid pRN1 requires a helix
#=GF RT   bundle domain for faithful primer synthesis.
#=GF RA   Beck K, Vannini A, Cramer P, Lipps G;
#=GF RL   Nucleic Acids Res. 2010; [Epub ahead of print]
#=GF DR   INTERPRO; IPR024966;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This alpha helical domain is found in a set of bacterial plasmid
#=GF CC   replication proteins [1]. The domain is found to the C-terminus
#=GF CC   of the primase/polymerase domain. Mutants of this domain are
#=GF CC   defective in template binding, dinucleotide formation and
#=GF CC   conformation change prior to DNA extension [1].
#=GF SQ   3
#=GS Q973E3_SULTO/215-350  AC Q973E3.1
#=GS Q980Y0_SACS2/217-347  AC Q980Y0.1
#=GS Q975W1_SULTO/199-329  AC Q975W1.1
Q973E3_SULTO/215-350             ...........VKKED--EKLEKLKEEMAKYDRFKGKTVEAIREEVCKEISKELEELKGKDDKKSKKWSAILTTAESAVCEGKTYAEIGIDRSRGDWAFYYVLFSHGATNLDVLEQLLPSDSKVF.APKWD..KYYVHTVKKVWEKVKPLLE
Q980Y0_SACS2/217-347             ...........NKKSDTEEDFEKLKEEMRKYDRYRGKTLDAIRDELCKAIKKKIEHA----EEKAKE---TLNIAKGVLCDKKTYADIGIDRSRGDWHLLNFLLSHGATDLDVVMQLLPEDSKVF.EPKWD..KYTFHTVAKIWERVKPWLT
Q975W1_SULTO/199-329             rgviewlgdrk--------------EELKAEDKHYEE---FIAELKKKNKFKSVEEAKNKICGKLKH----SSLEYKVICEGKTYADVGIDRSRGDFRVIKTSLYHGLRDPDLILQVLPEDSKAKnNEKWDsrKYFLITLKNAWSVVSKYLE
#=GC seq_cons                    ...........sKKpD..EchEKLKEEM+KYDRa+GKTl-AIREElCKsIpKclEEAKsK.-cKuK+...hLolAcuVlCEGKTYADIGIDRSRGDW+llpsLLSHGATDLDVlhQLLPEDSKVF.sPKWD..KYalHTVKKlWE+VKPaLE
//